changeset 0:e8d7b7dc55fc draft

"planemo upload for repository https://github.com/galaxyproteomics/tools-galaxyp/tree/master/tools/metamorpheus commit 7a40b99b4124b0c032a16067741fd55a60b48cb0-dirty"

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/macros.xml	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,713 @@
+<macros>
+    <token name="@PROFILE@">21.01</token>
+    <token name="@TOOL_VERSION@">0.0.316</token>
+    <token name="@VERSION_SUFFIX@">0</token>
+    <xml name="requirements">
+        <requirements>
+            <requirement type="package" version="@TOOL_VERSION@">metamorpheus</requirement>
+            <yield/>
+        </requirements>
+    </xml>
+
+    <token name="@DEFAULT_COMMON_TOML@">
+[CommonParameters]
+# MaxThreadsToUsePerFile = 11
+ListOfModsFixed = "Common Fixed\tCarbamidomethyl on C\t\tCommon Fixed\tCarbamidomethyl on U"
+ListOfModsVariable = "Common Variable\tOxidation on M"
+DoPrecursorDeconvolution = true # Calibration false
+UseProvidedPrecursorInfo = true
+DeconvolutionIntensityRatio = 3.0
+DeconvolutionMaxAssumedChargeState = 12
+DeconvolutionMassTolerance = "±4.0000 PPM"
+TotalPartitions = 1
+ProductMassTolerance = "±20.0000 PPM" # Calibration 25.0000
+PrecursorMassTolerance = "±5.0000 PPM" # Calibration 15.0000
+AddCompIons = false
+ScoreCutoff = 5.0
+ReportAllAmbiguity = true
+NumberOfPeaksToKeepPerWindow = 200
+MinimumAllowedIntensityRatioToBasePeak = 0.01
+NormalizePeaksAccrossAllWindows = false
+TrimMs1Peaks = false
+TrimMsMsPeaks = true # Calibration false
+UseDeltaScore = false
+QValueOutputFilter = 1.0
+CustomIons = []
+AssumeOrphanPeaksAreZ1Fragments = true
+MaxHeterozygousVariants = 4
+MinVariantDepth = 1
+DissociationType = "HCD"
+SeparationType = "HPLC"
+MS2ChildScanDissociationType = "Unknown"
+MS3ChildScanDissociationType = "Unknown"
+</token>
+
+    <token name="@DEFAULT_DIGESTION_TOML@">
+[CommonParameters.DigestionParams]
+MaxMissedCleavages = 2
+InitiatorMethionineBehavior = "Variable"
+MinPeptideLength = 7
+MaxPeptideLength = 2147483647
+MaxModificationIsoforms = 1024
+MaxModsForPeptide = 2
+Protease = "trypsin"
+SearchModeType = "Full"
+FragmentationTerminus = "Both"
+SpecificProtease = "trypsin"
+GeneratehUnlabeledProteinsForSilac = true
+</token>
+
+    <token name="@DEFAULT_CALIBRATION_TOML@"><![CDATA[
+TaskType = "Calibrate"
+
+[CalibrationParameters]
+WriteIntermediateFiles = false
+WriteIndexedMzml = true
+MinMS1IsotopicPeaksNeededForConfirmedIdentification = 3
+MinMS2IsotopicPeaksNeededForConfirmedIdentification = 2
+NumFragmentsNeededForEveryIdentification = 10
+
+[CommonParameters]
+MaxThreadsToUsePerFile = 11
+ListOfModsFixed = "Common Fixed\tCarbamidomethyl on C\t\tCommon Fixed\tCarbamidomethyl on U"
+ListOfModsVariable = "Common Variable\tOxidation on M"
+DoPrecursorDeconvolution = false
+UseProvidedPrecursorInfo = true
+DeconvolutionIntensityRatio = 3.0
+DeconvolutionMaxAssumedChargeState = 12
+DeconvolutionMassTolerance = "±4.0000 PPM"
+TotalPartitions = 1
+ProductMassTolerance = "±25.0000 PPM"
+PrecursorMassTolerance = "±15.0000 PPM"
+AddCompIons = false
+ScoreCutoff = 5.0
+ReportAllAmbiguity = true
+NumberOfPeaksToKeepPerWindow = 200
+MinimumAllowedIntensityRatioToBasePeak = 0.01
+NormalizePeaksAccrossAllWindows = false
+TrimMs1Peaks = false
+TrimMsMsPeaks = false
+UseDeltaScore = false
+QValueOutputFilter = 1.0
+CustomIons = []
+AssumeOrphanPeaksAreZ1Fragments = true
+MaxHeterozygousVariants = 4
+MinVariantDepth = 1
+DissociationType = "HCD"
+SeparationType = "HPLC"
+MS2ChildScanDissociationType = "Unknown"
+MS3ChildScanDissociationType = "Unknown"
+
+@DEFAULT_DIGESTION_TOML@
+]]></token>
+
+    <token name="@DEFAULT_GPTMD_TOML@"><![CDATA[
+TaskType = "Gptmd"
+
+[GptmdParameters]
+ListOfModsGptmd = "Common Biological\tAcetylation on K\t\tCommon Biological\tAcetylation on X\t\tCommon Biological\tADP-ribosylation on S\t\tCommon Artifact\tAmmonia loss on C\t\tCommon Artifact\tAmmonia loss on N\t\tCommon Biological\tButyrylation on K\t\tMetal\tCalcium on D\t\tMetal\tCalcium on E\t\tCommon Artifact\tCarbamyl on C\t\tCommon Artifact\tCarbamyl on K\t\tCommon Artifact\tCarbamyl on M\t\tCommon Artifact\tCarbamyl on R\t\tCommon Artifact\tCarbamyl on X\t\tCommon Biological\tCarboxylation on D\t\tCommon Biological\tCarboxylation on E\t\tCommon Biological\tCarboxylation on K\t\tCommon Biological\tCitrullination on R\t\tCommon Biological\tCrotonylation on K\t\tMetal\tCu[I] on D\t\tMetal\tCu[I] on E\t\tCommon Artifact\tDeamidation on N\t\tCommon Artifact\tDeamidation on Q\t\tCommon Biological\tDimethylation on K\t\tCommon Biological\tDimethylation on R\t\tMetal\tFe[II] on D\t\tMetal\tFe[II] on E\t\tMetal\tFe[III] on D\t\tMetal\tFe[III] on E\t\tCommon Biological\tFormylation on K\t\tCommon Biological\tGlu to PyroGlu on Q\t\tCommon Biological\tGlutarylation on K\t\tCommon Biological\tHexNAc on Nxs\t\tCommon Biological\tHexNAc on Nxt\t\tCommon Biological\tHexNAc on S\t\tCommon Biological\tHexNAc on T\t\tCommon Biological\tHydroxybutyrylation on K\t\tCommon Biological\tHydroxylation on K\t\tCommon Biological\tHydroxylation on N\t\tCommon Biological\tHydroxylation on P\t\tMetal\tMagnesium on D\t\tMetal\tMagnesium on E\t\tCommon Biological\tMalonylation on K\t\tCommon Biological\tMethylation on K\t\tCommon Biological\tMethylation on R\t\tCommon Biological\tNitrosylation on C\t\tCommon Biological\tNitrosylation on Y\t\tCommon Biological\tPhosphorylation on S\t\tCommon Biological\tPhosphorylation on T\t\tCommon Biological\tPhosphorylation on Y\t\tMetal\tPotassium on D\t\tMetal\tPotassium on E\t\tCommon Biological\tPyridoxal phosphate on K\t\tMetal\tSodium on D\t\tMetal\tSodium on E\t\tCommon Biological\tSuccinylation on K\t\tCommon Biological\tSulfonation on Y\t\tCommon Biological\tTrimethylation on K\t\tCommon Artifact\tWater Loss on E\t\tMetal\tZinc on D\t\tMetal\tZinc on E"
+
+@DEFAULT_COMMON_TOML@
+
+@DEFAULT_DIGESTION_TOML@
+]]></token>
+
+    <token name="@DEFAULT_SEARCH_TOML@"><![CDATA[
+TaskType = "Search"
+
+[SearchParameters]
+DisposeOfFileWhenDone = true
+DoParsimony = true
+ModPeptidesAreDifferent = false
+NoOneHitWonders = false
+MatchBetweenRuns = false
+Normalize = false
+QuantifyPpmTol = 5.0
+DoHistogramAnalysis = false
+SearchTarget = true
+DecoyType = "Reverse"
+MassDiffAcceptorType = "OneMM"
+WritePrunedDatabase = false
+KeepAllUniprotMods = true
+DoLocalizationAnalysis = true
+DoQuantification = true
+SearchType = "Classic"
+LocalFdrCategories = ["FullySpecific"]
+MaxFragmentSize = 30000.0
+HistogramBinTolInDaltons = 0.003
+MaximumMassThatFragmentIonScoreIsDoubled = 0.0
+WriteMzId = true
+WritePepXml = false
+WriteDecoys = true
+WriteContaminants = true
+WriteIndividualFiles = true
+CompressIndividualFiles = false
+TCAmbiguity = "RemoveContaminant"
+
+[SearchParameters.ModsToWriteSelection]
+'N-linked glycosylation' = 3
+'O-linked glycosylation' = 3
+'Other glycosylation' = 3
+'Common Biological' = 3
+'Less Common' = 3
+Metal = 3
+'2+ nucleotide substitution' = 3
+'1 nucleotide substitution' = 3
+UniProt = 2
+
+@DEFAULT_COMMON_TOML@
+
+@DEFAULT_DIGESTION_TOML@
+]]></token>
+
+    <xml name="input_spectrums" token_multiple="false" token_filetype="Spectrum">
+        <param name="spectrums" type="data" format="mzml" multiple="@MULTIPLE@" label="MS/MS @FILETYPE@ files"/>
+    </xml>
+    <xml name="calib_toml">
+        <param name="calib_tomls" type="data" format="toml" multiple="true" optional="true" label="Calibrated Spectrum TOML files"/>
+    </xml>
+    <xml name="input_databases">
+        <param name="databases" type="data" format="uniprotxml,fasta" multiple="true" label="Reference Protein Databases"/>
+    </xml>
+    <xml name="input_toml">
+        <param name="input_toml" type="data" format="toml" optional="true" label="Optional Config toml from history"/>
+    </xml>
+    <token name="@CMD_IMPORTS@">
+#import re
+#def identifier_or_name($input1)
+    #if hasattr($input1, 'element_identifier')
+        #return $input1.element_identifier
+    #else
+        #return $input1.name
+    #end if
+#end def
+#def clean($name1)
+    #set $name_clean = $re.sub('[^\w\-_]', '_', $re.sub('(?i)[.](fa|fasta|xml|imzml|mzml|raw|mgf)$','', $re.sub('.*/','', $name1.rstrip('.gz'))))
+    #return $name_clean
+#end def
+#def ln_name($ds)
+    #set $ext = ''
+    #if $ds.is_of_type('mzml') or $ds.is_of_type('imzml')
+        #set $ext = ".mzML"
+    #else if $ds.is_of_type('thermo.raw')
+        #set $ext = ".raw"
+    #else if $ds.is_of_type('toml')
+        #set $ext = ".toml"
+    #else if $ds.is_of_type('uniprotxml')
+        #set $ext = ".xml"
+    #else if $ds.is_of_type('fasta')
+        #set $ext = ".fasta"
+    #end if
+    #set $name = "%s%s" % ($clean($identifier_or_name($ds)),$ext)
+    #return $name
+#end def
+    </token>
+
+    <token name="@PREPARE_INPUTS@"><![CDATA[
+    @CMD_IMPORTS@
+    #set $spectrum_names = []
+    #set $database_names = []
+    #set $inputs_dir = 'inputs'
+    mkdir -p $inputs_dir &&
+    #for $sf in $spectrums
+      #set $i_name = $ln_name($sf)
+      $spectrum_names.append($i_name)
+      ln -s '${sf}' '${inputs_dir}/${i_name}' &&
+    #end for
+    #for $db in $databases
+      #set $d_name = $ln_name($db)
+      $database_names.append($d_name)
+      ln -s '${db}' '${d_name}' &&
+    #end for
+]]></token>
+    <token name="@LN_CALIB_TOML@"><![CDATA[
+    #for $tf in $calib_tomls
+      #set $t_name = $ln_name($tf)
+      ln -s '${tf}' '${inputs_dir}/${t_name}' &&
+    #end for
+]]></token>
+    
+    <token name="@MERGE_TOMLS@"><![CDATA[
+#def merge_tomls($tomls, $merged):
+    #import re
+    #set $config = dict()
+    #set $config['categories'] = []
+    #set $category = ' ' 
+    #for $toml in $tomls
+        #set $fh = open(toml,'r')
+        #for $line in $fh:
+            #set $entry = $line.rstrip()
+            #if $entry.strip() == '':
+                #continue
+            #end if
+            #set $m = $re.match('^((TaskType)\s*=\s*(.*))$', $entry)
+            #if $m:
+                #if $m.groups()[0] not in $config:
+                    #set $config['TaskType'] = $entry
+                    #continue
+                #end if 
+            #end if
+            #set $m = $re.match('^(\[.+\])$', $entry)
+            #if $m:
+                #set $category = $m.groups()[0]
+                #if $category not in $config['categories']:
+                    $config['categories'].append($category)
+                    #set $config[$category] = []
+                    #continue
+                #end if
+            #end if
+            #set $m = $re.match('^(\S+)\s*=\s*(.*)$',$entry)
+            #if $m:
+                #set $pname = $m.groups()[0]
+                #set $pval = $m.groups()[1]
+                #if $pname not in $config[$category]:
+                    $config[$category].append($pname)
+                #end if
+                #set $config[$pname] = $pval
+            #end if
+#*
+*#
+        #end for
+        $fh.close()
+    #end for
+    #set $wfh = open($merged,'w')
+    #if 'TaskType' in $config:
+        #silent $wfh.write('%s\n' % $config['TaskType'])
+    #end if
+    #for $category in $config['categories']:
+        #silent $wfh.write('\n')
+        #silent $wfh.write('%s\n' % $category)
+        #for $pname in $config[$category]:
+            #set $pval = $config[$pname]
+            #silent $wfh.write('%s = %s\n' % ($pname, $pval))
+        #end for
+    #end for
+    $wfh.close()
+#*
+*#
+#*
+    #echo $config 
+*#
+#end def
+#if $input_toml 
+    $merge_tomls([$default_toml,str($input_toml),$user_toml], $task_settings_toml)
+#else
+    $merge_tomls([$default_toml,$user_toml], $task_settings_toml)
+#end if
+ln -s '$task_settings_toml' tasksettings.toml &&
+
+]]></token>
+
+    <xml name="calibrate_params">
+        <conditional name="calibration">
+            <param name="set_calibration" type="select" label="Set Calibration Parameters">
+                <option value="no">no</option>
+                <option value="yes">yes</option>
+            </param>
+            <when value="no"/>
+            <when value="yes">
+                <param argument="MinMS1IsotopicPeaksNeededForConfirmedIdentification" type="integer" value="3" label="MinMS1IsotopicPeaksNeededForConfirmedIdentification"/>
+                <param argument="MinMS2IsotopicPeaksNeededForConfirmedIdentification" type="integer" value="2" label="MinMS2IsotopicPeaksNeededForConfirmedIdentification"/>
+                <param argument="NumFragmentsNeededForEveryIdentification" type="integer" value="10" label="NumFragmentsNeededForEveryIdentification"/>
+            </when>
+        </conditional>
+    </xml>
+    <token name="@CALIBRATE_CONFIG@"><![CDATA[
+#if $calibration.set_calibration == 'yes'
+[CalibrationParameters]
+WriteIntermediateFiles = false
+MinMS1IsotopicPeaksNeededForConfirmedIdentification = $calibration.MinMS1IsotopicPeaksNeededForConfirmedIdentification
+MinMS2IsotopicPeaksNeededForConfirmedIdentification = $calibration.MinMS2IsotopicPeaksNeededForConfirmedIdentification
+NumFragmentsNeededForEveryIdentification = $calibration.NumFragmentsNeededForEveryIdentification
+#end if
+]]></token>
+    <xml name="gptmd_params">
+
+    </xml>
+    <token name="@GPTMD_CONFIG@">
+TaskType = "Gptmd"
+
+[GptmdParameters]
+ListOfModsGptmd = "Common Biological\tAcetylation on K\t\tCommon Biological\tAcetylation on X\t\tCommon Biological\tADP-ribosylation on S\t\tCommon Biological\tButyrylation on K\t\tCommon Biological\tCarboxylation on D\t\tCommon Biological\tCarboxylation on E\t\tCommon Biological\tCarboxylation on K\t\tCommon Biological\tCitrullination on R\t\tCommon Biological\tCrotonylation on K\t\tCommon Biological\tDimethylation on K\t\tCommon Biological\tDimethylation on R\t\tCommon Biological\tFormylation on K\t\tCommon Biological\tGlu to PyroGlu on Q\t\tCommon Biological\tGlutarylation on K\t\tCommon Biological\tHexNAc on Nxs\t\tCommon Biological\tHexNAc on Nxt\t\tCommon Biological\tHexNAc on S\t\tCommon Biological\tHexNAc on T\t\tCommon Biological\tHydroxybutyrylation on K\t\tCommon Biological\tHydroxylation on K\t\tCommon Biological\tHydroxylation on N\t\tCommon Biological\tHydroxylation on P\t\tCommon Biological\tMalonylation on K\t\tCommon Biological\tMethylation on K\t\tCommon Biological\tMethylation on R\t\tCommon Biological\tNitrosylation on C\t\tCommon Biological\tNitrosylation on Y\t\tCommon Biological\tPhosphorylation on S\t\tCommon Biological\tPhosphorylation on T\t\tCommon Biological\tPhosphorylation on Y\t\tCommon Biological\tPyridoxal phosphate on K\t\tCommon Biological\tSuccinylation on K\t\tCommon Biological\tSulfonation on Y\t\tCommon Biological\tTrimethylation on K\t\tCommon Artifact\tAmmonia loss on C\t\tCommon Artifact\tAmmonia loss on N\t\tCommon Artifact\tCarbamyl on C\t\tCommon Artifact\tCarbamyl on K\t\tCommon Artifact\tCarbamyl on M\t\tCommon Artifact\tCarbamyl on R\t\tCommon Artifact\tCarbamyl on X\t\tCommon Artifact\tDeamidation on N\t\tCommon Artifact\tDeamidation on Q\t\tCommon Artifact\tWater Loss on E\t\tMetal\tCalcium on D\t\tMetal\tCalcium on E\t\tMetal\tCu[I] on D\t\tMetal\tCu[I] on E\t\tMetal\tFe[II] on D\t\tMetal\tFe[II] on E\t\tMetal\tFe[III] on D\t\tMetal\tFe[III] on E\t\tMetal\tMagnesium on D\t\tMetal\tMagnesium on E\t\tMetal\tPotassium on D\t\tMetal\tPotassium on E\t\tMetal\tSodium on D\t\tMetal\tSodium on E\t\tMetal\tZinc on D\t\tMetal\tZinc on E"
+    </token>
+
+    <xml name="search_params">
+        <conditional name="search_params">
+            <param name="set_search_params" type="select" label="Set Search Parameters">
+                <option value="no">no</option>
+                <option value="yes">yes</option>
+            </param>
+            <when value="no"/>
+            <when value="yes">
+                <param argument="DoParsimony" type="boolean" truevalue="true" falsevalue="false" checked="true" label="DoParsimony"/>
+                <param argument="ModPeptidesAreDifferent" type="boolean" truevalue="true" falsevalue="false" checked="false" label="ModPeptidesAreDifferent"/>
+                <param argument="NoOneHitWonders" type="boolean" truevalue="true" falsevalue="false" checked="false" label="NoOneHitWonders"/>
+                <param argument="MatchBetweenRuns" type="boolean" truevalue="true" falsevalue="false" checked="false" label="MatchBetweenRuns"/>
+                <param argument="Normalize" type="boolean" truevalue="true" falsevalue="false" checked="false" label="Normalize"/>
+                <param argument="QuantifyPpmTol" type="float" value="5.0" label="QuantifyPpmTol"/>
+                <param argument="DoHistogramAnalysis" type="boolean" truevalue="true" falsevalue="false" checked="false" label="DoHistogramAnalysis"/>
+                <param argument="SearchTarget" type="boolean" truevalue="true" falsevalue="false" checked="true" label="SearchTarget"/>
+                <param argument="DecoyType" type="select" label="DecoyType">
+                    <option value="Reverse" selected="true">Reverse</option>
+                    <option value="Slide">Slide</option>
+                    <option value="None">None</option>
+                </param>
+                <param argument="MassDiffAcceptorType" type="select" label="MassDiffAcceptorType">
+                    <option value="Exact">Exact</option>
+                    <option value="OneMM" selected="true">OneMM</option>
+                    <option value="TwoMM">TwoMM</option>
+                    <option value="ThreeMM">ThreeMM</option>
+                    <option value="PlusOrMinusThreeMM">PlusOrMinusThreeMM</option>
+                    <option value="ModOpen">ModOpen</option>
+                    <option value="Open">Open</option>
+                </param>
+                <param argument="KeepAllUniprotMods" type="boolean" truevalue="true" falsevalue="false" checked="true" label="KeepAllUniprotMods"/>
+                <param argument="DoLocalizationAnalysis" type="boolean" truevalue="true" falsevalue="false" checked="true" label="DoLocalizationAnalysis"/>
+                <param argument="DoQuantification" type="boolean" truevalue="true" falsevalue="false" checked="true" label="DoQuantification"/>
+                <param argument="SearchType" type="select" label="SearchType">
+                    <option value="Classic" selected="true">Classic</option>
+                    <option value="Modern">Modern</option>
+                    <option value="NonSpecific">NonSpecific</option>
+                </param>
+                <param argument="LocalFdrCategories" type="select" label="LocalFdrCategories">
+                    <option value="FullySpecific" selected="true">FullySpecific</option>
+                    <option value="SemiSpecific">SemiSpecific</option>
+                    <option value="NonSpecific">NonSpecific</option>
+                </param>
+                <param argument="MaxFragmentSize" type="float" value="30000.0" label="MaxFragmentSize"/>
+                <param argument="HistogramBinTolInDaltons" type="float" value="0.003" label="HistogramBinTolInDaltons"/>
+                <param argument="MaximumMassThatFragmentIonScoreIsDoubled" type="float" value="0.0" label="MaximumMassThatFragmentIonScoreIsDoubled"/>
+            </when>
+        </conditional>
+        <param name="search_outputs" type="select" multiple="true" label="Select Optional Search Outputs">
+            <option value="WriteMzId" selected="true">WriteMzId</option>
+            <option value="WritePepXml" selected="false">WritePepXml</option>
+            <option value="WritePrunedDatabase" selected="true">WritePrunedDatabase</option>
+            <option value="WriteDecoys" selected="false">WriteDecoys</option>
+            <option value="WriteContaminants" selected="false">WriteContaminants</option>
+        </param> 
+    </xml>
+    <token name="@SEARCH_CONFIG@"><![CDATA[
+[SearchParameters]
+#if $search_params.set_search_params == 'yes'
+DisposeOfFileWhenDone = true
+DoParsimony = $search_params.DoParsimony
+ModPeptidesAreDifferent = $search_params.ModPeptidesAreDifferent
+NoOneHitWonders = $search_params.NoOneHitWonders
+MatchBetweenRuns = $search_params.MatchBetweenRuns
+Normalize = $search_params.Normalize
+QuantifyPpmTol = $search_params.QuantifyPpmTol
+DoHistogramAnalysis = $search_params.DoHistogramAnalysis
+SearchTarget = $search_params.SearchTarget
+DecoyType = "$search_params.DecoyType"
+MassDiffAcceptorType = "$search_params.MassDiffAcceptorType"
+KeepAllUniprotMods = $search_params.KeepAllUniprotMods
+DoLocalizationAnalysis = $search_params.DoLocalizationAnalysis
+DoQuantification = $search_params.DoQuantification
+SearchType = "$search_params.SearchType"
+LocalFdrCategories = ["$search_params.LocalFdrCategories"]
+MaxFragmentSize = $search_params.MaxFragmentSize
+HistogramBinTolInDaltons = $search_params.HistogramBinTolInDaltons
+MaximumMassThatFragmentIonScoreIsDoubled = $search_params.MaximumMassThatFragmentIonScoreIsDoubled
+#end if
+WritePrunedDatabase = #echo str('WritePrunedDatabase' in $search_outputs).lower()
+WriteMzId = #echo str('WriteMzId' in $search_outputs).lower()
+WritePepXml = #echo str('WritePepXml' in $search_outputs).lower()
+WritePepXml = #echo str('WritePepXml' in $search_outputs).lower()
+WriteDecoys = #echo str('WriteDecoys' in $search_outputs).lower()
+WriteContaminants = #echo str('WriteContaminants' in $search_outputs).lower()
+
+[SearchParameters.ModsToWriteSelection]
+'N-linked glycosylation' = 3
+'O-linked glycosylation' = 3
+'Other glycosylation' = 3
+'Common Biological' = 3
+'Less Common' = 3
+Metal = 3
+'2+ nucleotide substitution' = 3
+'1 nucleotide substitution' = 3
+UniProt = 2
+]]></token>
+
+    <xml name="dissociation_options">
+                    <option value="Any">Any</option>
+                    <option value="CID">CID</option>
+                    <option value="LowCID">LowCID</option>
+                    <option value="ISCID">ISCID</option>
+                    <option value="MPD">MPD</option>
+                    <option value="ECD">ECD</option>
+                    <option value="PQD">PQD</option>
+                    <option value="ETD">ETD</option>
+                    <option value="HCD" selected="true">HCD</option>
+                    <option value="EThcD">EThcD</option>
+                    <option value="Custom">Custom</option>
+    </xml>
+
+    <xml name="common_params">
+        <conditional name="common">
+            <param name="set_common" type="select" label="Set Common Parameters">
+                <option value="no">no</option>
+                <option value="yes">yes</option>
+            </param>
+            <when value="no"/>
+            <when value="yes">
+                <param argument="UseProvidedPrecursorInfo" type="boolean" truevalue="true" falsevalue="false" checked="true" label="Use Provided Precursor"/>
+                <param argument="DoPrecursorDeconvolution" type="boolean" truevalue="true" falsevalue="false" checked="true" label="Deconvolute Precursor"/>
+                <param argument="DeconvolutionMaxAssumedChargeState" type="integer" value="12" label="Deconvolution Max Assumed Charge State"/>
+                <param argument="DeconvolutionIntensityRatio" type="float" value="3.0" label="DeconvolutionIntensityRatio"/>
+                <param argument="DeconvolutionMassTolerance" type="float" value="4.0000" label="DeconvolutionMassTolerance in PPM"/>
+                <param argument="TotalPartitions" type="integer" value="1" label="TotalPartitions"/>
+                <param argument="PrecursorMassTolerance" type="float" value="15.0000" label="PrecursorMassTolerance in PPM"/>
+                <param argument="ProductMassTolerance" type="float" value="25.0000" label="ProductMassTolerance in PPM"/>
+                <param argument="AddCompIons" type="boolean" truevalue="true" falsevalue="false" checked="false" label="AddCompIons"/>
+                <param argument="ScoreCutoff" type="float" value="5.0" label="ScoreCutoff"/>
+                <param argument="ReportAllAmbiguity" type="boolean" truevalue="true" falsevalue="false" checked="true" label="ReportAllAmbiguity"/>
+                <param argument="NumberOfPeaksToKeepPerWindow" type="integer" value="200" label="NumberOfPeaksToKeepPerWindow"/>
+                <param argument="MinimumAllowedIntensityRatioToBasePeak" type="float" value="0.01" label="MinimumAllowedIntensityRatioToBasePeak"/>
+                <param argument="NormalizePeaksAccrossAllWindows" type="boolean" truevalue="true" falsevalue="false" checked="false" label="NormalizePeaksAccrossAllWindows"/>
+                <param argument="TrimMs1Peaks" type="boolean" truevalue="true" falsevalue="false" checked="false" label="TrimMs1Peaks"/>
+                <param argument="TrimMsMsPeaks" type="boolean" truevalue="true" falsevalue="false" checked="true" label="TrimMsMsPeaks"/>
+                <param argument="UseDeltaScore" type="boolean" truevalue="true" falsevalue="false" checked="false" label="UseDeltaScore"/>
+                <param argument="QValueOutputFilter" type="float" value="1.0" label="QValueOutputFilter"/>
+                <param argument="MaxHeterozygousVariants" type="integer" value="4" label="MaxHeterozygousVariants"/>
+                <param argument="MinVariantDepth" type="integer" value="1" label="MinVariantDepth"/>
+                <param argument="SeparationType" type="select" label="SeparationType">
+                    <option value="HPLC" selected="true">HPLC</option>
+                    <option value="CZE">CZE</option>
+                </param>
+                <param argument="DissociationType" type="select" label="DissociationType">
+                    <expand macro="dissociation_options"/>
+                </param>
+                <param argument="MS2ChildScanDissociationType" type="select" label="MS2ChildScanDissociationType">
+                    <expand macro="dissociation_options"/>
+                </param>
+                <param argument="MS3ChildScanDissociationType" type="select" label="MS2ChildScanDissociationType">
+                    <expand macro="dissociation_options"/>
+                </param>
+            </when>
+        </conditional>
+    </xml>
+    <token name="@COMMON_CONFIG@">
+[CommonParameters]
+TaskDescriptor = "CalibrateTask"
+MaxThreadsToUsePerFile = 11
+#if $common.set_common == 'yes' 
+DoPrecursorDeconvolution = $common.DoPrecursorDeconvolution
+UseProvidedPrecursorInfo = $common.UseProvidedPrecursorInfo
+DeconvolutionIntensityRatio = $common.DeconvolutionIntensityRatio
+DeconvolutionMaxAssumedChargeState = $common.DeconvolutionMaxAssumedChargeState
+DeconvolutionMassTolerance = "±${common.DeconvolutionMassTolerance} PPM"
+TotalPartitions = $common.TotalPartitions
+ProductMassTolerance = "±${common.ProductMassTolerance} PPM"
+PrecursorMassTolerance = "±${common.PrecursorMassTolerance} PPM"
+AddCompIons = $common.AddCompIons
+ScoreCutoff = $common.ScoreCutoff
+ReportAllAmbiguity = $common.ReportAllAmbiguity
+NumberOfPeaksToKeepPerWindow = $common.NumberOfPeaksToKeepPerWindow
+MinimumAllowedIntensityRatioToBasePeak = $common.MinimumAllowedIntensityRatioToBasePeak
+NormalizePeaksAccrossAllWindows = $common.NormalizePeaksAccrossAllWindows
+TrimMs1Peaks = $common.TrimMs1Peaks
+TrimMsMsPeaks = $common.TrimMsMsPeaks
+UseDeltaScore = $common.UseDeltaScore
+QValueOutputFilter = $common.QValueOutputFilter
+## CustomIons = $common.CustomIons
+AssumeOrphanPeaksAreZ1Fragments = $common.AssumeOrphanPeaksAreZ1Fragments
+MaxHeterozygousVariants = $common.MaxHeterozygousVariants
+MinVariantDepth = $common.MinVariantDepth
+DissociationType = $common.DissociationType
+SeparationType = $common.SeparationType
+MS2ChildScanDissociationType = $common.MS2ChildScanDissociationType
+MS3ChildScanDissociationType = $common.MS3ChildScanDissociationType
+#else
+DoPrecursorDeconvolution = true
+UseProvidedPrecursorInfo = true
+DeconvolutionIntensityRatio = 3.0
+DeconvolutionMaxAssumedChargeState = 12
+DeconvolutionMassTolerance = "±4.0000 PPM"
+TotalPartitions = 1
+ProductMassTolerance = "±25.0000 PPM"
+PrecursorMassTolerance = "±15.0000 PPM"
+AddCompIons = false
+ScoreCutoff = 5.0
+ReportAllAmbiguity = true
+NumberOfPeaksToKeepPerWindow = 200
+MinimumAllowedIntensityRatioToBasePeak = 0.01
+NormalizePeaksAccrossAllWindows = false
+TrimMs1Peaks = false
+TrimMsMsPeaks = true
+UseDeltaScore = false
+QValueOutputFilter = 1.0
+CustomIons = []
+AssumeOrphanPeaksAreZ1Fragments = true
+MaxHeterozygousVariants = 4
+MinVariantDepth = 1
+DissociationType = "HCD"
+SeparationType = "HPLC"
+MS2ChildScanDissociationType = "Unknown"
+MS3ChildScanDissociationType = "Unknown"
+#end if
+    </token>
+    <xml name="mods_params">
+    </xml>
+    <token name="@MODS_CONFIG@">
+ListOfModsFixed = "Common Fixed\tCarbamidomethyl on C\t\tCommon Fixed\tCarbamidomethyl on U"
+ListOfModsVariable = "Common Variable\tOxidation on M"
+    </token>
+    <xml name="digest_params">
+        <conditional name="digest">
+            <param name="set_digest" type="select" label="Set Digest Parameters">
+                <option value="no">no</option>
+                <option value="yes">yes</option>
+            </param>
+            <when value="no"/>
+            <when value="yes">
+                <param name="Protease" type="select" label="Protease">
+                    <option value="Any">Any</option>
+                    <option value="Arg-C">Arg-C</option>
+                    <option value="Asp-N">Asp-N</option>
+                    <option value="chymotrypsin (don't cleave before proline)">chymotrypsin (don't cleave before proline)</option>
+                    <option value="chymotrypsin (cleave before proline)">chymotrypsin (cleave before proline)</option>
+                    <option value="CNBr">CNBr</option>
+                    <option value="Glu-C">Glu-C</option>
+                    <option value="Glu-C (with asp)">Glu-C (with asp)</option>
+                    <option value="Lys-C (don't cleave before proline)">Lys-C (don't cleave before proline)</option>
+                    <option value="Lys-C (cleave before proline)">Lys-C (cleave before proline)</option>
+                    <option value="Lys-N">Lys-N</option>
+                    <option value="semi-trypsin">semi-trypsin</option>
+                    <option value="trypsin" selected="true">trypsin</option>
+                    <option value="tryptophan oxidation">tryptophan oxidation</option>
+                    <option value="non-specific">non-specific</option>
+                    <option value="top-down">top-down</option>
+                    <option value="singleN">singleN</option>
+                    <option value="singleC">singleC</option>
+                    <option value="collagenase">collagenase</option>
+                </param>
+                <param name="SpecificProtease" type="select" label="SpecificProtease">
+                    <option value="Any">Any</option>
+                    <option value="Arg-C">Arg-C</option>
+                    <option value="Asp-N">Asp-N</option>
+                    <option value="chymotrypsin (don't cleave before proline)">chymotrypsin (don't cleave before proline)</option>
+                    <option value="chymotrypsin (cleave before proline)">chymotrypsin (cleave before proline)</option>
+                    <option value="CNBr">CNBr</option>
+                    <option value="Glu-C">Glu-C</option>
+                    <option value="Glu-C (with asp)">Glu-C (with asp)</option>
+                    <option value="Lys-C (don't cleave before proline)">Lys-C (don't cleave before proline)</option>
+                    <option value="Lys-C (cleave before proline)">Lys-C (cleave before proline)</option>
+                    <option value="Lys-N">Lys-N</option>
+                    <option value="semi-trypsin">semi-trypsin</option>
+                    <option value="trypsin" selected="true">trypsin</option>
+                    <option value="tryptophan oxidation">tryptophan oxidation</option>
+                    <option value="non-specific">non-specific</option>
+                    <option value="top-down">top-down</option>
+                    <option value="singleN">singleN</option>
+                    <option value="singleC">singleC</option>
+                    <option value="collagenase">collagenase</option>
+                </param>
+                <param name="InitiatorMethionineBehavior" type="select" label="InitiatorMethionineBehavior">
+                    <option value="Variable" selected="true">Variable</option>
+                    <option value="Undefined">Undefined</option>
+                    <option value="Retain">Retain</option>
+                    <option value="Cleave">Cleave</option>
+                </param>
+                <param name="SearchModeType" type="select" label="SearchModeType">
+                    <option value="Full" selected="true">Full</option>
+                    <option value="None">None</option>
+                    <option value="Semi">Semi</option>
+                    <option value="SingleN">SingleN</option>
+                    <option value="SingleC">SingleC</option>
+                </param>
+                <param name="FragmentationTerminus" type="select" label="FragmentationTerminus">
+                    <option value="Both" selected="true">Both</option>
+                    <option value="None">None</option>
+                    <option value="N">N</option>
+                    <option value="C">C</option>
+                </param>
+                <param name="MaxMissedCleavages" type="integer" value="2" min="0" max="5" label="MaxMissedCleavages"/>
+                <param name="MinPeptideLength" type="integer" value="7" min="4" label="MinPeptideLength"/>
+                <param name="MaxPeptideLength" type="integer" value="2147483647" max="2147483647" label="MaxPeptideLength"/>
+                <param name="MaxModificationIsoforms" type="integer" value="1024" min="0" max="5000" label="MaxModificationIsoforms"/>
+                <param name="MaxModsForPeptide" type="integer" value="2" min="0" max="10" label="MaxModsForPeptide"/>
+                <param name="GeneratehUnlabeledProteinsForSilac" type="boolean" truevalue="true" falsevalue="false" checked="false" label="GeneratehUnlabeledProteinsForSilac"/>
+            </when>
+        </conditional>
+    </xml>
+    <token name="@DIGEST_CONFIG@">
+[CommonParameters.DigestionParams]
+#if $digest.set_digest == 'yes'
+MaxMissedCleavages = $digest.MaxMissedCleavages
+InitiatorMethionineBehavior = "$digest.InitiatorMethionineBehavior"
+MinPeptideLength = $digest.MinPeptideLength
+MaxPeptideLength = $digest.MaxPeptideLength
+MaxModificationIsoforms = $digest.MaxModificationIsoforms
+MaxModsForPeptide = $digest.MaxModsForPeptide
+Protease = "$digest.Protease"
+SearchModeType = "$digest.SearchModeType"
+FragmentationTerminus = "$digest.FragmentationTerminus"
+SpecificProtease = "$digest.SpecificProtease"
+GeneratehUnlabeledProteinsForSilac = $digest.GeneratehUnlabeledProteinsForSilac
+#else
+MaxMissedCleavages = 2
+InitiatorMethionineBehavior = "Variable"
+MinPeptideLength = 7
+MaxPeptideLength = 2147483647
+MaxModificationIsoforms = 1024
+MaxModsForPeptide = 2
+Protease = "trypsin"
+SearchModeType = "Full"
+FragmentationTerminus = "Both"
+SpecificProtease = "trypsin"
+GeneratehUnlabeledProteinsForSilac = false
+#end if
+    </token>
+
+    
+    <xml name="output_settings_toml">
+        <data name="settings_toml" format="toml" label="${tool.name} on ${on_string} tasksettings.toml" from_work_dir="tasksettings.toml" />
+    </xml>
+    <xml name="calibrated_outputs">
+        <collection name="calibrated_scans" type="list" label="${tool.name} on ${on_string} Calibrated Spectrums">
+            <discover_datasets pattern="^(?P&lt;name&gt;.+\.mzML)$" ext="mzml" directory="output/Task1CalibrationTask" />
+        </collection>
+        <collection name="calibratation_toml" type="list" label="${tool.name} on ${on_string} Calibration TOMLs">
+            <discover_datasets pattern="^(?P&lt;name&gt;.+\.toml)$" ext="toml" directory="output/Task1CalibrationTask" />
+        </collection>
+    </xml>
+    <xml name="search_collection_outputs">
+        <collection name="mzids" type="list" label="${tool.name} on ${on_string} Spectrum Search mzIdent">
+            <filter>search_outputs and 'WriteMzId' in search_outputs</filter>
+            <discover_datasets pattern="^(?P&lt;name&gt;.+\.mzID)$" ext="mzid" directory="output/Task1SearchTask/Individual File Results" />
+        </collection>
+        <collection name="pepxmls" type="list" label="${tool.name} on ${on_string} Spectrum Search pep.xml">
+            <filter>search_outputs and 'WritePepXml' in search_outputs</filter>
+            <discover_datasets pattern="^(?P&lt;name&gt;.+\.pep\.XML)$" ext="pepxml" directory="output/Task1SearchTask/Individual File Results" />
+        </collection>
+    </xml>
+
+    <token name="@METAMORPHEUS_HELP@"><![CDATA[
+**MetaMorpheus**
+
+MetaMorpheus_ is a bottom-up proteomics database search software with integrated post-translational modification (PTM) discovery capability. 
+See the wiki page for details:  https://github.com/smith-chem-wisc/MetaMorpheus/wiki
+
+Typical MetaMorpheus Workflow:
+
+  1. MetaMorpheus Calibration - of MassSpec Spectrum files using a reference protein database (preferably in Uniprot XML format)
+  2. MetaMorpheus G-PTM-D - Post-translational modification (PTM) discovery from the Calibrated Spectrum files
+  3. MetaMorpheus Database Search - Proetomics Search using the Calibrated Spectrum files and the GPTMD protein database
+
+.. image:: MetaMorpheusWorkflow.png
+  :width: 823
+  :height: 759
+
+.. _MetaMorpheus: https://github.com/smith-chem-wisc/MetaMorpheus
+
+]]></token>    
+
+    <xml name="citations">
+        <citations>
+            <citation type="doi">10.1021/acs.jproteome.7b00873</citation>
+            <yield />
+        </citations>
+    </xml>
+
+</macros>

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/metamorpheus_calibration.xml	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,67 @@
+<tool id="metamorpheus_calibration" name="MetaMorpeus Calibration" version="@TOOL_VERSION@+galaxy@VERSION_SUFFIX@" profile="@PROFILE@" python_template_version="3.5">
+    <description>identify peptides by their calibrate the m/z values of all peaks in the spectra</description>
+    <macros>
+        <import>macros.xml</import>
+    </macros>
+    <expand macro="requirements" />
+    <command detect_errors="exit_code"><![CDATA[
+@PREPARE_INPUTS@
+@MERGE_TOMLS@
+metamorpheus
+-t tasksettings.toml
+## -s #echo ' '.join($spectrum_names)#
+-s $inputs_dir
+-d #echo ' '.join($database_names)#
+-o output
+--mmsettings data
+    ]]></command>
+    <configfiles>
+        <configfile name="default_toml"><![CDATA[#slurp
+@DEFAULT_CALIBRATION_TOML@
+]]></configfile>
+        <configfile name="user_toml">
+@CALIBRATE_CONFIG@
+@COMMON_CONFIG@
+        </configfile>
+        <configfile name="task_settings_toml">#slurp
+        </configfile>
+    </configfiles>
+    <inputs>
+        <expand macro="input_spectrums" multiple="true"/>
+        <expand macro="input_databases"/>
+        <expand macro="input_toml"/>
+        <expand macro="calibrate_params"/>
+        <expand macro="common_params"/>
+    </inputs>
+    <outputs>
+        <expand macro="output_settings_toml"/>
+        <data name="results" format="txt" label="${tool.name} on ${on_string} results.txt" from_work_dir="output/allresults.txt"/>
+        <data name="prose" format="txt" label="${tool.name} on ${on_string} prose.txt" from_work_dir="output/Task1CalibrationTask/prose.txt"/>
+        <expand macro="calibrated_outputs"/>
+    </outputs>
+    <tests>
+        <test>
+            <param name="spectrums" ftype="mzml" value="SmallCalibratible_Yeast.mzML"/>
+            <param name="databases" ftype="fasta" value="SmallYeast.fasta"/>
+            <output name="results">
+                <assert_contents>
+                    <has_text text="MS2 calibration datapoint count:" />
+                    <has_text text="Engine type: CalibrationEngine" />
+                </assert_contents>
+            </output>
+            <output_collection name="calibrated_scans" type="list">
+                <element name="SmallCalibratible_Yeast-calib.mzML">
+                    <assert_contents>
+                        <has_text_matching expression="id=.SmallCalibratible_Yeast-calib" />
+                        <has_text_matching expression="dataProcessing id=.mzLibProcessing" />
+                    </assert_contents>
+                </element>
+            </output_collection>
+ 
+        </test>
+    </tests>
+    <help><![CDATA[
+@METAMORPHEUS_HELP@
+    ]]></help>
+    <expand macro="citations" />
+</tool>

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/metamorpheus_g_ptm_d.xml	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,65 @@
+<tool id="metamorpheus_g_ptm_d" name="MetaMorpeus G-PTM-D" version="@TOOL_VERSION@+galaxy@VERSION_SUFFIX@" profile="@PROFILE@" python_template_version="3.5">
+    <description>Post-translational modification (PTM) discovery</description>
+    <macros>
+        <import>macros.xml</import>
+    </macros>
+    <expand macro="requirements" />
+    <command detect_errors="exit_code"><![CDATA[
+@PREPARE_INPUTS@
+@LN_CALIB_TOML@
+@MERGE_TOMLS@
+metamorpheus
+-t tasksettings.toml
+## -s #echo ' '.join($spectrum_names)#
+-s $inputs_dir
+-d #echo ' '.join($database_names)#
+-o output
+--mmsettings data
+    ]]></command>
+    <configfiles>
+        <configfile name="default_toml"><![CDATA[#slurp
+@DEFAULT_GPTMD_TOML@
+]]></configfile>
+        <configfile name="user_toml">
+@GPTMD_CONFIG@
+@COMMON_CONFIG@
+        </configfile>
+        <configfile name="task_settings_toml">#slurp
+        </configfile>
+    </configfiles>
+    <inputs>
+        <expand macro="input_spectrums" multiple="true" filetype="Calibrated Spectrum"/>
+        <expand macro="calib_toml"/>
+        <expand macro="input_databases"/>
+        <expand macro="input_toml"/>
+        <expand macro="common_params"/>
+    </inputs>
+    <outputs>
+        <expand macro="output_settings_toml"/>
+        <data name="results" format="txt" label="${tool.name} on ${on_string} results.txt" from_work_dir="output/allresults.txt"/>
+        <data name="prose" format="txt" label="${tool.name} on ${on_string} prose.txt" from_work_dir="output/Task*GptmdTask/prose.txt"/>
+        <data name="db_xml" format="uniprotxml" label="${tool.name} on ${on_string} ${databases[0].name.rsplit('.',1)[0]}GPTMD.xml" from_work_dir="output/Task*GptmdTask/*GPTMD.xml"/>
+        <data name="psmtsv" format="tabular" label="${tool.name} on ${on_string} GPTMD_Candidates.psmtsv" from_work_dir="output/Task*GptmdTask/GPTMD_Candidates.psmtsv"/>
+    </outputs>
+    <tests>
+        <test>
+            <param name="spectrums" ftype="mzml" value="SmallCalibratible_Yeast-calib.mzML"/>
+            <param name="calib_tomls" ftype="toml" value="SmallCalibratible_Yeast-calib.toml"/>
+            <param name="databases" ftype="fasta" value="SmallYeast_uniprot.xml"/>
+            <output name="results">
+                <assert_contents>
+                    <has_text text="Engine type: GptmdEngine" />
+                </assert_contents>
+            </output>
+            <output name="db_xml">
+                <assert_contents>
+                    <has_text text="mzLibProteinDb" />
+                </assert_contents>
+            </output>
+        </test>
+    </tests>
+    <help><![CDATA[
+@METAMORPHEUS_HELP@
+    ]]></help>
+    <expand macro="citations" />
+</tool>

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/metamorpheus_search.xml	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,73 @@
+<tool id="metamorpheus_search" name="MetaMorpeus Database Search" version="@TOOL_VERSION@+galaxy@VERSION_SUFFIX@" profile="@PROFILE@" python_template_version="3.5">
+    <description>identify peptides by their fragmentation spectra</description>
+    <macros>
+        <import>macros.xml</import>
+    </macros>
+    <expand macro="requirements" />
+    <command detect_errors="exit_code"><![CDATA[
+@PREPARE_INPUTS@
+@LN_CALIB_TOML@
+@MERGE_TOMLS@
+metamorpheus
+-t tasksettings.toml
+-s ${inputs_dir}
+-d #echo ' '.join($database_names)#
+-o output
+--mmsettings data
+    ]]></command>
+    <configfiles>
+        <configfile name="default_toml"><![CDATA[#slurp
+@DEFAULT_SEARCH_TOML@
+]]></configfile>
+        <configfile name="user_toml">
+@SEARCH_CONFIG@
+@COMMON_CONFIG@
+        </configfile>
+        <configfile name="task_settings_toml">#slurp
+        </configfile>
+    </configfiles>
+    <inputs>
+        <expand macro="input_spectrums" multiple="true" filetype="Calibrated Spectrum"/>
+        <expand macro="calib_toml"/>
+        <expand macro="input_databases"/>
+        <expand macro="input_toml"/>
+        <expand macro="common_params"/>
+        <expand macro="search_params"/>
+    </inputs>
+    <outputs>
+        <expand macro="output_settings_toml"/>
+        <data name="results" format="txt" label="${tool.name} on ${on_string} results.txt" from_work_dir="output/allresults.txt"/>
+        <data name="prose" format="txt" label="${tool.name} on ${on_string} prose.txt" from_work_dir="output/Task*SearchTask/prose.txt"/>
+        <data name="allpsms" format="tabular" label="${tool.name} on ${on_string} AllPSMs.psmtsv" from_work_dir="output/Task*SearchTask/AllPSMs.psmtsv"/>
+        <data name="allpsms_percolator" format="tabular" label="${tool.name} on ${on_string} AllPSMs_FormattedForPercolator.tab" from_work_dir="output/Task*SearchTask/AllPSMs_FormattedForPercolator.tab"/>
+        <data name="allpeptides" format="tabular" label="${tool.name} on ${on_string} AllPeptides.psmtsv" from_work_dir="output/Task*SearchTask/AllPeptides.psmtsv"/>
+        <data name="allquantifiedpeaks" format="tabular" label="${tool.name} on ${on_string} AllQuantifiedPeaks.tsv" from_work_dir="output/Task*SearchTask/AllQuantifiedPeaks.tsv">
+        </data>
+        <data name="allquantifiedpeptides" format="tabular" label="${tool.name} on ${on_string} AllQuantifiedPeptides.tsv" from_work_dir="output/Task*SearchTask/AllQuantifiedPeptides.tsv">
+        </data>
+        <data name="allquantifiedprotein" format="tabular" label="${tool.name} on ${on_string} AllQuantifiedProteinGroups.tsv" from_work_dir="output/Task*SearchTask/AllQuantifiedProteinGroups.tsv">
+        </data>
+        <expand macro="search_collection_outputs"/>
+    </outputs>
+    <tests>
+        <test>
+            <param name="spectrums" ftype="mzml" value="SmallCalibratible_Yeast-calib.mzML"/>
+            <param name="calib_tomls" ftype="toml" value="SmallCalibratible_Yeast-calib.toml"/>
+            <param name="databases" ftype="fasta" value="SmallYeastGPTMD.xml"/>
+            <output name="results">
+                <assert_contents>
+                    <has_text text="Engine type: ProteinScoringAndFdrEngine" />
+                </assert_contents>
+            </output>
+            <output name="allpsms">
+                <assert_contents>
+                    <has_text text="KGNNTANATN[Common Artifact:Deamidation on N]SANTVQK" />
+                </assert_contents>
+            </output>
+        </test>
+    </tests>
+    <help><![CDATA[
+@METAMORPHEUS_HELP@
+    ]]></help>
+    <expand macro="citations" />
+</tool>

Binary file static/images/MetaMorpheusWorkflow.png has changed

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/test-data/SmallCalibratible_Yeast-calib.mzML	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,8122 @@
+<?xml version="1.0" encoding="utf-8"?>
+<indexedmzML xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xmlns:xsd="http://www.w3.org/2001/XMLSchema" xmlns="http://psi.hupo.org/ms/mzml">
+  <mzML version="1.1.0" id="SmallCalibratible_Yeast-calib">
+    <cvList count="2">
+      <cv id="MS" fullName="Proteomics Standards Initiative Mass Spectrometry Ontology" version="4.0.1" URI="https://raw.githubusercontent.com/HUPO-PSI/psi-ms-CV/master/psi-ms.obo" />
+      <cv id="UO" fullName="Unit Ontology" version="12:10:2011" URI="http://obo.cvs.sourceforge.net/*checkout*/obo/obo/ontology/phenotype/unit.obo" />
+    </cvList>
+    <fileDescription>
+      <fileContent>
+        <cvParam cvRef="MS" accession="MS:1000579" value="" name="MS1 spectrum" />
+        <cvParam cvRef="MS" accession="MS:1000580" value="" name="MSn spectrum" />
+      </fileContent>
+      <sourceFileList count="1">
+        <sourceFile id="SmallCalibratible_Yeast.raw" name="SmallCalibratible_Yeast.raw" location="file:///C:/Data/SlicedYeastRawFiles">
+          <cvParam cvRef="MS" accession="MS:1000768" value="" name="Thermo nativeID format" />
+          <cvParam cvRef="MS" accession="MS:1000563" value="" name="Thermo RAW format" />
+          <cvParam cvRef="MS" accession="MS:1000569" value="4ede32545182c06b031abc46e29802452427783d" name="SHA-1" />
+        </sourceFile>
+      </sourceFileList>
+    </fileDescription>
+    <softwareList count="2">
+      <software id="mzLib" version="1">
+        <cvParam cvRef="MS" accession="MS:1000799" value="mzLib" name="custom unreleased software tool" />
+      </software>
+    </softwareList>
+    <instrumentConfigurationList count="1">
+      <instrumentConfiguration id="IC1">
+        <cvParam cvRef="MS" accession="MS:1000031" value="" name="instrument model" />
+        <componentList count="3">
+          <source order="1">
+            <cvParam cvRef="MS" accession="MS:1000008" value="" name="ionization type" />
+          </source>
+          <analyzer order="2">
+            <cvParam cvRef="MS" accession="MS:1000484" value="" name="orbitrap" />
+          </analyzer>
+          <detector order="3">
+            <cvParam cvRef="MS" accession="MS:1000026" value="" name="detector type" />
+          </detector>
+        </componentList>
+      </instrumentConfiguration>
+    </instrumentConfigurationList>
+    <dataProcessingList count="1">
+      <dataProcessing id="mzLibProcessing">
+        <processingMethod order="0" softwareRef="mzLib">
+          <cvParam cvRef="MS" accession="MS:1000544" value="" name="Conversion to mzML" />
+        </processingMethod>
+      </dataProcessing>
+    </dataProcessingList>
+    <run id="SmallCalibratible_Yeast-calib" defaultInstrumentConfigurationRef="IC1">
+      <spectrumList count="142" defaultDataProcessingRef="mzLibProcessing">
+        <spectrum id="controllerType=0 controllerNumber=1 scan=1" index="0" defaultArrayLength="1964">
+          <cvParam cvRef="MS" accession="MS:1000579" value="" name="MS1 spectrum" />
+          <cvParam cvRef="MS" accession="MS:1000511" value="1" name="ms level" />
+          <cvParam cvRef="MS" accession="MS:1000127" value="" name="centroid spectrum" />
+          <cvParam cvRef="MS" accession="MS:1000130" value="" name="positive scan" />
+          <cvParam cvRef="MS" accession="MS:1000528" value="300.17216704212484" name="lowest observed m/z" unitAccession="MS:1000040" unitName="m/z" unitCvRef="MS" />
+          <cvParam cvRef="MS" accession="MS:1000527" value="1499.108694781585" name="highest observed m/z" unitAccession="MS:1000040" unitName="m/z" unitCvRef="MS" />
+          <cvParam cvRef="MS" accession="MS:1000285" value="506163360" name="total ion current" />
+          <cvParam cvRef="MS" accession="MS:1000504" value="359.2405153718944" name="base peak m/z" unitAccession="MS:1000040" unitName="m/z" unitCvRef="MS" />
+          <cvParam cvRef="MS" accession="MS:1000505" value="10261801" name="base peak intensity" unitAccession="MS:1000131" unitName="number of detector counts" unitCvRef="MS" />
+          <scanList count="1">
+            <cvParam cvRef="MS" accession="MS:1000795" value="" name="no combination" />
+            <scan>
+              <cvParam cvRef="MS" accession="MS:1000016" value="24.044005" name="scan start time" unitAccession="UO:0000031" unitName="minute" unitCvRef="UO" />
+              <cvParam cvRef="MS" accession="MS:1000512" value="FTMS + p NSI Full ms [300.00-1500.00]" name="filter string" />
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+              <scanWindowList count="1">
+                <scanWindow>
+                  <cvParam cvRef="MS" accession="MS:1000501" value="300" name="scan window lower limit" unitAccession="MS:1000040" unitName="m/z" unitCvRef="MS" />
+                  <cvParam cvRef="MS" accession="MS:1000500" value="1500" name="scan window upper limit" unitAccession="MS:1000040" unitName="m/z" unitCvRef="MS" />
+                </scanWindow>
+              </scanWindowList>
+            </scan>
+          </scanList>
+          <binaryDataArrayList count="2">
+            <binaryDataArray encodedLength="20952">
+              <cvParam cvRef="MS" accession="MS:1000514" value="" name="m/z array" unitAccession="MS:1000040" unitName="m/z" unitCvRef="MS" />
+              <cvParam cvRef="MS" accession="MS:1000523" value="" name="64-bit float" />
+              <cvParam cvRef="MS" accession="MS:1000576" value="" name="no compression" />
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+              <cvParam cvRef="MS" accession="MS:1000523" value="" name="64-bit float" />
+              <cvParam cvRef="MS" accession="MS:1000576" value="" name="no compression" />
+              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9/mQXDLLd0A7fdv9atN3QOb84r2a03dAMbBcAF7jd0Ci6GDgeON3QAcxaECn43dAMWZyQOjjd0Bkv9tiQ/N3QJefDMTY+ndAD+48hWoCeECxrlTFAQN4QK1z18f+EnhAjKjgZzkTeECQTOyHgxN4QOvVA2gZFHhAyhcaSQUbeECdQiOpPxt4QLZcXcoPI3hAbKplqkQjeECmC2xKbSN4QHxYcQqPI3hAWN58atgjeEBsVYnKJyR4QCRFmWvrKnhAUeqoC08reEC0pl5M1C94QPYG/czEM3hAClkUTVk0eEAvIeSO4j94QNEkE+8NQXhAAsR174FDeEBkUo3vF0R4QMmalE9GRHhAV7CZr2ZEeEB4pKRvrER4QJ3AoNDxSnhAPammcBdLeEBYYmLRwk94QMei6REgU3hAuwD20W5TeEDSWgby1lN4QPx1DTIEVHhAAiIS8iFUeEAVGSqzGFt4QIoaL5M4W3hATjzoc9NfeEAPNGf0+2J4QGM2b/QuY3hAcI54dGpjeEBG0IsU5WN4QFbXktQRZHhA2u9f1StpeECzIu/WGXN4QJx+9PY7c3hAwG8GN65zeEAoZwvXzXN4QE9gFrcTdHhAlu10GSqDeECI/XeZPYN4QK+9xHqEi3hAHZfve/OSeEAZhAS8eJN4QLWjCVyZk3hAsZ0r3c+aeEDv645epqN4QKegxd9gq3hADhEDQUazeEALfAjBaLN4QGnZEsGqs3hACHpJwmS7eEA7T4gDU8N4QMQ6mGO4w3hAhlALhlHTeECWMh1mw9N4QPMZjOhB43hA8tAjS8TzeECrQkOs6vp4QMyPScwS+3hAZ/1XrG77eECKWJENOgN5QByfo22uA3lA+8i67UEEeUCXGsKuzgp5QCXXy64MC3lA+LkFcNsSeUDXSynwvRN5QIPlM3ABFHlAdUTw8LAYeUD392QRmBt5QIxIizLqInlA01qWsjAjeUC5IaFSdSN5QC/krZLGI3lAxIu08vAjeUCmvcQSWCR5QM2czDKKJHlAZT/WsyUreUC5LRWVFDN5QKtXG9U7M3lAor0gNV4zeUBR7CU1fzN5QBB7LVWvM3lAF+g5df4zeUBIVkoVZzR5QFFlXvZEO3lA0BphNlY7eUClZ2b2dzt5QLVllrcHQ3lA6duf90NDeUDcBaY3a0N5QEO+sje8Q3lAnt+9FwNEeUC6HQ+6xFJ5QHqWMpqmU3lAMP49Ou9TeUASsFm7/Vp5QGCZmHzsYnlAIkqc/ANjeUBP76ucZ2N5QCVwt9ywY3lAPGK7/MljeUAYgtV9zmp5QPGX2z31anlArcA235dzeUCjJjw/unN5QF6KcABme3lA1nSzQW6DeUA39Lmhl4N5QH/swWHKg3lAJ0H2wnWLeUBbRAHju4t5QH2Ln8Orj3lALVcipOySeUAzNy3kMZN5QGvPMoRVk3lA9jU6pISTeUDNXUqE65N5QK/QbWUrm3lAbm6GJcibeUB9ur8mk6N5QPnAxCazo3lAErDPxvijeUAzsefH76p5QPrAlohKr3lAkIcqifeyeUC3dUNJlrN5QJ3lbaoCu3lAoBZ7qla7eUB1jq/rAsN5QPuWu4tPw3lA7W0ADWTLeUBLED1ORNN5QA7bQ45v03lAHcnJsIDjeUDseNtQ8eN5QNav65BY5HlAZ0g9cxzzeUDcY0UTUPN5QEqUUFOX83lAN59Ts6rzeUBh7mBz//N5QDcWcVNm9HlAZBzRFYYDekBwwuPV/AN6QAz86zUxBHpACUL81ZgEekBNcQOWxgR6QEvoN/jQEnpA1GBJOEATekC6tFW4jhN6QHP/ZBjwE3pA6I1r2BkUekCNe3GYPxR6QOsMghipFHpAu+GImNQUekBvhoh5MBt6QCyamNmWG3pAeVrDOgUjekDdvM1aRyN6QOpt0jplI3pA1P3d2q4jekDBVup6/SN6QOBK9TpDJHpAf38AvOgqekDKJga8DCt6QO08Ddw5K3pA5xIY3H4rekC2QBq8jCt6QHskRl0CM3pASy1TXVUzekA4+V0dmjN6QK+Ea13wM3pANad6vVA0ekA0HJT+UDt6QNhOzP8UQ3pAhOjWf1hDekBBo+t/3EN6QMvau2AKSXpAzu4RgS5LekDYChzhbkt6QMLzIuGaS3pAxUklwalLekDFYyiBvUt6QJd0LiHkS3pArA18QdJNekCNwkvi/FJ6QAO5XqJ1U3pAHAFlop1TekCHNoSDwlp6QBlYoQN8W3pADt7jxIFjekBfS/FE12N6QPUBCUVuZHpAaRZVBw9zekDNU2pHlnN6QMa2diflc3pA9bSBJyt0ekB5Qbio5Ht6QMbC6mmEg3pA+pHvCaODekBfwPOpvYN6QMMI+wnsg3pAeNoty42LekBOzjcrzYt6QH5hPavwi3pACaVqDG+TekCSkHps1JN6QHU1iawxlHpAuSez7ZqbekDpfdvu+aJ6QN9l8A5/o3pAVqP0DpqjekCtcBgw3Kp6QI42QjDmq3pADxR7ca6zekBNWIXR77N6QLTRmTFytHpAgyasEkW7ekB5FPvTmcN6QN6qC3QDxHpA+7sSdDDEekCn/CGUkcR6QPfPN7V6y3pAbxN2VmXTekCJznp2g9N6QCGNixbu03pATxiY9j3UekBEJ70XiNt6QBa87Zgb43pAR7f/GI7jekAN2Ag5yON6QP0eC7nW43pAvfsbGULkekAaPyNZcOR6QMlIM3nW5HpAAIGB24TzekA934772fN6QHs9nBsv9HpADFCo+3v0ekCBt7V8L/t6QOn8w1yK+3pAkFH4vTUDe0AYIwVehwN7QOhFFR7uA3tAIGscnhsEe0D1kix+ggR7QHBYNX8YC3tA/+9Jn5sLe0Ay6n3ARBN7QBvilWDdE3tAPKKaoPsTe0BtwqEAKRR7QCLRsUCPFHtAufXKgY0be0CpAw8DnSN7QB6SFcPGI3tAGMEbI+4je0D6viXDLSR7QLuevKRMLntAaGqE5UQze0A7yZPFpjN7QDfBmiXTM3tA+tmqpTk0e0C//M7mfTt7QCZtDEhjQ3tA5aIYCLFDe0DSxx4o2EN7QHcfTAlXS3tAYP97CuZSe0BZsJEqcFN7QGcinmq/U3tATemoCgRUe0AvqtUrf1t7QAOMXyztXntAp+IhrcJje0CgRS6NEWR7QOhXOQ1YZHtAbHxjjsJre0BzLqLvr3N7QPQ5pw/Qc3tA7WrIkAF7e0DAPNaQWXt7QPgI4rCke3tAODIL8giDe0BhAyhywIN7QCpGLfLhg3tAyUpRcyWLe0CyLqD0eZN7QDGpyRSClHtAICwn15Gje0DJzElXbqR7QDnPQ1imqntAFbJpmJere0DexqI5YbN7QAw4rFmds3tAy/s7HO3De0A/mVN8g8R7QMj3YfzexHtATpNkvU3Le0A7Abye2NN7QACVw94I1HtA5MbT/m/Ue0ALKOveBNV7QBdk7T9x23tAMXM1QZrje0CWuzyhyON7QDG2TGEu5HtAiPRTgVzke0BlIWSBw+R7QAIzlUO48ntA6Xuvo1/ze0A21tFjOvR7QCqN2YNr9HtApW7po9D0e0C6t+TEEPt7QMFy+iSb+3tAcwguxkEDfEC+pEGmvgN8QDPaTAYGBHxAUDldRm4EfEC0g3/Hpgt8QAuUugh9E3xA5d3GSMsTfECxn+IIfBR8QCV1NitOI3xACBpFa6sjfECJP01L3yN8QDVMVusYJHxAb4hnq4YkfEDWSWJswyp8QHxkmwwvLHxANMvITa4zfEDKZ92NMTR8QKn14Y1ONHxAXJTsLZI0fECunknwnkN8QDeKWVAERHxAboGU8dlLfECHM8ISW1N8QPlG0RK7U3xAY6UEVGBbfECXTxQUxFt8QMXaIPQTXHxAg4VG9WFjfEBj1FJVsGN8QKOKZpoEhHxAhlRquhyEfEA/YIF6r4R8QHu8c18vpHxA6UV6/1ikfEB//JH/76R8QN+8qyDyq3xAmgbdIYqzfEBzqeTBurN8QBnl88EbtHxAUAr7QUm0fEA5QQuCsLR8QDzAIcI/tXxA1MYYw2S7fEABPlyEcMN8QMdEYuSWw3xAC090xAnEfEBJX3ikI8R8QI01hARvxHxA8n2LZJ3EfEA4KqUFn8t8QMPK7EbF03xA1IcJR3zUfED0YRFHrtR8QEsvNWjw23xASLp3SfbjfEBySH2pGeR8QAq5hAlJ5HxAW/KLCXfkfEDN0ZSJr+R8QI4x8mu+83xA0q4CbCf0fEBNaIBOBAR9QN4Hjg5bBH1AxB8/Mt0bfUBfX4Ez4SN9QD/IkFNDJH1An+XEVO0rfUAELsy0Gyx9QPfB+RWcM31AUXAG1uwzfUDGTBbWUTR9QLnMehiOQ31AaxKKWO9DfUCJI5FYHER9QMUW9RpVU31Aq1D+2o9TfUAPQArb21N9QJolhF2gY31Ak5eh3VtkfUDtmwygwXN9QGboIUBJdH1AaTMyALF0fUDkApQi3IN9QMBJp+JWhH1AxymyIpyEfUAQfPIE8pJ9QEQFLGVglH1AmHoyhYmUfUBbk0IF8JR9QHmkSQUdlX1A/lNaRYeVfUAD5Ffm1Zt9QKVCncfto31A5mmr50ekfUDMvbdnlqR9QLz5x8f9pH1AEqgwqlS0fUBgvztKm7R9QL5QTMoEtX1ATfNSCi+1fUBfVJLsfsN9QJpcnSzFw31Ao16kzPHDfUDBvbQMWsR9QDIQvKyIxH1AwSAJjtHMfUD+7xBvYdN9QMmIGM+R031AoL85T2XUfUArJkFvlNR9QFxgS4/V1H1AoslNEEPbfUCzMY4w3dx9QIt5lhFw431Ayhq7UVnkfUBOlsURnOR9QKjONlQp9H1AaiOiFpEDfkCEa6gWuQN+QEn/r1bpA35ACSHz9/ILfkA1JTiZCBR+QHlGsNvBI35Ays3AGyskfkAEwgI9LSx+QC5CeR/cO35AOoB/3wM8fkBl+rsg40N+QLurwWAHRH5AE30EAg9MfkCyQBXCeUx+QCn3UYNaVH5AyGxZA4pUfkBGH7/lzWN+QM6X0CU9ZH5ABjDWxWBkfkDooN6FlmR+QPKI4mWvZH5AtMNKaAN0fkBP/VLIN3R+QE9/YoiadH5AwdFpKMl0fkDRJnooMXV+QJe6gWhhdX5AG06Lifx7fkCluWHqUYF+QD6pxOrHg35AsG7KquyDfkAl2NuKW4R+QDvk4mqIhH5AK3nuKtKEfkA78/MK9YR+QEfVj6vViH5Av9/4i3KLfkBvzwXsxIt+QGtuEewOjH5AP9l9TMGOfkB4ZEgNy5N+QGG1Ww1GlH5A4BFj7XSUfkCjKnNt25R+QP2zik1xlX5AMxaGDrKbfkAQaIvu05t+QJFFxC+co35AI5fIr7ejfkBuPs6v26N+QCD32w8zpH5A6RTsr5mkfkCr3/LvxKR+QG4d+E/mpH5AD2kNEcyrfkD8rVCS1rN+QCl4VRL1s35AOiZhcj+0fkBWhXGyp7R+QMsKoXM0vH5APJPJtJTDfkBZS9VU38N+QDa33fQUxH5A19vitDXEfkCtgmX3MdR+QFZTb3dw1H5AcKqGFwXVfkADpMz5fuN+QLVC15nC435AwKzqOT7kfkB1h/T5fOR+QN0aDBoT5X5AAOtevN7zfkA6ZmgcG/R+QIJecNxN9H5AajnoXgUEf0D/Cx5Augt/QDzJYGHBE39AYGxpYfgTf0B5WNejcCN/QMey+WNLJH9AjcgQZN4kf0CS3jxFVSx/QChjaebOM39AJKl5hjY0f0B8Wn/GWjR/QATTkAbKNH9AvNyjZ6E7f0Azx+aoqUN/QC2sAklbRH9A3GcJKYZEf0A7UhUJ0kR/QPXGdYv0U39Aq3yKa3hUf0DfJpor3FR/QLsFoesHVX9AEYq4q51Vf0AHJMSL51V/QOCsyGsEVn9AuDqcjEdbf0DepQyOcWR/QCkOGu7GZH9AuLI7T/trf0AomH5wA3R/QELVklCEdH9AHHia8LR0f0DXi6pQG3V/QN7EsPBCdX9Al0HCcRB8f0Cpe/FSm4N/QEEG/HLeg39ArFMD8wyEf0A4RwzzRYR/QIN7E9NzhH9AfN4fs8KEf0BCDDYUrot/QLwyeHWxk39AGgOBlemTf0Bu4JO1YZR/QNeyo3XGlH9ACXQZmHCkf0BEIyl41KR/QAxjkZootH9A7ruxu1S7f0AvQvXcYMN/QF+/Fh02xH9AHNMmfZzEf0BVMZC/99N/QHbMnx9b1H9Aby+s/6nUf0DDSBpiI+R/QJx4I+Jd5H9A/iswwq7kf0Bu/anEcvR/QKCfjMP5AYBAG8CUgy0CgECkQ5jjQwKAQG9V2AQ6CoBAvdTvpM8KgEAXaxTGFhKAQGJGIEZiEoBAVZtVBxQagECfz1znQRqAQL05X0dRGoBABL9o540agEBO82/HuxqAQG/Nd8ftGoBAJdIASFYegEDthJUoCSKAQKnxoOhRIoBAwsaoyIMigEBrl7JIwiKAQIUv3akvKoBA+UrlSWMqgECBzuipeSqAQDAX8WmuKoBAta4ZCw8ygEAjxSGLQjKAQOLGJ8toMoBAkWgr638ygEDYI1Ys7jmAQOZhXOwVOoBALLNfDCs6gED5MWSsRzqAQPYPaExgOoBABoptLIM6gEDeI57NFkKAQA8qom0wQoBAuwKljUJCgEBQkKgtWUKAQENHsE2KQoBAgNveDhFKgEA52OQuN0qAQIcJ846RSoBAH3Ej8CNSgEDaImHxClqAQMDpa5FPWoBAfFZ3UZhagEBIJaBS+mGAQLeUozIQYoBAEZyrUkNigEDGHbqyn2KAQGeYSxM+ZoBAvwOGE7JngEBrzuLzAGqAQFwv6DMjaoBACtHrUzpqgEBoACp1JHKAQA1hLlVAcoBA2mw01WZygECF/WdWDXqAQCQadHZaeoBAKRq8F4OCgECyrus4EIqAQDO68FgwioBAb4iN2RaOgEAJdTy6cJKAQHGGRBqkkoBAu2FQmu+SgEAs6njbT5qAQMXNflt1moBA7KyGe6eagEAJgbD8D6KAQJCRtTwwooBAaqe7/FaigEBTA8EceaKAQHZE970wqoBA0b79/VmqgEALvjE/A7KAQPRnQJ9gsoBA+xl/AE66gEC95IVAebqAQBSNtIEAwoBAlrK8YTTCgEA+3MFBVcKAQOTjysGOwoBAuVv/AjvKgECmDQcDbMqAQDq1DWOWyoBAfQabQxrOgECFUzxkHdKAQJXNQURA0oBAbIfd5B/WgEC17HuFENqAQDANhEVE2oBARnjAJiPigECenMSGPeKAQGItXQcJ5oBAlAgEiC/qgEBaFUSJJfKAQFn2iEo6+oBAxJyLKkv6gEBDhpTqg/qAQNFI2IuRAoFAPP7rCw8DgUBFdQztOwqBQMeaFM1vCoFAadkcTaQKgUDO/C7NFwuBQBczUc5PEoFAOIBX7ncSgUAb11zumRKBQB57aA7kEoFAbtCN7y8agUBuBJRvVxqBQD5MmQ95GoFARIWfr6AagUBCJKuv6hqBQIoSLLAfHoFAIc7NkCUigUCPGNyQgCKBQEcV4rCmIoFAAO8NEhwqgUANryOSpiqBQJ6PRBPWMYFAyN5R0yoygUAZBJC0FDqBQEMfl/RBOoFAzMuutNg6gUBUB7XXGk6BQB9TY7hwUoFAdSSmWXhagUDdO+hae2KBQElK9zrbYoFAjjtxu+NlgUCpTSh8cWqBQEXVORzhaoFAo0Nw3ZlygUDQmnY9wnKBQI9Urd58eoFA7QqzPqF6gUCl2ex/b4KBQMVA9l+rgoFAMN4hQR+KgUBx6yyhZYqBQAYgNeGZioFAirddgvqRgUBUbWEiEpKBQLyybwJtkoFAqxN1Qo+SgUAmRanDOZqBQC/UsUNwmoFAy/O245CagUD4Sr1DuZqBQESpQ+QQnoFAw/oqBjCqgUDHnjYmeqqBQFpow6b6rYFAIdFtxzeygUD4HXOHWbKBQEwGeMd4soFAqZ3C6LG6gUCcNyrrAcqBQLm7LwslyoFApeA1K0zKgUBoPnjsUNKBQIJseyxl0oFAChmT7PvSgUAeqw1tCNaBQBPpri0L2oFAV4u0DS/agUAw78MNkdqBQMkX/M5U4oFAVNf+TmbigUDW4gNvhuKBQOkaGC8H44FAIKpG0I3qgUAdFUxQsOqBQMI2WJD96oFA7otakWrxgUCYRoDRWvKBQAkmiVGT8oFAgNaLcaTygUD/v5Qx3fKBQJQFyTKI+oFAMsAC9FUCgkB6EQYUawKCQEmNETS0AoJALktF1VsKgkB9SE21jgqCQKYqlva8EoJABlO8Fw4agkA0N8RXQBqCQNCk0jecGoJAA58GWUUigkDCAva5OSiCQJlJkzojLIJA4SEw+wkwgkCV5prbsTKCQBklyBwwOoJAwsHLHEc6gkCKONcckDqCQAj6TZ9ASoJA+wlRH1RKgkDls19/sUqCQL5nk+BYUoJA4Qqc4I9SgkC9h9BBPFqCQDyl34GcWoJAPwEcA3tigkB90idDxmKCQIxmMOP8YoJAhnszgxBjgkCTI2FkkWqCQLTydkQca4JA8d+gZYVygkCwFa0l03KCQOYx3aZjeoJAhJMbCE+CgkA9HSMIf4KCQNUAKYikgoJAXsaqCT2MgkAGoKJKZ5KCQFdBtkrkkoJAujLdazqagkAcBietbqKCQF26Nq3SooJAokviLRengkAiK2QuUqqCQFYapi9UsoJAquPvMIi6gkCGafuQ0bqCQJbBkRLtxIJADaB306TKgkBfgINz8MqCQE0dEpR8zoJAANC3tJvSgkAuNs+0MNOCQAMs9DV62oJAZxsANsbagkAD/idXIuKCQCqENBdy4oJAIB5A97vigkDIYUiX8OKCQENQZfgG6oJABtxzmGPqgkBaN3f4eOqCQHDqgnjD6oJAM0KLmPjqgkBZ76dZDfKCQGrRuTl/8oJAntTEWcXygkC9yuo6FfqCQOibB7vM+oJAMDGNWx/+gkBWwzv8dgKDQOsrSrzSAoNAXyR4nVUKg0B2C4qdxwqDQHzIuh5cEoNAu+xZf1EWg0CcWvN/IhqDQJJn/X9iGoNA5LoHQKQag0Bu2T/BZyKDQMbYTkHHIoNA1j6LAqYqg0AKqqIiOyuDQI5bzoOvMoNAiLki5SY7g0A5G1AGpkKDQNlRX+YGQ4NAOtFlRjBDg0CaOIQHUEqDQJS1k6eySoNAKeqb5+ZKg0A9LaLHDkuDQCmizEh7UoNATwPkKBBTg0C3FgeqTVqDQDZZC8poWoNALDIPSoFag0BCsRRKpFqDQMHoJkoYW4NAs7tMS2dig0BC61Rrm2KDQMDal8yjaoNAqqltblN2g0BXcRYvhnqDQBOwVRB3goNAz1tZcI6Cg0Bh8o8xSIqDQLgwl1F2ioNAzg7SUkuSg0BRQ+vS65KDQGyapjavqoNAqsUv+dS6g0Cxizd5BruDQNrcX1plwoNAJLhr2rDCg0AoQnQ658KDQEGKejoPw4NAaDeX+yPKg0CLwJw7R8qDQEEOpRt8yoNAOI6tO7LKg0CTVr27FsuDQB2/3/xP0oNAJzTlvHLSg0BKC/Q80dKDQKLcNt7Y2oNA1tZq/4Hig0D/hK3AiOqDQLuP5iFS8oNAYHL6wdDyg0DUNiIjLPqDQLrEbsRxAoRAC5GxRXkKhEDu57ZFmwqEQA4h9EZ/EoRAjD4Dh98ShEC8w3mJjiKEQInpgsnIIoRAMIHOSggrhEDs09ZKPSuEQPmVB+zRMoRAJ3oPLAQzhEBeuRlsRTOEQNlZLY0gOoRA7+dDLbA6hEA9WEot2TqEQFTxUu0PO4RAHdtcDU87hEA+b5nN0DyEQAU5fU57QoRAyAOEjqZChEClb4wu3EKEQLJ/xg+sSoRAkHsRsedShEBjeE4yylqEQC+KjlPAYoRAg6aZEwdjhEDTmoWU5WiEQHbw3LQRa4RAsqHCVchwhEAaLgfWfHKEQG8mn9gAg4RAyrsTOeeFhEAdW9558YqEQC0J6tk7i4RANlsV262ShEAAICobMpOEQGAJWJy0moRAcJJuHESbhECXwZqd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d+Q1Do07eEAiF+RO4j94QJswXs/rQnhAQ45pLzRDeEC8cnLPbEN4QIglfe+wQ3hAaleNDxhEeEBrv5kPZ0R4QHikpG+sRHhAkFmGsElKeEBDrqaQF0t4QGoArdA/S3hAADW1EHRLeEBeZ2Lxwk94QJR66REfU3hA7yj20W9TeEDEUAay1lN4QAJ7DVIEVHhAIzsSkiJUeEBXpimyt1R4QNSyI/PvWnhAbcov8zxbeEC3VzIzTVt4QE8nb5QuY3hA8fJ49GxjeEBwg4ZUw2N4QBmtizTkY3hAY+GSFBJkeEDm0mbWtW94QIIC6HbscnhAzTbvVhpzeEAOUwtXzXN4QIVTMtgje3hAi8Z4mUKDeEAbeJB52YN4QFQpu3pHi3hAgprEmoOLeEDcGgV8fJN4QPbVCZyak3hADDI13QybeEDyCWw+yKJ4QB92vd8sq3hA9tzFX2KreEDI2QLhRLN4QB+LCCFps3hAadkSwaqzeECwb0giXrt4QCg6TgKDu3hAJtlZAs27eEDQwojjVcN4QJofkSOLw3hAggiYI7fDeEAnN7Gktcp4QII5AUYR03hApioThoPTeED0qSomGdR4QAAkjChC43hANAMki8XzeEDBwUisDft4QG0CWMxu+3hAm/eLzRcDeUD15JAtNwN5QP9OpM2yA3lALPSzbRYEeUCyVbttRQR5QA8z0c4uC3lApHgF0NkSeUDY4xzwbhN5QD+cKfC/E3lAAOrvsK4YeUBLOWWxmRt5QFh3a3HBG3lAtDzH0QkeeUA1wJlSRiN5QEiQoRJ4I3lAzWSnMp0jeUDEi7Ty8CN5QKa9xBJYJHlAfJfLsoMkeUAkDdZzJCt5QHveGBUsM3lAF4Atda8zeUAk8jm1/jN5QDVHSrVmNHlAXm9eNkU7eUCZXWa2dzt5QGAklhcGQ3lA4wqmV2tDeUDM2amXg0N5QCkDrheeQ3lAF5uyV7tDeUCY2r33AkR5QBA04Ng7S3lAFW3meGNLeUD8jOx4ikt5QKZtcvneTnlA6MIeWihTeUBzQyk6a1N5QFp9MvqlU3lAjrRDmhNUeUDRfVl7/Fp5QFCbaLtcW3lAgxFy+5hbeUDeJ4u7OFx5QICymBztYnlA7qOrvGVjeUCAtrecsmN5QB672x32anlAIq3wfXtreUCX/P6d1mt5QMYtMr96c3lAnSE8H7pzeUBEdnCAZXt5QEvPs4Fwg3lAPvm5wZeDeUDTItDhJIR5QMbQAAO5i3lAaXyfY6uPeUCvuyIk75J5QDo8LQQyk3lAEIkyxFOTeUD9OjrEhJN5QH5GP+Skk3lA02JKpOuTeUDS9YUlxZt5QPh9rQYfo3lAAie5RmmjeUD/HsCmlaN5QLtxyKbKo3lAJr/PJvmjeUBZz+eH8Kp5QHBuKun2snlACYY26UOzeUD/rEOpl7N5QErhSonFs3lA+CtuagS7eUAIZ3uqWLt5QKBqvothw3lADttDjm/TeUCcg4Rvadt5QM+8sDDh4nlAzI/CsFLjeUD6gtuQ8eN5QNy067BY5HlAA236kRTreUCr2zGz0/J5QLG7PPMY83lA/HxFs1DzeUCeYlLTovN5QDCaU5Oq83lAM8tgk/7zeUBcF9H1hQN6QCYQ7LUxBHpAFkz8FZkEekBGbAN2xgR6QB91E7eKC3pA1MhVOI8TekB6BGU48BN6QCK7a/gaFHpAh+lvmDUUekCNvoi40xR6QKbqh5ksG3pAf1/DWgUjekBE2cfaISN6QPDLzbpHI3pA1P3d2q4jekDNYOq6/SN6QO5U9XpDJHpAXmYAHOgqekC2FwZcDCt6QPMcGBx/K3pAHqJGfQUzekARAFM9VDN6QNCoXR2YM3pAF0hqfegzekCVF3B9DTR6QEGxev1QNHpAmKOT/k07ekBhk9e/XEN6QEfN4H+XQ3pA2VLrf9pDekBeqQBgYkR6QKO8u6AJSXpAi9kNgRRLekCoQxDhI0t6QFflEwE7S3pA2Aoc4W5LekDyUiLhlkt6QLUDJmGuS3pAxWMogb1LekDcVSyh1kt6QMWXLgHlS3pAdwIzIQFMekA9YjThCUx6QOI1N+EbTHpAtZ844SRMekCyEnxh0k16QBun/uERUXpAlMdLAv1SekASPlaiP1N6QNtmWGJNU3pAu4FeQnRTekD4HmQCmFN6QJF1aKKzU3pA6zShI3tbekC0+9CECWN6QALU44SBY3pAlD/rxLBjekBGN/HE1mN6QGCOCGVrZHpAP5EmpohrekDJYVXnEHN6QLM/aseVc3pAK5dxh8RzekDAsXYH5XN6QOeqgecqdHpAmYqfSEd7ekCmb6qojHt6QEUZuKjje3pAuRHmiWaDekDth+/JooN6QLkG9Gm/g3pA5+r7qfGDekAu/QYqOIR6QB25IutGi3pAefQwi6GLekCjDzjLzot6QPDyPOvti3pAUdxqbHCTekCydXSMrZN6QGHYfwz2k3pAQQ2JrDCUekAWqrLNl5t6QFb87258o3pAR131rp6jekChRUKQ5qt6QBUZe5Gus3pA8hGFEe6zekCavZmxcbR6QIkrrDJFu3pAIsXH8vS7ekCJ8u0zRsN6QPW2ElQwxHpAVV0ptR7LekCPFyu1Kct6QE8ZMfVPy3pA17Y3FXrLekCskD61pct6QPrmQfW6y3pANI161oHTekAB3Jd2PNR6QDcdvdeH23pAWP3+eInjekDJ3Af5weN6QFWrGxlA5HpA+iUjuW/kekDJSDN51uR6QC24StrJ63pAI8uOe9nzekB0OJz7LvR6QDpzqNt89HpAzURzXIj5ekAZZ7V8Lft6QFwp+L00A3tA8gQFnoYDe0CbCRWe7AN7QBJhHF4bBHtA740sXoIEe0BWRDX/Fwt7QCUOSl+cC3tArRV4oB8Te0BjwJpg/BN7QHnMoUApFHtAUPSxIJAUe0DDtLoBJht7QPBuFePFI3tA1KAlAy0ke0Bs7DeDoSR7QPBGg6U9M3tAeL+U5awze0A3wZol0zN7QEERqwU7NHtAXXFrBgQ5e0A0v9smzzt7QL+EGEiwQ3tA/4hMqVlLe0ACcooKQlN7QIfTkQpxU3tARgmeyr5Te0A52qiqA1R7QI3OIS3CY3tAdCIurRBke0BTFaJPr3N7QNQgp2/Pc3tA+6azLx90e0Du0LlvRnR7QNRWyBABe3tA/g3i0KR7e0AKDwsSCIN7QLb2HtKGg3tAuWYkcqmDe0DqbCgSw4N7QJUiUXMki3tAeAGg1HiTe0Cf/sk0hJR7QJWEDPaJnHtA+Q0nF5Gje0CEGzPX3aN7QBD1OBcDpHtAuMVCl0Gke0Cos0m3baR7QKckRHioqntA7LtXOCWre0CQcJ/5S7N7QJHYq/mas3tAT5LimlW7e0AfgFPcgsR7QM78YRzfxHtA+o/DvgjUe0DQt9Oeb9R7QOsO6z4E1XtAJ6rsn2zbe0BKhzXBmuN7QP0LPaHK43tAJKxMIS7ke0B86lNBXOR7QFVzWCF55HtASw1kAcPke0CEyYAi2Ot7QC3fvOO083tARODRozr0e0AXftkja/R7QKVu6aPQ9HtAHz/kxA37e0DBcvokm/t7QKSQQSa+A3xA3ANS5iYEfEBQOV1GbgR8QG1Mf2elC3xAeem6KH8TfEBGgsKIrxN8QPHnxojLE3xApJXiyHsUfEByWDtLbSN8QGZ3T2vtI3xAY35na4YkfECpJmKMwip8QPBcye2xM3xAiU/gDUQ0fECiy+yNkzR8QHHD5I6+OnxAR3M+0FdDfECy2kgQmkN8QL+/U3DfQ3xA3ENZkAJEfEBdtWZRtkp8QLVQiFGMS3xAnuCT8dVLfECEc5gR80t8QG0fwpJaU3xA1ZjW8txTfEDyNt/SE1R8QKCrgVqxhHxAQY9zPy6kfEB68HnfVqR8QJ8Vkp/wpHxAWoCZAH6rfECYhavA8Kt8QFcL3OGDs3xADNvzgRu0fEA29vrBSLR8QDM8C2KwtHxAtWETQuS0fEDo1RgjZbt8QDXiMaMEvHxAedRb5G3DfEBwOmFEkMN8QAtPdMQJxHxA5Nd4pCbEfECHMITkbsR8QIMoi0SbxHxA/M2bRAXFfEAKAu2mxtN8QL0t+SYU1HxA4ZEJh3zUfEBL3xAHq9R8QDggNQjw23xAfOJ3SffjfEDw43wpF+R8QPCkhIlI5HxAKjG6qvvrfEDvfPJLwPN8QEpFAswk9HxAL4t/zv4DfUAz+4RuIQR9QD0Dxq8dDH1AvRo/Et0bfUDydkWSBRx9QK2bgbPiI31AHq+Qs0IkfUAegcTU6it9QIPJyzQZLH1AsCDSlEEsfUCVdvk1mjN9QNmlAPbHM31ATqcF1uczfUDj2w0WHDR9QHkQFlZQNH1AkTCKGPBDfUDpbpE4HkR9QEEvqBivRH1AyN/1GlpTfUCkWg9b/FN9QPtbOfxlW31AhxaE/Z9jfUDBuqG9XGR9QFjPEGDcc31AUosYoA10fUBT2SHgSHR9QMe1MeCtdH1AK1lPwch7fUCz15qiB4R9QIwhp+JVhH1AVpiy4p6EfUCPswQFZpN9QAkiFgXVk31AxhsjpSeUfUB4YTLliJR9QE+JQsXvlH1AqQNJBRmVfUCpElqlhZV9QN8BV0bQm31A0lqrh0ekfUDz27cnl6R9QML+x+f9pH1ARtAwqlW0fUBTtTsKm7R9QD15TSoMtX1AYsSXjKHDfUCta52MxcN9QLFopAzyw31Azse0TFrEfUAS97sMiMR9QJP9CK7QzH1AJA4RL2LTfUC9Cxpvm9N9QBHPKc//031A2uw5b2bUfUBFOkHvlNR9QNe/S+/X1H1A1iVUkGvbfUCTGI6Q3Nx9QE6sqVHq431AiVu5MU7kfUB/gsbxoeR9QPHu0FHk5H1AjjgnFMbzfUAaRjPUEvR9QJKDN9Qt9H1A/IO3NhkEfkAvP/O38wt+QNveN9kGFH5AnTx6mgscfkDkX7HbyCN+QLOCwZsvJH5AqU02ntMzfkBUYHnf3Dt+QIiDwWAGRH5AHUXLgEREfkBnvgSiEEx+QG57NSOlU35AsmBSI11UfkCoU1ljiVR+QJf/yoUZZH5ANnXSBUlkfkC0eN6FlWR+QH2iYmibdH5Au8xpCMl0fkAFT3ooMnV+QIqwgShhdX5A126RaMV1fkA1YosJ/Xt+QKBCzgoFhH5AG8viyoeEfkBL6+kqtYR+QEWN7qrShH5AgGHzavGEfkA1DBYrzoV+QFvABYzEi35An4JIzcuTfkBVq1vNRZR+QNMHY610lH5AoypzbduUfkDJi4pNcJV+QANei67Tm35Al0rET5yjfkAZ/c0P2qN+QBny2+8ypH5A7xnsz5mkfkBrrfKvw6R+QI42+O/mpH5AcA0JUbCrfkAizFBS17N+QBkNYdI+tH5ARHZxUqe0fkCx/3fy0LR+QNcUobM0vH5AJUjKNJnDfkBjGdZ05MN+QNRr3RQTxH5AXaX2tLPEfkC6jGU3MtR+QDU6b9dv1H5AaaWG9wTVfkDa9Yk4eNt+QIzo17nG435AAd/qeT/kfkBhePSZfOR+QCRSDHoU5X5AoQ9kfP/zfkA6dXm8h/R+QJKQph0F/H5AcX3gHtQDf0DISOkeDAR/QDAQB7/JBH9AYX4XXzIFf0BjqGiB8xN/QKDp1YNnI39Aupnog94jf0D7GfIDGyR/QBVi+ANDJH9AYkX9I2Ikf0ABoQHkfSR/QHDrD+TYJH9AhtQ8BVUsf0Cvb0+mKTN/QLCCf8ZbNH9Ao4eQJsg0f0AxOagGXzV/QNb0wmdnPH9AuM/ySPZDf0BOOAEJUkR/QIutdIvtU39AZBGEi09Uf0BOfJpL3lR/QCehsatxVX9AxpjI6wNWf0Ckg/6NF2R/QNKbDE5xZH9AXTYa7sdkf0CrtTGOXWV/QFxsO4/5a39AtB1Bzx1sf0AIf37QAnR/QPQWgxAgdH9AY+6S8IR0f0APbpqwtHR/QB/DqrAcdX9A+sjBcQ18f0A7AfxS3oN/QPHBAlMJhH9AJTgMk0WEf0BpZxNTc4R/QJbyHzPDhH9A/sQv8yeFf0CC75MVYpR/QN23o5XGlH9A4ywFeO+jf0CVGRlYbqR/QItaKdjVpH9A5c4MOX6qf0DuA4FawLN/QAxjkZootH9AHzOZWlq0f0CiwK063bR/QNussVtUu39AAZvKG/O7f0CA2Ba9NsR/QPS0Jr2bxH9AluWfv1vUf0CwYaw/q9R/QDRyDaLR439Ag0ogoknkf0Cc4C/irOR/QOyUisSq839A9KGUwywCgECdPpjDQwKAQFVB2IQ5CoBAqsXvRM8KgEDc6lLnAhqAQDuHVYcTGoBALpdYBycagEBlolzHQBqAQIkRX0dQGoBABL9o540agEBc/W8HvBqAQH1PAAhTHoBAr/agCFIigEAD+agIhSKAQIUv3akvKoBA80XlKWMqgECv8eiJeiqAQDAX8WmuKoBAta4ZCw8ygEA92SELQzKAQO/QJwtpMoBApXcrS4AygED4PFbM7jmAQDO4XywrOoBAnetj7EU6gEBgKWlMZzqAQP+EbQyDOoBAPU2iTTFCgEAwXaXNREKAQNs1qO1WQoBALziw7YlCgEBqdtzOAUqAQEKsH/ALUoBABV0jcCNSgEA4v2ORG1qAQCVxa5FMWoBAfFZ3UZhagEAuEaDS+WGAQPHBo1IRYoBApgS6Ep9igEDGFOOzAmqAQEIb6LMiaoBAEdbrczpqgEDQ1/GzYGqAQCGE99OEaoBAR1oo9RlygEA6hC41QXKAQMxiNJVmcoBAnGJqlhx6gEDc4nMWWXqAQOkMsbc8goBAhWC814SCgED51L/XmoKAQMgI/Fh4ioBACXU8unCSgEBqgUT6o5KAQK5XUFrvkoBAJuV4u0+agEA/LX+7d5qAQBnQhluomoBAaXO1fC+igEBwrLscV6KAQJQ1wVx6ooBAPIr1vSWqgEDXw/0dWqqAQL3jAx6BqoBAkycy3wWygEDAP0CfX7KAQCgubkDiuYBA4QV/gE26gECWxoWAeLqAQI+tvEE0woBAS+bBgVXCgEDk48rBjsKAQCAF+2IfyoBAzGr/YjvKgEDtRAdjbcqAQO14DeOUyoBAgwubYxrOgECrcTwkHtKAQL9BRORP0oBA+2jcxBjWgEBuz37lItqAQB3+g+VD2oBA5Wu45u/hgEAU8VyHB+aAQI3P/ecH6oBAxIr0CCvwgEBtJETpJfKAQMT1hoot+oBAAVSUqoL6gEAVWr0L5gGBQLc02AuRAoFA9QXkS9wCgUAO2+srDgOBQOMpDA06CoFA4a4UTXAKgUBi1BwtpAqBQD9RUY5QEoFAF2dXTncSgUAU0lzOmRKBQApsaK7jEoFAtiGRD0UagUBYYJmPeRqBQD6An4+gGoFAF8qrz+4agUB7+sqQEyKBQHUE3BCAIoFAG/Lh0KUigUA6HA4yHSqBQJGFRNPVMYFA9XRQ0yEygUBLcfCTHDaBQCip8rMqNoFA6FaHdN05gUDS0K7U2DqBQF274NV0QoFAzjgX9y1KgUCshLSXF06BQM7lVTgbUoFAJVhj2HBSgUA18qUZd1qBQGyKq7maWoFAT0/3WttigUBpWiDcPmqBQAdsOtzkaoFAo0Nw3ZlygUDN8bKeoHqBQLfFQL8nfoFAxfLsH3CCgUCPafgfuYKBQGrmLIFlioFA+RU1oZmKgUCky10C+5GBQMi8b0JtkoFAi/p0oo6SgUBQ53dCoZKBQPyrsUNvmoFA+Eq9Q7magUAKI0hkLZ6BQMP6KgYwqoFAoIA2ZnmqgUAbzG2nN7KBQOoTc0dZsoFAk3F+p6GygUDgZa+IN7qBQOtHSykYvoFAGs3vyS/CgUCm9P5JkMKBQPzbJSvmyYFAqUEqKwLKgUDz6C8rJsqBQIvMNatLyoFAMHJszAXSgUCbZnjsUdKBQAQUk8z70oFAA8zDLZDagUDMdtWtANuBQM82/65o4oFA1uIDb4bigUAapUawjeqBQAkGTPCv6oFASt9Q0M7qgUBrpN/wW+6BQI/U6dCc7oFARkxxcfvxgUBDXnuRO/KBQNJzgPFb8oFAUF2JsZTygUCRapQR2/KBQOtoxTJx+oFAd1zOMqr6gUDxJfazBQKCQPiSAtRUAoJABbcF1GgCgkBw6gmUgwKCQI37EJSwAoJAvVE5lQ8KgkCTuEEVRQqCQHaCRTVdCoJAo2ZNdY8KgkBf85WWuxKCQJ8CvBcMGoJAJy3EF0AagkBuWdJXmhqCQMOr/rgSIoJAEakGmUUigkCIwRW5pSKCQJxuQ7omKoJAb8Z/+qYrgkCI3JqbsTKCQEBdy5xEOoJAcCTXnI86gkCKbV+/r0qCQG34aj/5SoJA5w+cAJBSgkC6IKKgtlKCQGCdxGHwWYJAsH3QATxagkA8pd+BnFqCQAwmdYJUXoJAjD0cg3xigkBjvifDxWKCQIZ7M4MQY4JAsLJYpFtqgkBf+2BkkGqCQAfMauTOaoJAP5h2BBprgkDx36BlhXKCQG6b3UZmeoJAZ5wXyDWCgkCydyNIgYKCQCPbVqkmioJAMGdmqYmKgkCEZLYq5ZKCQIHv+AvrmoJAKRAn7W6igkChKDYNz6KCQJO8Y25PqoJAqlumz1WygkCqw7LPpLKCQOoV8HCJuoJARTf7UNC6gkDTXSxyZ8KCQO2GdzOkyoJAo1aP0zvLgkA5DhI0fM6CQBo9s5R+0oJA9BPBtNbSgkCsacI039KCQKKQz/Qy04JAywxV9YTWgkBJoYHVoNeCQJKa9PV82oJAbiAAVsbagkCuJDS3b+KCQBoZQNe74oJAlDlIl+/igkA2RmW4BuqCQP/wdjh36oJAEN56OJDqgkBe24IYw+qCQAYfi7j36oJAZ/mnmQ3ygkBq0bk5f/KCQJ7UxFnF8oJAlK3I2d3ygkA8dftaf/qCQOibB7vM+oJAj7OMOxz+gkDIVDs8dAKDQEmuSZzPAoNAt6F3XVIKg0AVwIm9xQqDQG++ut5bEoNAaTvKfr4Sg0BsSf2/YRqDQKIBQMFoIoNAi6tOIcYig0Bh1XkiNyqDQMIvi6KlKoNAEK+iQjsrg0DCqMNjazKDQBoBzkOtMoNANFjl40Ezg0C13CLFJzuDQB8HUIalQoNA2VFf5gZDg0AwdmNGIUODQCZgk4ewSoNACNGbR+ZKg0A9LaLHDkuDQDWszIh7UoNAl1/ZaMxSg0BXCORIEFODQB70CIpZWoNAVsAUqqRag0Cn1CbKF1uDQBvNVKuaYoNA8LeHDD1qg0AXRM5tXHKDQFdxFi+GeoNAmxlWsHmCg0C8TFkQjoKDQP+mj1FGioNAV3KYUX6Kg0AaI5zRlYqDQK710bJKkoNAWoTqEueSg0CgbmNVpaKDQOiB8PfjsoNAlk4jmYW6g0Cz7Ct5vLqDQJryLrnPuoNAqYY3WQa7g0CINsJ5eb6DQGkmazqtwoNA9Bl0OubCg0AVZ3paDsODQGunnJtGyoNARdelG4HKg0A0OKtbo8qDQIX+szvbyoNAA6vffE/Sg0DS8uQccdKDQH4z9DzS0oNACrYZPh/ag0CV0jae2NqDQNzbah+C4oNAOmSkoE7qg0CoB64AjOqDQITH+YHM8oNAKNU8o9X6g0BtcG/jF/yDQLO/bqRxAoRAEZaxZXkKhEDNzralmgqEQLUrbIYdD4RAKDX0xn8ShEBognnpjCKEQInpgsnIIoRAmE+/iqcqhEBepM4qCSuEQMy61qo8K4RA2XwHTNEyhEBBjg+sBDOEQPzxQ22wOoRAPVhKLdk6hEDzpVINDjuEQNUNhM6mQoRAaW27j2VKhEC7/73vdUqEQEbzxu+uSoRAnkL60FNShEDyxhGR6VKEQKARNXIoWoRAOJFNcsRahEAAkuuSsl6EQIBbiVOfYoRAvoWQ88xihECQsJlTB2OEQMy9LnS8ZoRAi2OFNORohECfStyUDWuEQDc6VlfSeoRAwAcW2fWFhECbpLU57omEQMmB6tk+i4RAlkRx+piOhEBQ+Pe68pGEQCpRFZutkoRA7BAquzGThECaNli8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+            </binaryDataArray>
+          </binaryDataArrayList>
+        </spectrum>
+        <spectrum id="controllerType=0 controllerNumber=1 scan=47" index="46" defaultArrayLength="94">
+          <cvParam cvRef="MS" accession="MS:1000580" value="" name="MSn spectrum" />
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+          </binaryDataArrayList>
+        </spectrum>
+        <spectrum id="controllerType=0 controllerNumber=1 scan=62" index="61" defaultArrayLength="95">
+          <cvParam cvRef="MS" accession="MS:1000580" value="" name="MSn spectrum" />
+          <cvParam cvRef="MS" accession="MS:1000511" value="2" name="ms level" />
+          <cvParam cvRef="MS" accession="MS:1000127" value="" name="centroid spectrum" />
+          <cvParam cvRef="MS" accession="MS:1000130" value="" name="positive scan" />
+          <cvParam cvRef="MS" accession="MS:1000528" value="101.10706517781338" name="lowest observed m/z" unitAccession="MS:1000040" unitName="m/z" unitCvRef="MS" />
+          <cvParam cvRef="MS" accession="MS:1000527" value="748.3660799920525" name="highest observed m/z" unitAccession="MS:1000040" unitName="m/z" unitCvRef="MS" />
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</binary>
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+            </binaryDataArray>
+          </binaryDataArrayList>
+        </spectrum>
+        <spectrum id="controllerType=0 controllerNumber=1 scan=118" index="117" defaultArrayLength="63">
+          <cvParam cvRef="MS" accession="MS:1000580" value="" name="MSn spectrum" />
+          <cvParam cvRef="MS" accession="MS:1000511" value="2" name="ms level" />
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+              <cvParam cvRef="MS" accession="MS:1000576" value="" name="no compression" />
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bCe9688reECnnF4M1C94QCAE4swYM3hAi4XvzG4zeEBug/lsrjN4QApZFE1ZNHhA930abYA0eEARHGitbjZ4QF7BJO4fO3hAYTEqjkI7eEAHbTmOozt4QBYBQi7aO3hA+/jjjuE/eEASnknPaEJ4QAYlau83Q3hA6eN776hDeEBqV40PGER4QFewma9mRHhAxuCk761EeEAVi6awFkt4QGT7rLA/S3hABoi+cK9LeECMimLRw094QJqz77FGU3hA2xn2cW9TeEDMVQbS1lN4QPx1DTIEVHhAxbgSsiVUeEC12h9SeVR4QCVLYPTPYnhADvVuVC1jeEDR2XhUbGN4QHYvixThY3hAauaSNBJkeEAhCqlV/Wp4QG8HsTUwa3hAOxO3tVZreEDQ/+9WH3N4QPSi+FZWc3hAZmj+FntzeEAvbAv3zXN4QOCZMpgle3hA1qY8mGV7eEB2y4a4PX14QFHYcBkQg3hAYq+Q2dqDeEDzSwE8ZJN4QMN5Axxyk3hAvKgJfJmTeEAA2BA8x5N4QHe8Gdz/k3hAgU09fUCbeEA8cnmeHaN4QEZ0gD5Ko3hAPSiP3qejeEC795TezKN4QLIEn94MpHhAuHGr/lukeEDye9FfrKt4QKRz11/Sq3hAp9oFAVizeEBJwBIhqrN4QJG4GuHcs3hAerskoRy0eEDQVEJCN7t4QIYVSUJiu3hAzvNNQoG7eECjXHHjwMJ4QBUXhYM+w3hAz0VIZBnIeEC5PstkW8t4QJtNAcYR03hAUoEG5jLTeEBlNwvmUNN4QPSpKiYZ1HhALco0x7faeECy7EMnGNt4QK+LTydi23hAwnuUSHfjeEB+aq/IIuR4QG7244nP63hAU9kMCzLzeEAQRhjLevN4QMyyI4vD83hAzAAty/7zeEBAXUgsC/t4QM4OYAyi+3hA4URwbWcCeUCtK4EN0wJ5QBxcjE0aA3lAjq6T7UgDeUBQx6NtrwN5QISWqA3OA3lAo2fZDmMLeUBcWwgw7BJ5QNjjHPBuE3lATMRLcJkUeUAOTlaxOht5QGNQXrFtG3lAHxZl0ZgbeUA+55XSLSN5QMcroZJ1I3lAad2nMqAjeUByUq3ywiN5QMSLtPLwI3lAk67EslckeUCgINHypiR5QBDKz5P8KnlADTXVEx8reUCFGd6zVyt5QMyE5JOAK3lAgrjps6EreUAgZBLVAjN5QLydGjU3M3lA9/4g1V8zeUBvViiVjjN5QG/9LDWsM3lAnx00ldkzeUCvlzl1/DN5QNkASvVkNHlAn21Y9h47eUB4RGYWdzt5QBBCb1awO3lA2Qiftz5DeUBUnKWXaEN5QDpJrXeZQ3lAngSz971DeUByvL03AkR5QN56ehi0SHlAyPzfeDpLeUCpL6BZAlB5QBzrHlopU3lAcHooOmZTeUCH3yp6dVN5QDwtM1qqU3lA5sk2WsFTeUCtN2tbbVt5QJPBmHztYnlAmmKrHGRjeUDrQre8r2N5QN5U1V3NanlAGLbb/fVqeUC2ihh/13J5QDRaHn/8cnlAo+MkHyZzeUBv/js/uXN5QIXyWoDcenlAKE+FQOp7eUDg8o8ALnx5QAPMuaGWg3lAjzLBwcWDeUBe4tJhNoR5QK8d9YJui3lAiZAVIz2MeUDB111jCY55QJ2kn2Osj3lATb4rhCiTeUC8oC2ENJN5QLxHMiRSk3lA3CE6JISTeUAw5UmE6JN5QOiU9iQ0mHlA7OBxRUWbeUDL+3clbJt5QAlahUXBm3lAD/2yBkKjeUApK7ZGVqN5QDaDv8aRo3lA8u/KhtqjeUD4g+en7qp5QCIyKmn1snlA3pNDCZezeUAWn0fJsLN5QJ48Tunas3lAs3IZ6ui4eUAfGocqo7t5QI/lxouXw3lAkycATWLLeUA4FQYNiMt5QAHLCa2fy3lA8P1CDmrTeUDac0vun9N5QM/4Ik/82HlAzW+FT2/beUBOCIxPmdt5QBZ2wFBF43lAvFjU8MPjeUCpfdoQ6+N5QEWd37AL5HlAr5Hr0FfkeUCIWwNyTet5QIvLCBJw63lAkpEQkqHreUBK9iKyFux5QEqQMdPR8nlAd2lH81zzeUAp1EsTefN5QJSuVHOx83lAjmpcs+LzeUAdAnHTZfR5QFWihtWrAXpAtDe21doCekA/FduVxQN6QK645PUCBHpAMxrs9TEEekDSdfC1TQR6QMgP/JWXBHpANF0DFsYEekAz8kL2WgZ6QCgaAHcPC3pA32sn1wkMekAm1y23Mgx6QPF8QlgUE3pAjRNlmPATekDuBWoYEBR6QFlTcZg+FHpAh7mImNMUekD0mYY5JBt6QNiBrJkVHHpAPi3DGgQjekDEqM3aRiN6QPQW3nqvI3pAAeLlGuEjekC5Uepa/SN6QKYd9RpCJHpAwyEGnAwrekCVUkmdFjN6QF4XXt2aM3pAa1VkncIzekC8AWq95jN6QMMVe31TNHpA7Ibgv5VDekADVO//80N6QBl8FME+S3pAuPEbQW5LekClfi5h5Et6QIe9S8L8UnpArh5jopFTekBApG2i1FN6QKSZs0PwW3pAL1vR5AtjekBQt+ikoGN6QIFk8eTXY3pAH8D1pPNjekC6RGrnlXN6QM4UcqfHc3pA9bSBJyt0ekCfAp6IPXt6QDyZwMgZfHpA2cLZKRiDekCsIekJeoN6QM1u7ymig3pAKPgGCjiEekDiCRML44p6QFGtHGsgi3pAWyIiK0OLekAGYzFLpIt6QDaQReyCknpAdAhWzOuSekCO92BsMZN6QFE1ZsxSk3pA3c9zbKmTekB1NYmsMZR6QKyomWyalHpAyF6hrSmbekCeE7Ntmpt6QCAw5E4xo3pAc0zvDnijekAp3Q4PQaR6QJQQE89bpHpArXAYMNyqekA/nSfQPKt6QEqJSjAbrHpApTCEUIqtekB3AI7xJrR6QNuJqBIuu3pAreP/c7jDekDxawKUyMN6QCjfElQxxHpALCojFJnEekDDczE1Ust6QEsROFV8y3pAovGLlvDTekBlY5d2OdR6QOqsttde23pAmFT0mEXjekBHg/mYZuN6QD4dBXmw43pAlVsMmd7jekA0UyPZcOR6QESoM9nY5HpAjnXeeRjpekDCf46b1/N6QDoLnNst9HpAiK+oW370ekDLMO+d+wJ7QJTB/V1YA3tAICgFfocDe0DvShU+7gN7QCZwHL4bBHtAHLEsPoMEe0D/u0MfdAt7QOuHTt+4C3tAvrJXP/MLe0DOyorAlhN7QBIUlUDYE3tAmuWh4CkUe0Bd/rFgkBR7QDKmzaGeG3tAGODWYdkbe0A+aP5CMyN7QIMzGIPXI3tAll42xPUqe0AK8VsE5St7QC5ieaX+MntAzPGD5UEze0CL2YZlVDN7QDFukcWXM3tAF6iahdIze0ADz7vGAzt7QM+BxuZHO3tAOgPU5p07e0B64acH40B7QM8UAmghQ3tANHcMiGNDe0C5fxgosEN7QDQtIsjtQ3tAdJMoiBZEe0CJhXEI50V7QGovT4lqS3tA9SJYiaNLe0BZsJEqcFN7QE30miqrU3tATUKkauZTe0BA36jKA1R7QGOEzOtEW3tAvYvUC3hbe0BqmN2rsVt7QCOV48vXW3tA/YZfDO1ee0BSxhbte2N7QK3nIc3CY3tAApEubRNke0CXL17OoGt7QLdiYS61a3tAqhlpTuZre0DnhIOv7HJ7QNrXnU+Uc3tAtymjL7Zze0CtAqevznN7QDiDsY8RdHtA/g3i0KR7e0AKkRrSaoN7QN2hIHKRg3tAUsw5sjGEe0DJeZ90dZN7QA0RszTyk3tAHGMm14yje0B4ETOX3aN7QK7fWdgyq3tAUO56WAWse0Ce7Z1ZQrN7QH3Jq5mas3tAqm67Of6ze0DoDdwaLLt7QELw7lqku3tA5C732ti7e0DKRSbcYsN7QNF+LHyKw3tAQ3g4vNbDe0DEgz3c9sN7QIf1SLw/xHtAJYVT/ILEe0AoD1xcucR7QG8fY31Ey3tAtoppXW3Le0By3NhekNR7QM3L+N+523tAwx01IZjje0AQjjshweN7QDG2TGEu5HtAdeVTIVzke0DaR15BnuR7QGwmZKHD5HtALTJ+osfre0DS/KmjPPN7QGRDvAOx83tAN8fAw83ze0CyNdLDPPR7QKIj2eNo9HtAtWj65Jr7e0DfVTVGcAN8QCl/Sgb3A3xAMw5Thi0EfEB+XF0mbwR8QPugfGeUC3xA7qWNxwAMfECeYZSnKwx8QMTaqugYE3xApwy7CIATfECd9M8oBRR8QL1yP2uHI3xAPgtGa7EjfEA7HVCL8SN8QIbTZiuCJHxAJ5J6DF4rfEByu4/M5Ct8QJl3vS1mM3xAdf3Ija8zfECPVOAtRDR8QIj4/85rO3xAzIY8kEtDfEDzDElQm0N8QF7NTvC/Q3xAvCpZ8AFEfEAEymVQUkR8QG1YgJFZS3xAgaqXEe5LfEAZ3sHyWFN8QMiO1rLcU3xA9XLe8g5UfEDb+vDyhFR8QLlKrRM0WXxABepGdWRjfEBPOFEVpmN8QF0SalVEZHxA54u4V/RyfEBZ/OE3/HN8QL/B+3j+enxAVY1eutGDfEB5Smp6HIR8QBoLgrqzhHxAmU+h+9iLfEBot+P83ZN8QJhHTB80o3xAiwJzvyqkfECVE4v/w6R8QNI9kp/xpHxAy62rwPGrfEB3JNyBhLN8QPLG8wEbtHxAPPv64Ui0fEBUVQsCsbR8QM5bEALRtHxAM6QXYv+0fEDKYCSjrrt8QH3ANqMjvHxAFRlWZEnDfECd+XOkB8R8QJM6hCRvxHxA3m6LBJ3EfEChh5uEA8V8QLNKrcXSy3xAS07wptvTfEDDMvlGFNR8QLRuCad71HxA8ZgQR6nUfEBCICGHEtV8QETiZamE43xAWwhwScXjfEAq93mJBOR8QCp5iUln5HxAmamUia7kfEDm+NvrMPN8QKhq58t583xAVGz+Swz0fEDFDipNgPt8QK9FOo3n+3xAm3tsboUDfUDexHbuxgN9QHeofG7sA31AMJG5b84LfUCacfxw1hN9QB5seZOuI31AT4yA89sjfUBj6YmTFyR9QBiqkJNCJH1An4HX1GMsfUDgdvqVoDN9QKZ9APbGM31Ab9oINvwzfUByCxY2UDR9QJXKPBelO31AySZDl807fUAKGks3ADx9QC3Of/itQ31AJxeJGOlDfUB79Js4YUR9QCabs/lVS31AHU/CmbNLfUBZpPi6a1N9QDkNCNvNU31ApGs7HHNbfUDoLX5demN9QENemt0tZH1AjZKhvVtkfUCb37gd8GR9QInLu95ga31AGOHAPoFrfUDqav+fbXN9QA5rIoBMdH1AKQEywK90fUCnBD5A/HR9QK3SmoIHhH1AAZaq4muEfUAoHLeiu4R9QJjH0GQbkn1AEXUfZRCUfUCldSElHZR9QIVrMiWJlH1ADiM8BceUfUA7ekJl75R9QLAiTOUslX1AMJqTR7CjfUB0Vpzn56N9QMVQq0dHpH1A3B26h6WkfUCO1sfn/KR9QJisHcrbs31ADKMwilS0fUB60zvKm7R9QM8jTQoKtX1ASOjqqva4fUAIaUyLY7t9QFbOYGvlu31AdNHBK0++fUBV34wsXMN9QJ3xl6yiw31AkMKijOfDfUCtrrSsWcR9QMu/u6yGxH1AEO15rUHJfUDYTlEunc59QBH/EM9h031ATpwWj4XTfUDg8TmPZtR9QP4CQY+T1H1AchFTsGTbfUCm1WUw3Nt9QDigonG9431AzEep0efjfUCMJLoxU+R9QK+K5bLF631ANlMbVHrzfUD8jSc0yPN9QOC/N1Qv9H1AELJy1QT8fUAZHqGWigN+QEP6rzbpA35AZNS3NhsEfkBuJMgWgwR+QKdoLpnKE35AIok2Wf4TfkAFbT05KhR+QJtiTdmPFH5AGA95GgQcfkD9/JO7DSN+QPTKpRt/I35Ab5Kye9AjfkCQ+btbDCR+QEIA0/ueJH5AthnXPBcrfkCfUOd8fit+QExS/vwQLH5AykFBXhk0fkAna0XeMzR+QJhiNuOqU35AMPxRo1pUfkDswVjDhVR+QMz6gOOFVX5AXY+zRYRjfkDEoLult2N+QBK4xkX+Y35ASSvXBWdkfkCONenl2WR+QDnC/ea6a35AkdGIZzBvfkAHFqVn5G9+QBXMMyhxc35ASTdLSAZ0fkA4NGMIn3R+QKe9aajIdH5AxRx66DB1fkDleJGoxXV+QB4ouEp4g35APgLASqqDfkAOJdAKEYR+QNAJ2gpQhH5AeBncKl2EfkAHvOJqh4R+QPQU7wrWhH5AFxHzau+EfkAYvBaL0oV+QHvZBSzFi35AxqBIjcyTfkD2KFztSJR+QEgJaI2UlH5A1lJzbdyUfkAT7dvPMqR+QOMP7I+ZpH5ANGP2T9ukfkBgRGEyQLR+QFCAcZKntH5AvQChMzS8fkDe9sYUhMN+QPH61FTdw35ARaTh9C3EfkA8feV0RsR+QEUrwPW2yX5A5W6XthHPfkBFV1rX6tN+QEL2Zdc01H5AIitvd2/UfkAT50XYxtl+QPMYm1jl235AAUPY+cjjfkDg0Nz55eN+QKJC6Nku5H5AsLT0GX7kfkA7Nf/5wOR+QCRfGbvF635AzxIn+xzsfkA090Dbwex+QGchXPzM835AId9pfCT0fkCICnWca/R+QC5GhJzM9H5AEGCsHSr8fkB0RuEe2QN/QBnB6L4IBH9AMBv53nAEf0B4hv++mQR/QHqrgaA0Dn9A5PJlQeITf0C1fYIBmBR/QP/lj2HtFH9AWN82ohQZf0AU906mJjN/QO0bZga6M39AnT955jM0f0Cjh5AmyDR/QCd+7sjaQ39Ar4MB6VNEf0DzqTGq5Et/QN/udCvvU39AV3qCa0VUf0C5CJpr21R/QKLxoGsHVX9A32mxS3BVf0CVdr0sG1x/QHRsziyHXH9A/Ob6jQBkf0AcggruY2R/QG27Ee6RZH9AhFQarshkf0BHbSouL2V/QP+dNs58ZX9AuqAxL7trf0ABn3OQvXN/QMQ5k9CGdH9A+16aULR0f0DfkKpwG3V/QD49+3LZg39AYlMCkwaEf0ArPQyzRYR/QIN7E9NzhH9AAn8fU8CEf0AY2S9zKIV/QD5sSXQpjH9AZN6MFTWUf0BBZJh1fpR/QMmoozXGlH9ANM4YeGykf0B4Syl41aR/QGBLltpHtH9AehIPPQXEf0CA8hl9SsR/QAjEJh2cxH9AX7GHn8HTf0CJ5pGfAtR/QEipnz9a1H9AL/2rv6jUf0BOhg0i0uN/QJydGMIY5H9A6pogokvkf0D2JjCiruR/QN+kjUS+839Ae1GUxOjzf0BxXp7EKPR/QHGhteS89H9Akr7UBIP1f0AMw9Wl5/t/QA62lEMtAoBAiWnYhDoKgECTEuTEhAqAQJa27+TOCoBAK64apj4SgEAe2CDmZRKAQOeCMmbWEoBAebFcJ0EagEDTnmGHYBqAQPGvaIeNGoBAylJwJ74agEC2BHgn7xqAQIX1nIg4IoBAbjef6EYigECyDatIkiKAQA+yMEnlJYBA1V87SSkmgEBeEd3pLiqAQCBp5QlkKoBAm+LoKXoqgED97vBprSqAQLuzGSsPMoBAMM8hy0IygEDMYSWLWTKAQL+LK8uAMoBA+XkzS7MygECJ7b3rJDaAQGrOVQzsOYBA0lJcjBU6gEDIRWPMQTqAQKHOZ6xeOoBABoptLIM6gEDZa/cs8T2AQOLsns0bQoBA62GkjT5CgEAFqqqNZkKAQDc9sA2KQoBA7vHmjkRKgEBwF+9ueEqAQFPh8o6QSoBA61MVEMpRgEDePiOwIlKAQP6LKdBKUoBANdxf0QJagEByrWsRTlqAQFFMnNLhYYBAeZ6iEgpigECwNqiyLWKAQFhgrZJOYoBAiFLoEyRqgEBEv/PTbGqAQF4NNHVkcoBAlV1qdhx6gEDI87AXPIKAQHzLSxgWhoBAxUrteBqKgEBaf/W4ToqAQEpt/Nh6ioBAI4k8OnGSgEBxhkQapJKAQO/ISDq/koBAbIrtWtiWgEBJk3PbLZqAQBnbeHtPmoBArg+Bu4OagEAwjoT7mZqAQEhrDzwOnoBA6PSxPBmigEBjbrVcL6KAQGOiu9xWooBAp0TBvHqigEBGLcdcoKKAQHMI+J01qoBAg4L9fViqgEBmZgRehKqAQK1ECV6jqoBA2NeYnjWugEAYVTNfDbKAQIxWOD8tsoBAKKpDX3WygEAbYUt/prKAQMNNc+ACuoBAb816oDK6gEBLU4YAfLqAQOjqE6EBvoBAM4cngX6+gECZLbQh/sGAQLohv+FDwoBAxl/FoWvCgEBmTVUiAMaAQJn09SL/yYBA45v7IiPKgECPjgEDScqAQO1EB2NtyoBAsnY8RB7SgEADfD3EJNKAQF72QwRO0oBAA+RJxHPSgEDsan5lINqAQKKeg4VB2oBA7HC4BvDhgEBNfcBGI+KAQNUax2ZN4oBA//dXKaTygED7jYwqUfqAQDyBlMqD+oBAFZeaiqr6gEA0VDALZP6AQFm9yks7AoFAaarOS1QCgUCdINiLkAKBQKUQX8zrBYFAbvpo7CoGgUCYFXAsWAaBQJn1BC0MCoFAlmAKrS4KgUDHmhTNbwqBQNrdGq2XCoFA/mYg7boKgUDekaLN9w2BQBczUc5PEoFA901XrnYSgUAb11zumRKBQGoY504KFoFA07CITw8agUBVvI1vLxqBQHKzka9IGoFAN0eZ73gagUDJJZ9PnhqBQLAroo+xGoFAMW3IUAMigUBV9s2QJiKBQHUE3BCAIoFA7EHgEJsigUDFcwSy3ymBQMkXENIpKoFAW/YVMk8qgUAXLxtycCqBQC0hH5KJKoFABVmrcgYugUC62rnSYi6BQO8hR3PmMYFAdBBQUx8ygUBh3FoTZDKBQBY7j7QPOoFAfkyXFEM6gUCemZ00azqBQI76onSNOoFAzMuutNg6gUBNGMeV0UGBQM/k0xUjQoFALA7YlT1CgUBj/9iVQ0KBQKPpCTfZSYFAkM8XtzFKgUBwdx93YkqBQCJhlvkTWoFAaCDgukdigUB16+daeWKBQCEs93raYoFAaVog3D5qgUC2Vyi8cWqBQGVyZJ1OcoFAw1xwfZpygUARs3O9r3KBQK8FoX4ueoFABFayvpx6gUB7k7a+t3qBQCCd2l/7gYFABiXtX3GCgUDJlvg/uoKBQC7ve6D+hYFAUFAdQQKKgUAJgSnhT4qBQFDSLAFlioFA5gY1QZmKgUAz6jlhuIqBQGysvsEFjoFAE65fAgeSgUDOjWniRZKBQM7Bb2JtkoFANtN3wqCSgUB316sjSpqBQMJ+sSNumoFAvh29I7iagUDit+4kUqKBQNhR+gScooFAy/8qJjCqgUDOiTOGZqqBQFlJNgZ4qoFAM0rD5vmtgUA7l2QH/bGBQBfPZicLsoFA699sxzGygUD+InOnWbKBQC+irwg5uoFAO+C1yGC6gUC9bcqo47qBQHpDTckkvoFA5gNTaUm+gUBEpd/pyMGBQMa6PSt+yoFA6Bvfy4HOgUD66HfMTtKBQB2MgMyF0oFAB3WHzLHSgUD2CZOM+9KBQP66IS2I1oFAa/OvzRHagUD6mdWNAduBQE9eUE4P3oFAkdjxjhPigUDc5wOPhuKBQEr+Cw+64oFAHRVMULDqgUAFvVZRUvGBQAyhgBFd8oFAU5mI0Y/ygUAmqo5xtvKBQKo2xfJv+oFAh7zQUrn6gUCGWv7zOQKCQGM5BbRlAoJA1P4KdIoCgkBMyRBUrwKCQNvukbTlBYJAi4WjtFUGgkAEiTn1EAqCQJm9QTVFCoJAUrpHVWsKgkDKhE01kAqCQN7HUxW4CoJAAOB1Vu8RgkDXlIcWYBKCQFshvpcZGoJAJy3EF0AagkAnItL3mBqCQMS5X5geHoJAZeoGOUcigkCLyQ5ZeSKCQJPIpjlBJoJAki1EeisqgkC1nEb6OiqCQLwuSPpEKoJAQch0+mArgkC9znn6gCuCQH2WEXtHL4JA8o2Pm2kygkCy1MccLjqCQN6uX1+xSoJATyyWgGpSgkC77Jsgj1KCQP/Cp4DaUoJAlmnQgTtagkCUCNyBhVqCQCIe4eGlWoJAsMDnIdBagkDG1HFiP16CQH/lEgNBYoJAcykcA3xigkD7UyQDsGKCQNHUL0P5YoJA3dVYhFxqgkCaQmREpWqCQDoqjIUBcoJA8MWdpXFygkD2GKcFrXKCQPqIrKXPcoJAOo3gBnl6gkCSWOkGsXqCQLn6E6gegoJApW0jCIGCgkAQLimopYKCQBNwYmlwioJAsCHzyQmOgkDMfZRKDZKCQHcXn8pQkoJAis2jym6SgkDGwDUrEJaCQMcI1ysTmoJAAt3b6zGagkDcmeZLdpqCQFAuJ61vooJA9DtqzniqgkBPq37u+qqCQLqLwe8Cs4JA/tbmkE66gkBTQfuQ0LqCQGPvBvEau4JAyKCFsUG+gkB7rCYyQ8KCQAegLzJ8woJAP1I4krPCgkDX9kVyCsOCQMDFSbIiw4JAlYdos0TKgkBRdoMz8MqCQJYyjNMny4JABDGstFHSgkDDZrh0n9KCQLYdwJTQ0oJAyWDGdPjSgkDkNjm109WCQOMS9JV52oJA2az/dcPagkAhMgkWANuCQApFj9ZV3oJA3C0x11zigkDSxzy3puKCQC2HdThu6oJAQ5N8GJvqgkCk1aX5//GCQDZ1s7lW8oJAh1W/WaLygkCQysQZxfKCQN4mAvup+oJA7qAH28z6gkD7D3e9TgqDQF/ruZ5WEoNAeWfGHqYSg0BLIex/9BmDQDRY/L9bGoNA3A4DgIYag0CpaBJA6BqDQA2ZMQENIoNAlRFDQXwig0ArlFTB6yKDQDfEywOfMoNAR8L7xC46g0C1EkRmWUKDQM5AR6ZtQoNAsT5RRq1Cg0CRGl+GBUODQG2Xk+exSoNAqIWbZ+RKg0BW38/oj1KDQHAn1ui3UoNAk7DbKNtSg0AvohTqo1qDQBksuEq1XoNAkL9I601ig0Cz1U8Le2KDQD88VyuqYoNARY9gi+Vig0DAjI6MaGqDQAQvlGyMaoNAKAaj7Opqg0CCtsrNRXKDQC732e2mcoNABt8Tz3V6g0B1Thevi3qDQF4uR7AagoNAryhWEHqCg0CYnl7wr4KDQIfciXEhioNAZ1SqMfCKg0AfkSoU3ZqDQMTzSRUDooNAPz1mNbeig0BJ9502eKqDQExno9aaqoNAra3rN8Wyg0D7PS+Z0bqDQJ18NxkGu4NAFApgembCg0ArvWv6sMKDQA0UcfrSwoNA+1J62g3Dg0An+qSbe8qDQO1OtDvdyoNAccHn/ILSg0BeGvSc0dKDQN/dKR6G2oNAgsM2Ptjag0Bx3GzfjuKDQLuDct+y4oNA9uR4f9vig0AzDOPBO/KDQFoF7qGB8oNAM0/64c/yg0CLjQEC/vKDQO6yLqN7+oNAAnhEQwb7g0Aj/W9jG/yDQKrxbYRsAoRAgLFxZIQChEDa2LblmgqEQF/7xUX7CoRAaIzp5jsShEDuB/SmfhKEQB6b+SaiEoRACfGWB4wWhEAeSDhojxqEQChKPwi8GoRA4+xraTYihEBlB4IpwyKEQGiRion5IoRAFLiW6UYjhEDZgb/KqCqEQGtgxSrOKoRAeJPZyk4rhEB+NgeMzzKEQJiYEEwLM4RA/NdArZw6hEAJFkdtxDqEQG7rT638OoRAbaOADpFChEADTPLOZEWEQBcbYZCEToRA9KX20DxShECU3AWxnVKEQDuQnbFjVoRAnXuh8zhjhEDkQb5UTmqEQPvAw1RxaoRA9A8HFnxyhEC9LRe24nKEQBTlVpfWeoRAABuJeHSChED0LxbZ9oWEQI7YFJuqkoRA36RXHLKahEChmHK8XZuEQGN/l92mooRAwU+g/d6ihECkKLW9Y6OEQLsc1P6GqoRASb/aPrGqhEAF+N9+0qqEQC9YGQCesoRAgHcdQLiyhED7nV+hu7qEQPEdaMHxuoRAO+WqIvnChECwcP3CBsWEQETzJQXF0oRAE1dJhgTahECysk1GINqEQPw/UIYw2oRAALBVJlPahEDFKVqmb9qEQP3BX0aT2oRAkoNpZtHahEDIB6bnsOKEQF1C6Mi06oRAvq0lCpryhEAxs47KNvWEQM4tZYuM+oRAlDRr67L6hEAlXMIMPAOFQJVVE60/BYVAigP/bRwLhUCDti+vsBKFQBT9QQ8lE4VAyppuUJ8ahUAhv3KwuRqFQGV7e1DxGoVAFTeCMBwbhUDJIrix0SKFQNBbvlH5IoVAs4T3csMqhUCpXfvy2yqFQH7EA3MRK4VA6boqtGcyhUCUVDU0qzKFQPM+QRT3MoVAEMNGNBozhUAg23m1vTqFQFfBiJUcO4VAAALdFTU9hUAF57aWoEKFQNW7vRbMQoVAbf74l6NKhUDYqjUZhFKFQKMvdFpwWoVApoC+u6dihUDxVhK9G2uFQBHyIR1/a4VA6qVVfiZzhUAzieRetHaFQNacj7/1eoVAkruRPwN7hUDgF88g6IKFQOGEZQGmhoVA3K0DIpWKhUDPfg4C2oqFQNYqE8L3ioVAgZAXwhOLhUDf5ErDuJKFQCBlVEP1koVAGT16ZESahUDmyo+kzZqFQDomkwTjmoVAt2iXJP6ahUBP9bxlS6KFQCY30AXGooVAGxYOJ66qhUAJrhJny6qFQPvXGKfyqoVAsPdUqM+yhUDfBEOqGb+FQASzDyyPyoVA42BRjY/ShUA+G7vNMNWFQE51mg6/2oVAX/v8bjLdhUBRFO6vMeOFQBl9ajIG84VAp57j1MUChkDEKCOWuAqGQAE5J3bSCoZAOByZ+GMahkDU17AY+xqGQAqQ8xkCI4ZAlYP8GTsjhkCfIzFb6CqGQAPLbbzIMoZAHRN0vPAyhkCBbKfdlTqGQLhsuX0IO4ZAUHD8XhFDhkBuNxmfyEOGQGVFjv+xRoZApNwrgJ1KhkBQQjCAuUqGQHoePyAYS4ZA4FHNoKFOhkAkZ9Ggu06GQBRV2MDnToZAwuh6AfNShkAJrXxB/lKGQBflGsLtVoZAIfpRgkxYhkBTzboC6FqGQHMawSIQW4ZAH/n94/FihkC9zTpl02qGQJ8+QyUJa4ZAO719xttyhkDAq4amFHOGQCi9jgZIc4ZA9y/DJ/R6hkDwXsmHG3uGQJ+n0UdQe4ZAbrL5aK2ChkDgOAeJA4OGQBA/Cykdg4ZAvUsUyVaDhkC8zz6qw4qGQBBfSIoAi4ZANjDBLL6ahkAzkNSMOZuGQDIjEA4To4ZAYwY673uqhkC+EWGPdKuGQMfhfNCDsoZAJrKF8LuyhkDkVdhRKLuGQDLg4RFlu4ZANwS0Mp/AhkClALnyvsCGQJxmvlLhwIZAhrD+snrChkBTTpDzGcaGQCzXlNM2xoZAAligE4DGhkCFBEKUhcqGQImsbDSVy4ZACnwW+OjihkCfsB44HeOGQAa0lxrc8oZAvtDam+X6hkDaB1mexQqHQGAQZT4SC4dAQqycf9ISh0B/fai/HROHQN0zrh9CE4dADZ9PAEYXh0CF++Cg4xqHQODD8CBIG4dAI4e1hEczh0A6r9pFkjqHQPNH8+UuO4dA0rIdJ5tCh0D5BCRnw0KHQMEzYMigSodAgZ1yCBZLh0CuYr8JXVOHQFkTMOzmYodAdh9/bTxrh0AqsrmOD3OHQC27NFHbgodA2uFAsSiDh0AkqYMSMIuHQEecsHOskodAdz9JtjSjh0CKboZ3GKuHQLoBjPc7q4dA3qrOmEKzh0Afig0aMbuHQJ3SS9sbw4dAblfSvTDTh0AkxRf/SNuHQAZHTID14odAboxaYFDjh0CFNo/h/eqHQNnfm4FO64dAdCrQovnyh0AdVNWCGvOHQCWLZMVmA4hAfRliqHEWiECLPJ4LCyuIQD375QwyM4hAJGn1TJQziEBkUybuKTuIQH67aU81Q4hA2Khur1RDiEA58dExiVKIQFP635HiUohAdm8cs8FaiEAzo2l0C2OIQAf2qNX8aohAumCt9RhriEDcKS34AnuIQPZT+ts3k4hAR0lRvb+biEASE8I/SquIQIPE/uAqs4hAx/MFoViziECqTCbChLqIQCUPe6P+wohAFJC9RATLiEB7P/NFuNKIQHqKSEwM+4hA4JcaUGATiUA0xVHRHRuJQO46kLIJI4lA1z2ackkjiUDh5qWykyOJQFUEyXPRKolAexfXEysriUAN9txzUCuJQLkc6dOdK4lADRYa1TMziUCp3CMVcjOJQACoLBWqM4lA7cNbNjQ7iUBk89C42kqJQF6K4xhRS4lAUNQmultTiUDX21T73lqJQObu/ZsTX4lAPIORXL9iiUA2nLN8mGOJQDIJ1B3FaolAOBxM3x90iUA4E3XggnuJQCGYjmAlfIlAB0exYWCDiUADuPCCUouJQIvoMiRWk4lAGEmkZuSiiUBqFefn66qJQOEJg0qJu4lAtyi8K1PDiUAhCf8sW8uJQDHXR+6I04lA8PiKj5LbiUAYWw3Q0N6JQCd5qJCs4olAMGsFklrriUDy0qB09PuJQFau41X8A4pAPyom1wEMikAYYGn4CxSKQHxCf3n1GopA/AvYv19DikCIBRthaEuKQBJefCcJdIpAch6WSAt7ikAUHqYocXuKQKxG3uk0g4pAWIftCZaDikBHLSWLVouKQKjxXSwek4pAjjGhjSibikCbiiwwXKuKQKkmc7ZS04pAF331+EzjikCstzfaUOuKQAD6uZxK+4pAtDatfVcBi0Ce9wp+rAOLQEPRRx+OC4tAx8WKoJYTi0DxbZPAzROLQJJB8uLlIotA5uCOhYczi0B+lsgmVTuLQHjf0UaQO4tAwlgLaFxDi0BUURSIlUOLQH6xTQlhS4tA+F5XqZ5Li0Bq9pCKa1OLQElFneq5U4tA/PTTS3Rbi0ADXjf3+KOLQBYlaLiNq4tAsWSquZGzi0AOYOJaVLuLQBfrtH6r04tALor337Hbi0BugzkhtOOLQAwv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\ No newline at end of file

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/test-data/SmallCalibratible_Yeast-calib.toml	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,2 @@
+PrecursorMassTolerance = "±3.7699 PPM"
+ProductMassTolerance = "±8.4670 PPM"

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/test-data/SmallCalibratible_Yeast.mzML	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,8555 @@
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+  <mzML xmlns="http://psi.hupo.org/ms/mzml" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://psi.hupo.org/ms/mzml http://psidev.info/files/ms/mzML/xsd/mzML1.1.0.xsd" id="SmallCalibratible_Yeast" version="1.1.0">
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+      <fileContent>
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+          <userParam name="Thermo/Xcalibur peak picking"/>
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+          <cvParam cvRef="MS" accession="MS:1000511" name="ms level" value="2"/>
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+      <offset idRef="controllerType=0 controllerNumber=1 scan=49">499463</offset>
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+      <offset idRef="controllerType=0 controllerNumber=1 scan=141">1411929</offset>
+      <offset idRef="controllerType=0 controllerNumber=1 scan=142">1419044</offset>
+    </index>
+    <index name="chromatogram">
+      <offset idRef="TIC">1441766</offset>
+    </index>
+  </indexList>
+  <indexListOffset>1445342</indexListOffset>
+  <fileChecksum>9193c5186ed5d828310b72d8c3f2233a88a2afc4</fileChecksum>
+</indexedmzML>

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/test-data/SmallYeast.fasta	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,1187 @@
+>sp|P38013|AHP1_YEAST Peroxiredoxin type-2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=AHP1 PE=1 SV=4
+MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSP
+TCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGC
+AFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL
+
+>sp|P46672|ARC1_YEAST tRNA-aminoacylation cofactor ARC1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=ARC1 PE=1 SV=2
+MSDLVTKFESLIISKYPVSFTKEQSAQAAQWESVLKSGQIQPHLDQLNLVLRDNTFIVST
+LYPTSTDVHVFEVALPLIKDLVASSKDVKSTYTTYRHILRWIDYMQNLLEVSSTDKLEIN
+HDLDLPHEVIEKKKKAPAGGAADAAAKADEDVSKKAKKQDHPRGKPDEETLKKLREEAKA
+KKAAKKAANAKQQQEQQNKAPEKPKPSAIDFRVGFIQKAIKHPDADSLYVSTIDVGDEEG
+PRTVCSGLVKHFPLDAMQERYVVVVCNLKPVNMRGIKSTAMVLCGSNDDKVEFVEPPKDS
+KAGDKVFFEGFGDEAPMKQLNPKKKIWEHLQPHFTTNDGLEVIFKDEEEKDHPVRKLTNA
+KGESFKVASIANAQVR
+
+>sp|Q01389|BCK1_YEAST Serine/threonine-protein kinase BCK1/SLK1/SSP31 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=BCK1 PE=1 SV=1
+MPFLRKIAGTAHTHSRSDSNSSVKFGHQPTSSVASTKSSSKSPRATSRKSIYDDIRSQFP
+NLTPNSTSSQFYESTPVIEQSFNWTTDDHISAGTLENPTSFTNSSYKNDNGPSSLSDSRK
+SSGGNSVNSLSFDKLILSWDPTDPDEWTMHRVTSWFKFHDFPESWILFFKKHQLFGHRFI
+KLLAYDNFAVYEKYLPQTKTASYTRFQQLLKKTMTKNVTNSHIRQKSASKLKSSRSSSES
+IKSKLKNSKSQEDISNSRSTSESALSPTKSGPSKTDEKNFLHSTSTHQKTKSASSLYRRS
+FISLRGSSSSNASSAKSPSNIKLSIPARPHSIIESNSTLTKSASPPASPSYPSIFRRHHK
+SSSSESSLLNSLFGSGIGEEAPTKPNPQGHSLSSENLAKGKSKHYETNVSSPLKQSSLPT
+SDDKGNLWNKFKRKSQIGVPSPNTVAYVTSQETPSLKSNSSTATLTVQTADVNIPSPSSS
+PPPIPKTANRSLEVISTEDTPKISSTTASFKETYPDCINPDKTVPVPVNNQKYSVKNFLL
+DQKFYPLKKTGLNDSENKYILVTKDNVSFVPLNLKSVAKLSSFKESALTKLGINHKNVTF
+HMTDFDCDIGAAIPDDTLEFLKKSLFLNTSGKIYIKDQMKLQQKPKPAPLTSENNVPLKS
+VKSKSSMRSGTSSLIASTDDVSIVTSSSDITSFDEHASGSGRRYPQTPSYYYDRVSNTNP
+TEELNYWNIKEVLSHEENAPKMVFKTSPKLELNLPDKGSKLNIPTPITENESKSSFQVLR
+KDEGTEIDFNHRRESPYTKPELAPKREAPKPPANTSPQRTLSTSKQNKPIRLVRASTKIS
+RSKRSKPLPPQLLSSPIEASSSSPDSLTSSYTPASTHVLIPQPYKGANDVMRRLKTDQDS
+TSTSPSLKMKQKVNRSNSTVSTSNSIFYSPSPLLKRGNSKRVVSSTSAADIFEENDITFA
+DAPPMFDSDDSDDDSSSSDDIIWSKKKTAPETNNENKKDEKSDNSSTHSDEIFYDSQTQD
+KMERKMTFRPSPEVVYQNLEKFFPRANLDKPITEGIASPTSPKSLDSLLSPKNVASSRTE
+PSTPSRPVPPDSSYEFIQDGLNGKNKPLNQAKTPKRTKTIRTIAHEASLARKNSVKLKRQ
+NTKMWGTRMVEVTENHMVSINKAKNSKGEYKEFAWMKGEMIGKGSFGAVYLCLNVTTGEM
+MAVKQVEVPKYSSQNEAILSTVEALRSEVSTLKDLDHLNIVQYLGFENKNNIYSLFLEYV
+AGGSVGSLIRMYGRFDEPLIKHLTTQVLKGLAYLHSKGILHRDMKADNLLLDQDGICKIS
+DFGISRKSKDIYSNSDMTMRGTVFWMAPEMVDTKQGYSAKVDIWSLGCIVLEMFAGKRPW
+SNLEVVAAMFKIGKSKSAPPIPEDTLPLISQIGRNFLDACFEINPEKRPTANELLSHPFS
+EVNETFNFKSTRLAKFIKSNDKLNSSKLRITSQENKTE
+
+>sp|P07267|CARP_YEAST Saccharopepsin OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PEP4 PE=1 SV=1
+MFSLKALLPLALLLVSANQVAAKVHKAKIYKHELSDEMKEVTFEQHLAHLGQKYLTQFEK
+ANPEVVFSREHPFFTEGGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSN
+ECGSLACFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQDFAE
+ATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEKRFAFYLGDTSKDTE
+NGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEGIGLGDEYAELESHGAAIDTGTSLI
+TLPSGLAEMINAEIGAKKGWTGQYTLDCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGS
+CISAITPMDFPEPVGPLAIVGDAFLRKYYSIYDLGNNAVGLAKAI
+
+>sp|P29547|EF1G1_YEAST Elongation factor 1-gamma 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=CAM1 PE=1 SV=2
+MSQGTLYANFRIRTWVPRGLVKALKLDVKVVTPDAAAEQFARDFPLKKVPAFVGPKGYKL
+TEAMAINYYLVKLSQDDKMKTQLLGADDDLNAQAQIIRWQSLANSDLCIQIANTIVPLKG
+GAPYNKKSVDSAMDAVDKIVDIFENRLKNYTYLATENISLADLVAASIFTRYFESLFGTE
+WRAQHPAIVRWFNTVRASPFLKDEYKDFKFADKPLSPPQKKKEKKAPAAAPAASKKKEEA
+KPAATETETSSKKPKHPLELLGKSTFVLDDWKRKYSNEDTRPVALPWFWEHYNPEEYSLW
+KVTYKYNDELTLTFMSNNLVGGFFNRLSASTKYMFGCLVVYGENNNNGIVGAVMVRGQDY
+VPAFDVAPDWESYDYAKLDPTNDDDKEFINNMWAWDKPVSVNGEPKEIVDGKVLK
+
+>sp|P43616|DUG1_YEAST Cys-Gly metallodipeptidase DUG1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=DUG1 PE=1 SV=1
+MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFHD
+IKMVDLGIQPPPISTPNLSLPPVILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFK
+LVIDEAKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDE
+LIKKEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGV
+VAEPMIDLMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKT
+SLYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPAKVFGKFSIRTVPDMDSEKLTS
+LVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFNAQFTAAKKATKLVYGVDPDFTREG
+GSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQYYSESPE
+N
+
+>sp|P02994|EF1A_YEAST Elongation factor 1-alpha OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TEF1 PE=1 SV=1
+MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVL
+DKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGV
+GEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVG
+YNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPT
+DKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQG
+VPGDNVGFNVKNVSVKEIRRGNVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLD
+CHTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVKFVPSKPMCVEAFSEYPPLG
+RFAVRDMRQTVAVGVIKSVDKTEKAAKVTKAAQKAAKK
+
+>sp|P16521|EF3A_YEAST Elongation factor 3A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=YEF3 PE=1 SV=4
+MSDSQQSIKVLEELFQKLSVATADNRHEIASEVASFLNGNIIEHDVPEHFFGELAKGIKD
+KKTAANAMQAVAHIANQSNLSPSVEPYIVQLVPAICTNAGNKDKEIQSVASETLISIVNA
+VNPVAIKALLPHLTNAIVETNKWQEKIAILAAISAMVDAAKDQVALRMPELIPVLSETMW
+DTKKEVKAAATAAMTKATETVDNKDIERFIPSLIQCIADPTEVPETVHLLGATTFVAEVT
+PATLSIMVPLLSRGLNERETGIKRKSAVIIDNMCKLVEDPQVIAPFLGKLLPGLKSNFAT
+IADPEAREVTLRALKTLRRVGNVGEDDAIPEVSHAGDVSTTLQVVNELLKDETVAPRFKI
+VVEYIAAIGADLIDERIIDQQAWFTHITPYMTIFLHEKKAKDILDEFRKRAVDNIPVGPN
+FDDEEDEGEDLCNCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQ
+VDGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMP
+ISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDS
+VFLDNVCEYIINYEGLKLRKYKGNFTEFVKKCPAAKAYEELSNTDLEFKFPEPGYLEGVK
+TKQKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLP
+TSGEVYTHENCRIAYIKQHAFAHIESHLDKTPSEYIQWRFQTGEDRETMDRANRQINEND
+AEAMNKIFKIEGTPRRIAGIHSRRKFKNTYEYECSFLLGENIGMKSERWVPMMSVDNAWI
+PRGELVESHSKMVAEVDMKEALASGQFRPLTRKEIEEHCSMLGLDPEIVSHSRIRGLSGG
+QKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLT
+EEVWAVKDGRMTPSGHNWVSGQGAGPRIEKKEDEEDKFDAMGNKIAGGKKKKKLSSAELR
+KKKKERMKKKKELGDAYVSSDEEF
+
+>sp|P53911|EAF7_YEAST Chromatin modification-related protein EAF7 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=EAF7 PE=1 SV=1
+MVVHWTIVDEIRLLRWASEFKPAGIHKHFHMFCIVERMNSPDKYPVTLLQKETMKLGKVF
+TAKDIWDKLSQSYNLEKIDEMENTYSLEATTESSRNGNGNGDDAEIHEETLLELNNRIRV
+RKQDFTLPWEEYGELILENARKSPNSNEEYPRVEDMNEKDSTIPKESPSTDLKNDNNKQE
+KNATIKVKELPEYHTEENDSPIDVQKEPIKEVQSDEKELQREHMSEEEQKMKSTNKTAAP
+VRKSQRLKRSKEVKFEDEEKEEIEEDNTKDEEQKEKKEEIQEPKITHNEEVDKEKNENEE
+GDDEREKSTSYENTNGSESEGVDEGVDEELGYESEREAEGKGKQIESEGGNLKKKTENKK
+GDDQQDDTKKDSKDKNEPLAKRTRHSSSTGNTSNETSPKRKRRKAGSRKNSPPATRVSSR
+LRNKK
+
+>sp|P00359|G3P3_YEAST Glyceraldehyde-3-phosphate dehydrogenase 3 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TDH3 PE=1 SV=3
+MVRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVSH
+DDKHIIVDGKKIATYQERDPANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVIT
+APSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSLT
+ATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSV
+VDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQ
+LSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA
+
+>sp|P00358|G3P2_YEAST Glyceraldehyde-3-phosphate dehydrogenase 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TDH2 PE=1 SV=3
+MVRVAINGFGRIGRLVMRIALQRKNVEVVALNDPFISNDYSAYMFKYDSTHGRYAGEVSH
+DDKHIIVDGHKIATFQERDPANLPWASLNIDIAIDSTGVFKELDTAQKHIDAGAKKVVIT
+APSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSMT
+ATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSV
+VDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSNSSIFDAAAGIQ
+LSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA
+
+>sp|P24583|KPC1_YEAST Protein kinase C-like 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PKC1 PE=1 SV=3
+MSFSQLEQNIKKKIAVEENIIRGASALKKKTSNVMVIQKCNTNIREARQNLEYLEDSLKK
+LRLKTAQQSQGENGSEDNERCNSKEYGFLSTKSPNEHIFSRLDLVKYDCPSLAQRIQYML
+QQLEFKLQVEKQYQEANTKLTKLYQIDGDQRSSSAAEGGAMESKYRIQMLNKALKKYQAI
+NVDFDQFKHQPNDIMDNQQPKFRRKQLTGVLTIGITAARDVDHIQSPMFARKPESYVTIK
+IDDTIKARTKPSRNDRWSEDFQIPVEKGNEIEITVYDKVNDSLIPVAIMWLLLSDIAEEI
+RKKKAGQTNEQQGWVNASNINGGSSLASEEGSTLTSTYSNSAIQSTSAKNVQGENTSTSQ
+ISTNSWFVLEPSGQILLTLGFHKSSQIERKQLMGGLHRHGAIINRKEEIFEQHGHHFVQK
+SFYNIMCCAYCGDFLRYTGFQCQDCKFLCHKKCYTNVVTKCIAKTSTDTDPDEAKLNHRI
+PHRFLPTSNRGTKWCCHCGYILPWGRHKVRKCSECGIMCHAQCAHLVPDFCGMSMEMANK
+ILKTIQDTKRNQEKKKRTVPSAQLGSSIGTANGSDLSPSKLAERANAPLPPQPRKHDKTP
+SPQKVGRDSPTKQHDPIIDKRISLQTHGREKLNKFIDENEAYLNFTEGAQQTAEFSSPEK
+TLDPTSNRRSLGLTDLSIEHSQTWESKDDLMRDELELWKAQREEMELEIKQDSGEIQEDL
+EVDHIDLETKQKLDWENKNDFREADLTIDSTHTNPFRDMNSETFQIEQDHASKEVLQETV
+SLAPTSTHASRTTDQQSPQKSQTSTSAKHKKRAAKRRKVSLDNFVLLKVLGKGNFGKVIL
+SKSKNTDRLCAIKVLKKDNIIQNHDIESARAEKKVFLLATKTKHPFLTNLYCSFQTENRI
+YFAMEFIGGGDLMWHVQNQRLSVRRAKFYAAEVLLALKYFHDNGVIYRDLKLENILLTPE
+GHIKIADYGLCKDEMWYGNRTSTFCGTPEFMAPEILKEQEYTKAVDWWAFGVLLYQMLLC
+QSPFSGDDEDEVFNAILTDEPLYPIDMAGEIVQIFQGLLTKDPEKRLGAGPRDADEVMEE
+PFFRNINFDDILNLRVKPPYIPEIKSPEDTSYFEQEFTSAPPTLTPLPSVLTTSQQEEFR
+GFSFMPDDLDL
+
+>sp|Q12460|NOP56_YEAST Nucleolar protein 56 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=NOP56 PE=1 SV=1
+MAPIEYLLFEEPTGYAVFKVKLQQDDIGSRLKEVQEQINDFGAFTKLIELVSFAPFKGAA
+EALENANDISEGLVSESLKAILDLNLPKASSKKKNITLAISDKNLGPSIKEEFPYVDCIS
+NELAQDLIRGVRLHGEKLFKGLQSGDLERAQLGLGHAYSRAKVKFSVQKNDNHIIQAIAL
+LDQLDKDINTFAMRVKEWYGWHFPELAKLVPDNYTFAKLVLFIKDKASLNDDSLHDLAAL
+LNEDSGIAQRVIDNARISMGQDISETDMENVCVFAQRVASLADYRRQLYDYLCEKMHTVA
+PNLSELIGEVIGARLISHAGSLTNLSKQAASTVQILGAEKALFRALKTKGNTPKYGLIYH
+SGFISKASAKNKGRISRYLANKCSMASRIDNYSEEPSNVFGSVLKKQVEQRLEFYNTGKP
+TLKNELAIQEAMELYNKDKPAAEVEETKEKESSKKRKLEDDDEEKKEKKEKKSKKEKKEK
+KEKKDKKEKKDKKEKKDKKKKSKD
+
+>sp|Q99207|NOP14_YEAST Nucleolar complex protein 14 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=NOP14 PE=1 SV=1
+MAGSQLKNLKAALKARGLTGQTNVKSKNKKNSKRQAKEYDREEKKKAIAEIREEFNPFEI
+KAARNKRRDGLPSKTADRIAVGKPGISKQIGEEQRKRAFEARKMMKNKRGGVIDKRFGER
+DKLLTEEEKMLERFTRERQSQSKRNANLFNLEDDEDDGDMFGDGLTHLGQSLSLEDELAN
+DEEDFLASKRFNEDDAELQQPQRKKTKAEVMKEVIAKSKFYKQERQKAQGIMEDQIDNLD
+DNFEDVMSELMMTQPKKNPMEPKTDLDKEYDIKVKELQLDKRAAPSDRTKTEEEKNAEAE
+EKKRELEQQRLDRMNGMIELEEGEERGVEDLDDGFWENEEDYEDDNDGIADSDDDIKFED
+QGRDEGFSQILKKKNISISCPRTHDALLDQVKKLDLDDHPKIVKNIIKAYQPKLAEGNKE
+KLGKFTAVLLRHIIFLSNQNYLKNVQSFKRTQNALISILKSLSEKYNRELSEECRDYINE
+MQARYKKNHFDALSNGDLVFFSIIGILFSTSDQYHLVITPALILMSQFLEQIKFNSLKRI
+AFGAVLVRIVSQYQRISKRYIPEVVYFFQKILLTFIVEKENQEKPLDFENIRLDSYELGL
+PLDVDFTKKRSTIIPLHTLSTMDTEAHPVDQCVSVLLNVMESLDATISTVWKSLPAFNEI
+ILPIQQLLSAYTSKYSDFEKPRNILNKVEKLTKFTEHIPLALQNHKPVSIPTHAPKYEEN
+FNPDKKSYDPDRTRSEINKMKAQLKKERKFTMKEIRKDAKFEARQRIEEKNKESSDYHAK
+MAHIVNTINTEEGAEKNKYERERKLRGGKK
+
+>sp|P54784|ORC1_YEAST Origin recognition complex subunit 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=ORC1 PE=1 SV=1
+MAKTLKDLQGWEIITTDEQGNIIDGGQKRLRRRGAKTEHYLKRSSDGIKLGRGDSVVMHN
+EAAGTYSVYMIQELRLNTLNNVVELWALTYLRWFEVNPLAHYRQFNPDANILNRPLNYYN
+KLFSETANKNELYLTAELAELQLFNFIRVANVMDGSKWEVLKGNVDPERDFTVRYICEPT
+GEKFVDINIEDVKAYIKKVEPREAQEYLKDLTLPSKKKEIKRGPQKKDKATQTAQISDAE
+TRATDITDNEDGNEDESSDYESPSDIDVSEDMDSGEISADELEEEEDEEEDEDEEEKEAR
+HTNSPRKRGRKIKLGKDDIDASVQPPPKKRGRKPKDPSKPRQMLLISSCRANNTPVIRKF
+TKKNVARAKKKYTPFSKRFKSIAAIPDLTSLPEFYGNSSELMASRFENKLKTTQKHQIVE
+TIFSKVKKQLNSSYVKEEILKSANFQDYLPARENEFASIYLSAYSAIESDSATTIYVAGT
+PGVGKTLTVREVVKELLSSSAQREIPDFLYVEINGLKMVKPTDCYETLWNKVSGERLTWA
+ASMESLEFYFKRVPKNKKKTIVVLLDELDAMVTKSQDIMYNFFNWTTYENAKLIVIAVAN
+TMDLPERQLGNKITSRIGFTRIMFTGYTHEELKNIIDLRLKGLNDSFFYVDTKTGNAILI
+DAAGNDTTVKQTLPEDVRKVRLRMSADAIEIASRKVASVSGDARRALKVCKRAAEIAEKH
+YMAKHGYGYDGKTVIEDENEEQIYDDEDKDLIESNKAKDDNDDDDDNDGVQTVHITHVMK
+ALNETLNSHVITFMTRLSFTAKLFIYALLNLMKKNGSQEQELGDIVDEIKLLIEVNGSNK
+FVMEIAKTLFQQGSDNISEQLRIISWDFVLNQLLDAGILFKQTMKNDRICCVKLNISVEE
+AKRAMNEDETLRNL
+
+>sp|P06169|PDC1_YEAST Pyruvate decarboxylase isozyme 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PDC1 PE=1 SV=7
+MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADG
+YARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNG
+DFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKL
+LQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQF
+PAFVTPMGKGSIDEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYS
+YKTKNIVEFHSDHMKIRNATFPGVQMKFVLQKLLTTIADAAKGYKPVAVPARTPANAAVP
+ASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTG
+ATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLI
+HGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIML
+PVFDAPQNLVEQAKLTAATNAKQ
+
+>sp|P02293|H2B1_YEAST Histone H2B.1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=HTB1 PE=1 SV=2
+MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQ
+KSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTR
+AVTKYSSSTQA
+
+>sp|P02294|H2B2_YEAST Histone H2B.2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=HTB2 PE=1 SV=2
+MSSAAEKKPASKAPAEKKPAAKKTSTSVDGKKRSKVRKETYSSYIYKVLKQTHPDTGISQ
+KSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTR
+AVTKYSSSTQA
+
+>sp|P15108|HSC82_YEAST ATP-dependent molecular chaperone HSC82 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=HSC82 PE=1 SV=4
+MAGETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQALSDPKQLETEP
+DLFIRITPKPEEKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQF
+GVGFYSLFLVADRVQVISKNNEDEQYIWESNAGGSFTVTLDEVNERIGRGTVLRLFLKDD
+QLEYLEEKRIKEVIKRHSEFVAYPIQLLVTKEVEKEVPIPEEEKKDEEKKDEDDKKPKLE
+EVDEEEEEKKPKTKKVKEEVQELEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPL
+YVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSF
+VKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFDKFYSAFAKN
+IKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEK
+SPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEI
+KEYEPLTKALKDILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMS
+SYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTNLLFETALLTSGFSLEEPTSF
+ASRINRLISLGLNIDEDEETETAPEASTEAPVEEVPADTEMEEVD
+
+>sp|P10591|HSP71_YEAST Heat shock protein SSA1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=SSA1 PE=1 SV=4
+MSKAVGIDLGTTYSCVAHFANDRVDIIANDQGNRTTPSFVAFTDTERLIGDAAKNQAAMN
+PSNTVFDAKRLIGRNFNDPEVQADMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSM
+VLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIA
+YGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQ
+EFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFE
+ELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSI
+NPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTK
+KSEIFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSN
+GILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLE
+SIAYSLKNTISEAGDKLEQADKDTVTKKAEETISWLDSNTTASKEEFDDKLKELQDIANP
+IMSKLYQAGGAPGGAAGGAPGGFPGGAPPAPEAEGPTVEEVD
+
+>sp|P10592|HSP72_YEAST Heat shock protein SSA2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=SSA2 PE=1 SV=3
+MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMN
+PANTVFDAKRLIGRNFNDPEVQGDMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSM
+VLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIA
+YGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQ
+EFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFE
+ELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSI
+NPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTK
+KSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSN
+GILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLE
+SIAYSLKNTISEAGDKLEQADKDAVTKKAEETIAWLDSNTTATKEEFDDQLKELQEVANP
+IMSKLYQAGGAPEGAAPGGFPGGAPPAPEAEGPTVEEVD
+
+>sp|P0CS90|HSP77_YEAST Heat shock protein SSC1, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=SSC1 PE=1 SV=1
+MLAAKNILNRSSLSSSFRIATRLQSTKVQGSVIGIDLGTTNSAVAIMEGKVPKIIENAEG
+SRTTPSVVAFTKEGERLVGIPAKRQAVVNPENTLFATKRLIGRRFEDAEVQRDIKQVPYK
+IVKHSNGDAWVEARGQTYSPAQIGGFVLNKMKETAEAYLGKPVKNAVVTVPAYFNDSQRQ
+ATKDAGQIVGLNVLRVVNEPTAAALAYGLEKSDSKVVAVFDLGGGTFDISILDIDNGVFE
+VKSTNGDTHLGGEDFDIYLLREIVSRFKTETGIDLENDRMAIQRIREAAEKAKIELSSTV
+STEINLPFITADASGPKHINMKFSRAQFETLTAPLVKRTVDPVKKALKDAGLSTSDISEV
+LLVGGMSRMPKVVETVKSLFGKDPSKAVNPDEAVAIGAAVQGAVLSGEVTDVLLLDVTPL
+SLGIETLGGVFTRLIPRNTTIPTKKSQIFSTAAAGQTSVEIRVFQGERELVRDNKLIGNF
+TLAGIPPAPKGVPQIEVTFDIDADGIINVSARDKATNKDSSITVAGSSGLSENEIEQMVN
+DAEKFKSQDEARKQAIETANKADQLANDTENSLKEFEGKVDKAEAQKVRDQITSLKELVA
+RVQGGEEVNAEELKTKTEELQTSSMKLFEQLYKNDSNNNNNNNGNNAESGETKQ
+
+>sp|P40576|INA22_YEAST Inner membrane assembly complex subunit 22 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=INA22 PE=1 SV=1
+MFMARQVLRNGLFLRSLAPIKITARTVASANAGIKRKSRFDKTMIKPLLLVMIFGSILNA
+VIAEKRNIIDMERKYKLKLDKLKELIRRVHDNNGKVDFDADDELKLVNLRLGIVGKNATG
+MKEDETDIVVPKEESLEEIWQSIIDEAKKEVIEKTPDAGVKNKEGIVTDLNVLKDLEKSK
+KEDEKVYLSGDVHMMMNQPGDLNEIAKEHDKIPKFL
+
+>sp|P02829|HSP82_YEAST ATP-dependent molecular chaperone HSP82 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=HSP82 PE=1 SV=1
+MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEP
+DLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQF
+GVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDD
+QLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDK
+KPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDW
+EDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPE
+WLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSA
+FSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLK
+AVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAER
+EKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRD
+SSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDE
+PTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEVD
+
+>sp|P32589|HSP7F_YEAST Heat shock protein homolog SSE1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=SSE1 PE=1 SV=4
+MSTPFGLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGETGKNKQTSN
+IKNTVANLKRIIGLDYHHPDFEQESKHFTSKLVELDDKKTGAEVRFAGEKHVFSATQLAA
+MFIDKVKDTVKQDTKANITDVCIAVPPWYTEEQRYNIADAARIAGLNPVRIVNDVTAAGV
+SYGIFKTDLPEGEEKPRIVAFVDIGHSSYTCSIMAFKKGQLKVLGTACDKHFGGRDFDLA
+ITEHFADEFKTKYKIDIRENPKAYNRILTAAEKLKKVLSANTNAPFSVESVMNDVDVSSQ
+LSREELEELVKPLLERVTEPVTKALAQAKLSAEEVDFVEIIGGTTRIPTLKQSISEAFGK
+PLSTTLNQDEAIAKGAAFICAIHSPTLRVRPFKFEDIHPYSVSYSWDKQVEDEDHMEVFP
+AGSSFPSTKLITLNRTGDFSMAASYTDITQLPPNTPEQIANWEITGVQLPEGQDSVPVKL
+KLRCDPSGLHTIEEAYTIEDIEVEEPIPLPEDAPEDAEQEFKKVTKTVKKDDLTIVAHTF
+GLDAKKLNELIEKENEMLAQDKLVAETEDRKNTLEEYIYTLRGKLEEEYAPFASDAEKTK
+LQGMLNKAEEWLYDEGFDSIKAKYIAKYEELASLGNIIRGRYLAKEEEKKQAIRSKQEAS
+QMAAMAEKLAAQRKAEAEKKEEKKDTEGDVDMD
+
+>sp|P46997|JJJ2_YEAST J protein JJJ2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=JJJ2 PE=1 SV=2
+MSQVIEPQLDRTTYYSILGLTSNATSSEVHKSYLKLARLLHPDKTKSDKSEELFKAVVHA
+HSILTDEDQKLRYDRDLKIKGLHTYQPKKNCHIFKTKAKESQGASPTLGQSEAYHRQNKP
+YEQQPYGFGVGKKMTSSSKSKVPIFKSFNLKSYQRNHYYSSKKERKHGSPDIDSLFHETN
+GASKVRMTDAGKMDTNSQFQEIWEILGKNAYTHKSYSEDPNSCLGSALSDHEEEEEAGKQ
+QQQQQQQQQQQQHYGMTSKSSSPDEEKKNNKEPKRESRVSPEENGEEETGHKQFKLPKTS
+TFSSGSHDSNLQSPFYNHEYRHYARSKFECKNQFRKSVSPIKEIPATTSANEGWNILRDI
+IEKLNISNVDDRNKDLLFRRDEIGDKNHSDSIDIENLSIKEPKGMKRRKKDDISLEELFQ
+SLPREKDYFMMDAINDSLESINLFKKPKTTQSHEQGGTFAQAESNRAKFKPLLEQCGITP
+EILDLEIPEIPEFDAVADLETLKLNVQLFNNQCNKLKETIHQVSLQRLRADTQFSDMLTQ
+KQSIMVWKTYLEFDKSLMDKLNILQERQMQVIKIFSERCDGKV
+
+>sp|Q12230|LSP1_YEAST Sphingolipid long chain base-responsive protein LSP1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=LSP1 PE=1 SV=1
+MHRTYSLRNQRAPTAAELQAPPPPPSSTKSKFFGKASIASSFRKNAAGNFGPELARKLSQ
+LVKTEKGVLRAMEVVASERREAAKQLSLWGADNDDDVSDVTDKLGVLIYELGELQDQFID
+KYDQYRVTLKSIRNIEASVQPSRDRKEKITDEIAHLKYKDPQSTKIPVLEQELVRAEAES
+LVAEAQLSNITREKLKAAYSYMFDSLRELSEKFALIAGYGKALLELLDDSPVTPGEARPA
+YDGYEASRQIIMDAESALESWTLDMAAVKPTLSFHQTVDDVYEDEDGEEEEEPEIQNGDI
+PGQVVEEEEVEWTTEVPVDDEAHEADHHVSQNGHTSGSENI
+
+>sp|Q12117|MRH1_YEAST Protein MRH1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=MRH1 PE=1 SV=1
+MSTFETLIKRGGNEAIKINPPTGADFHITSRGSDWFWTCFCCYLLFGLILTFLMFRKPVN
+DRFFYLTGIAPNFFMCIAYFTMASNLGWIPVKAKYNHVQTSTQKEHPGYRQIFYSRFVGW
+FLALPWPIIQICMLAGTPFWQMAFNVCITEFFTVCWLIAACVHSTYKWGYYTIGLGAAIV
+VSISVMTTSYNLVKQRDNDIRLTFLVFFSIIMFLWIIAYPTCFGITDGGNVLQPDSAGIF
+YGIIDLILMCFIPTLLVPIANHFGADKLGYHFGPSDAEAVMAPKAPVASPRPAATPNLSK
+DKKKKSKKSKKSKKSKKSEE
+
+>sp|Q06820|MDM36_YEAST Mitochondrial distribution and morphology protein 36 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=MDM36 PE=1 SV=1
+MDENGTVKPGYELKGLNSGNSRSNMDKDPIVSKFHRAGLNDSADEEDTDINGNRNTSWIT
+SMISEEKRKVEGKSMLNDEEDLHLSKATLNKCDALVKILADIIKLEFVIHQSWYIRSLHK
+SVLIQFEVETSGGNKNSAGDSGDDDDDNHNGNLDDSFYKDLSLKCIKKCEKSSLALESLS
+RDIDQIRDFIMSNTIEDNRVDRLLQNSMTLLLECWIYSMKRLRRLRMKIAGIFVRSKLLL
+IDHELVTIWHFLQEQNEHETVNNENELKLAETIKSYRAFIKIFIQQLEDSESGSPSSSLF
+EECLHVFLDIESMYNSLNLNWLLNENKALQERLLSPSSTSENDHTNNLPVIDETKEIEDI
+SSFVNSIVDASMLTHDLTPINSSDSDNLSNGEIDRLDGRRLSSSTSDMSLMMQRTSLQKQ
+LPSLLTAFNNARRLEQELQNACKVNDNKHSTKDTDSNIRRNEHAMSSSVSSIISQNSTLA
+SPSPPMSSSFISTAPSQSSSRMSTLPLSPSSSLLESQSQTLKNNMSQWLNQSRSGLNGTK
+LIPTNHIGFHSNVLNTLYGIGGGPVSKSYKSNQPSSQNT
+
+>sp|O14467|MBF1_YEAST Multiprotein-bridging factor 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=MBF1 PE=1 SV=2
+MSDWDTNTIIGSRARAGGSGPRANVARSQGQINAARRQGLVVSVDKKYGSTNTRGDNEGQ
+RLTKVDRETDIVKPKKLDPNVGRAISRARTDKKMSQKDLATKINEKPTVVNDYEAARAIP
+NQQVLSKLERALGVKLRGNNIGSPLGAPKKK
+
+>sp|P00560|PGK_YEAST Phosphoglycerate kinase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PGK1 PE=1 SV=2
+MSLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVL
+ASHLGRPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLEN
+LRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLP
+QRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAF
+TFKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVT
+DKEGIPAGWQGLDNGPESRKLFAATVAKAKTIVWNGPPGVFEFEKFAAGTKALLDEVVKS
+SAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKK
+
+>sp|Q05568|PEX10_YEAST Peroxisome biogenesis factor 10 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=PEX10 PE=1 SV=1
+MKNDNKLQKEALMRLSQLRFPFADAPSIVQAHQKDEQIQGLLIMKVTELCKLIKSQLFVN
+SYPKELSIFAKLLYLLFTTGRRGRTLGEEYVDLTYTNRKGTRLAGRLKMIVFAFAYPLCP
+YFITKLYKKIMKNNKESKIEDTESVAAFCKGLLDFILDVHMTLFYFKGAFYSISKRIFGM
+RYVFKHILSKNEANFREEGSQKYKVLGYILLAQNVMKWYPVLTSTLGSWIYGRKRTNDSI
+TRSSVGLQERSEHESIEGIPKESQLTHINLSDKNQLPFIPEASRKCILCLMNMSDPSCAP
+CGHLFCWSCLMSWCKERPECPLCRQHCQPQEILVLRQ
+
+>sp|P00950|PMG1_YEAST Phosphoglycerate mutase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=GPM1 PE=1 SV=3
+MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSR
+AIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVP
+PPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIA
+AHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAA
+VANQGKK
+
+>sp|O13516|RS9A_YEAST 40S ribosomal protein S9-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPS9A PE=1 SV=3
+MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKKEIYRISFQLSKIRRAARDLL
+TRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAK
+SVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARK
+AEASGEAADEADEADEE
+
+>sp|P02407|RS17A_YEAST 40S ribosomal protein S17-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPS17A PE=1 SV=1
+MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKR
+IQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLS
+VINVSAQRDRRYRKRV
+
+>sp|P05756|RS13_YEAST 40S ribosomal protein S13 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPS13 PE=1 SV=3
+MGRMHSAGKGISSSAIPYSRNAPAWFKLSSESVIEQIVKYARKGLTPSQIGVLLRDAHGV
+TQARVITGNKIMRILKSNGLAPEIPEDLYYLIKKAVSVRKHLERNRKDKDAKFRLILIES
+RIHRLARYYRTVAVLPPNWKYESATASALVN
+
+>sp|P46784|RS10B_YEAST 40S ribosomal protein S10-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPS10B PE=1 SV=1
+MLMPKQERNKIHQYLFQEGVVVAKKDFNQAKHEEIDTKNLYVIKALQSLTSKGYVKTQFS
+WQYYYYTLTEEGVEYLREYLNLPEHIVPGTYIQERNPSQRPQRRY
+
+>sp|Q05911|PUR8_YEAST Adenylosuccinate lyase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=ADE13 PE=1 SV=1
+MPDYDNYTTPLSSRYASKEMSATFSLRNRFSTWRKLWLNLAIAEKELGLTVVTDEAIEQM
+RKHVEITDDEIAKASAQEAIVRHDVMAHVHTFGETCPAAAGIIHLGATSCFVTDNADLIF
+IRDAYDIIIPKLVNVINRLAKFAMEYKDLPVLGWTHFQPAQLTTLGKRATLWIQELLWDL
+RNFERARNDIGLRGVKGTTGTQASFLALFHGNHDKVEALDERVTELLGFDKVYPVTGQTY
+SRKIDIDVLAPLSSFAATAHKMATDIRLLANLKEVEEPFEKSQIGSSAMAYKRNPMRCER
+VCSLARHLGSLFSDAVQTASVQWFERTLDDSAIRRISLPSAFLTADILLSTLLNISSGLV
+VYPKVIERRIKGELPFMATENIIMAMVEKNASRQEVHERIRVLSHQAAAVVKEEGGENDL
+IERVKRDEFFKPIWEELDSLLEPSTFVGRAPQQVEKFVQKDVNNALQPFQKYLNDEQVKL
+NV
+
+>sp|P28272|PYRD_YEAST Dihydroorotate dehydrogenase (fumarate) OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=URA1 PE=1 SV=1
+MTASLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPR
+YISVPLGSINSMGLPNEGIDYYLSYVLNRQKNYPDAPAIFFSVAGMSIDENLNLLRKIQD
+SEFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKKPLGVKLPPYFDFAHFDIM
+AKILNEFPLAYVNSINSIGNGLFIDVEKESVVVKPKNGFGGIGGEYVKPTALANVRAFYT
+RLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKG
+YTSIDQFRGKLNSI
+
+>sp|Q00816|REG1_YEAST Resistance to glucose repression protein 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=REG1 PE=1 SV=1
+MSTNLANYFAGKKDIENEHVNRNASHESNSKSDVKISGNDNDNDEDMGPSVSMAVQAKND
+DDFHKSTFNLKRTRSMGLLDEYIDPTKKLLGRSDDLYDNDNEYYDNSSNNSSSNSSDDDY
+DDGYQEHSTSVSPPPADNDSYLIPQDDNDVVVEPERHVDYLSHEWKESEISNSWKYIILK
+KKKRDVDLVNAARLENASWRTWAKARNNLKTVSPEVVNWSKDSDVTWLYGPIVRDSEGNA
+QSEEEHDLERGYGSDDENSKRISMPTKNSKSIAAAPKPILKKRTVTEIIEDNALWKLNEA
+RKHMTEMKHASVIMDPNGNKNVHDDFDALAAQVNAQYYHYPKESNSSVSLKSQHSDKKDN
+STIPNPVGENSNGGGDKGEEDLHLKSALHVQNNRSTAQSNKSILENSTNDRKANLDQNLN
+SPDNNRFPSSTSSSNRDNENNSMGLSSILTSNPSEKSNKPTKNRHIHFNDRVEQCMALRY
+PASQSEDDESDDENKQYVDVNNNANVTTINNNRTPLLAIQHKSIPINSATEHLNKNTSDD
+DTSSQSSSSSHSDDEEHGGLYINARFSRRSDSGVHSPITDNSSVASSTTSRAHVRPIIKL
+LPDTTLNYGSDEESDNGEFNGYGNAVSHNVNTSRGYDYIYDYNSVYTGDTSSFLPVDSCD
+IVDVPEGMDLQTAIADDNASNYEFNNAVESKEKHVPQLHKASANNTTRQHGSHMLLYDDD
+NYSSSSDSEQQFIEDSQYNSSDDEEEEDDDDQEVDDNHDEGLSLRRTLSLGKSGSTNSLY
+DLAQPSLSSATPQQKNPTNFTGGKTDVDKDAQLAVRPYPLKRNSSSGNFIFNSDSEEESS
+SEEEQRPLPANSQLVNRSVLKGSVTPANISSQKKKALPKQPKASDSSQSFRIVNNTPSPA
+EVGASDVAIEGYFSPRNESIKSVVSGGNMMDHQDHSEMDTLAKGFENCHINNASKLKDKK
+VDSVQTTRKEASLTDSSNESLHKVVQNARGMASKYLHSWKKSDVKPQENGNDSS
+
+>sp|P0CX50|RL18B_YEAST 60S ribosomal protein L18-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL18B PE=1 SV=1
+MGIDHTSKQHKRSGHRTAPKSDNVYLKLLVKLYTFLARRTDAPFNKVVLKALFLSKINRP
+PVSVSRIARALKQEGAANKTVVVVGTVTDDARIFEFPKTTVAALRFTAGARAKIVKAGGE
+CITLDQLAVRAPKGQNTLILRGPRNSREAVRHFGMGPHKGKAPRILSTGRKFERARGRRR
+SKGFKV
+
+>sp|P0CX82|RL19A_YEAST 60S ribosomal protein L19-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL19A PE=1 SV=1
+MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSK
+SRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLY
+HVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEK
+RDALLKEDA
+
+>sp|P40212|RL13B_YEAST 60S ribosomal protein L13-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL13B PE=1 SV=1
+MAISKNLPILKNHFRKHWQERVKVHFDQAGKKVSRRNARAARAAKIAPRPLDLLRPVVRA
+PTVKYNRKVRAGRGFTLAEVKAAGLTAAYARTIGIAVDHRRQNRNQEIFDANVQRLKEYQ
+SKIIVFPRDGKAPEAEQVLSAAATFPIAQPATDVEARAVQDNGESAFRTLRLARSEKKFR
+GIREKRAREKAEAEAEKKK
+
+>sp|Q12690|RL13A_YEAST 60S ribosomal protein L13-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL13A PE=1 SV=1
+MAISKNLPILKNHFRKHWQERVKVHFDQAGKKVSRRNARATRAAKIAPRPLDLLRPVVRA
+PTVKYNRKVRAGRGFTLAEVKAAGLTAAYARTIGIAVDHRRQNRNQEIFDANVQRLKEYQ
+SKIIVFPRNGKAPEAEQVLSAAATFPIAQPATDVEARAVQDNGESAFRTLRLARSEKKFR
+GIREKRAREKAEAEAEKKK
+
+>sp|P26784|RL16A_YEAST 60S ribosomal protein L16-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL16A PE=1 SV=3
+MSVEPVVVIDGKGHLVGRLASVVAKQLLNGQKIVVVRAEELNISGEFFRNKLKYHDFLRK
+ATAFNKTRGPFHFRAPSRIFYKALRGMVSHKTARGKAALERLKVFEGIPPPYDKKKRVVV
+PQALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEAKRKVSSAEYYAKKRAFTKKVAS
+ANATAAESDVAKQLAALGY
+
+>sp|P0CX83|RL19B_YEAST 60S ribosomal protein L19-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL19B PE=1 SV=1
+MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSK
+SRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLY
+HVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEK
+RDALLKEDA
+
+>sp|Q02753|RL21A_YEAST 60S ribosomal protein L21-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL21A PE=1 SV=1
+MGKSHGYRSRTRYMFQRDFRKHGAVHLSTYLKVYKVGDIVDIKANGSIQKGMPHKFYQGK
+TGVVYNVTKSSVGVIINKMVGNRYLEKRLNLRVEHIKHSKCRQEFLERVKANAAKRAEAK
+AQGVAVQLKRQPAQPRESRIVSTEGNVPQTLAPVPYETFI
+
+>sp|P26785|RL16B_YEAST 60S ribosomal protein L16-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL16B PE=1 SV=3
+MSQPVVVIDAKDHLLGRLASTIAKQVLNGQKIVVVRAEALNISGEFFRNKLKYHDFLRKA
+TAFNKTRGPFHFRAPSRILYKAIRGMVSHKTARGKAALERLKIFEGIPPPYDKKKRVVVP
+QALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEDKRKVRSAEYYAKKRAFTKKVSSA
+SAAASESDVAKQLASFGY
+
+>sp|P0CX49|RL18A_YEAST 60S ribosomal protein L18-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL18A PE=1 SV=1
+MGIDHTSKQHKRSGHRTAPKSDNVYLKLLVKLYTFLARRTDAPFNKVVLKALFLSKINRP
+PVSVSRIARALKQEGAANKTVVVVGTVTDDARIFEFPKTTVAALRFTAGARAKIVKAGGE
+CITLDQLAVRAPKGQNTLILRGPRNSREAVRHFGMGPHKGKAPRILSTGRKFERARGRRR
+SKGFKV
+
+>sp|Q08961|RKM1_YEAST Ribosomal lysine N-methyltransferase 1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RKM1 PE=1 SV=1
+MSSDALKALLQWGASFGVIVPEELKFLYTDLKGIICVCEKDIDNPSIKIPPEIVISRNLP
+MKFFGLSESTKNINGWLKLFFAKIKFDRDNDTIVDNVRVNDKFKPYLDALPSRLNSPLVW
+NPSELKRLSSTNIGNSIHEKFEGIFKEWFELVSSSDMFDLERVADDVQTFHNLDELTYEA
+LYEKILKITELQRPTIWYSFPAFLWSHLIFISRAFPEYVLNRNCPDNSIVLLPIVDLLNH
+DYRSKVKWYPENGWFCYEKIGTASQSRELSNNYGGKGNEELLSGYGFVLEDNIFDSVALK
+VKLPLDVVSTILETEPSLKLPLLSDYTTYAFENKDCVQQEKKATRSATDYINGVTYFINI
+QNEQCLEPLLDLFTYLSKAEEEDLHDLRARLQGIQMLRNALQSKLNSITGPPATDDSYAI
+DPYRVYCADVYTKGQKQILKEALTRLKKLEKTMLSENKHQLLTMSKILKNDPAFAETELP
+SLFSNEDGEEVIFESTYDLLILWILLKTKKNSYPTKYEWVGQQYTNFKQTAYISDDAKAF
+HTAYFEKQDDVDLAEVDHAIQFVVDNSFTRTSSTTEETILVRK
+
+>sp|P26321|RL5_YEAST 60S ribosomal protein L5 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL5 PE=1 SV=4
+MAFQKDAKSSAYSSRFQTPFRRRREGKTDYYQRKRLVTQHKAKYNTPKYRLVVRFTNKDI
+ICQIISSTITGDVVLAAAYSHELPRYGITHGLTNWAAAYATGLLIARRTLQKLGLDETYK
+GVEEVEGEYELTEAVEDGPRPFKVFLDIGLQRTTTGARVFGALKGASDGGLYVPHSENRF
+PGWDFETEEIDPELLRSYIFGGHVSQYMEELADDDEERFSELFKGYLADDIDADSLEDIY
+TSAHEAIRADPAFKPTEKKFTKEQYAAESKKYRQTKLSKEERAARVAAKIAALAGQQ
+
+>sp|P0CX24|RL20B_YEAST 60S ribosomal protein L20-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL20B PE=1 SV=1
+MAHFKEYQVIGRRLPTESVPEPKLFRMRIFASNEVIAKSRYWYFLQKLHKVKKASGEIVS
+INQINEAHPTKVKNFGVWVRYDSRSGTHNMYKEIRDVSRVAAVETLYQDMAARHRARFRS
+IHILKVAEIEKTADVKRQYVKQFLTKDLKFPLPHRVQKSTKTFSYKRPSTFY
+
+>sp|P0CX46|RL2B_YEAST 60S ribosomal protein L2-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL2B PE=1 SV=1
+MGRVIRNQRKGAGSIFTSHTRLRQGAAKLRTLDYAERHGYIRGIVKQIVHDSGRGAPLAK
+VVFRDPYKYRLREEIFIANEGVHTGQFIYAGKKASLNVGNVLPLGSVPEGTIVSNVEEKP
+GDRGALARASGNYVIIIGHNPDENKTRVRLPSGAKKVISSDARGVIGVIAGGGRVDKPLL
+KAGRAFHKYRLKRNSWPKTRGVAMNPVDHPHGGGNHQHIGKASTISRGAVSGQKAGLIAA
+RRTGLLRGSQKTQD
+
+>sp|Q12672|RL21B_YEAST 60S ribosomal protein L21-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL21B PE=1 SV=1
+MGKSHGYRSRTRYMFQRDFRKHGAVHMSTYLKIYKVGDIVDIKANGSIQKGMPHKFYQGK
+TGVVYNVTKSSVGVIINKMVGNRYLEKRLNLRVEHIKHSKCRQEFLERVKANAAKRAEAK
+AQGVAVQLKRQPAQPRESRIVSTEGNVPQTLAPVPYETFI
+
+>sp|P41056|RL33B_YEAST 60S ribosomal protein L33-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL33B PE=1 SV=2
+MAESHRLYVKGKHLSYQRSKRVNNPNVSLIKIEGVATPQEAQFYLGKRIAYVYRASKEVR
+GSKIRVMWGKVTRTHGNSGVVRATFRNNLPAKTFGASVRIFLYPSNI
+
+>sp|P0CX23|RL20A_YEAST 60S ribosomal protein L20-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL20A PE=1 SV=1
+MAHFKEYQVIGRRLPTESVPEPKLFRMRIFASNEVIAKSRYWYFLQKLHKVKKASGEIVS
+INQINEAHPTKVKNFGVWVRYDSRSGTHNMYKEIRDVSRVAAVETLYQDMAARHRARFRS
+IHILKVAEIEKTADVKRQYVKQFLTKDLKFPLPHRVQKSTKTFSYKRPSTFY
+
+>sp|P0CX45|RL2A_YEAST 60S ribosomal protein L2-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL2A PE=1 SV=1
+MGRVIRNQRKGAGSIFTSHTRLRQGAAKLRTLDYAERHGYIRGIVKQIVHDSGRGAPLAK
+VVFRDPYKYRLREEIFIANEGVHTGQFIYAGKKASLNVGNVLPLGSVPEGTIVSNVEEKP
+GDRGALARASGNYVIIIGHNPDENKTRVRLPSGAKKVISSDARGVIGVIAGGGRVDKPLL
+KAGRAFHKYRLKRNSWPKTRGVAMNPVDHPHGGGNHQHIGKASTISRGAVSGQKAGLIAA
+RRTGLLRGSQKTQD
+
+>sp|P05744|RL33A_YEAST 60S ribosomal protein L33-A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL33A PE=1 SV=3
+MAESHRLYVKGKHLSYQRSKRVNNPNVSLIKIEGVATPQDAQFYLGKRIAYVYRASKEVR
+GSKIRVMWGKVTRTHGNSGVVRATFRNNLPAKTFGASVRIFLYPSNI
+
+>sp|P05739|RL6B_YEAST 60S ribosomal protein L6-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPL6B PE=1 SV=4
+MTAQQAPKWYPSEDVAAPKKTRKAVRPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLED
+NTLLVTGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEAN
+LFPEQQTKEIKTERVEDQKVVDKALLAEIKKTPLLKQYLSASFSLKNGDKPHLLKF
+
+>sp|P48589|RS12_YEAST 40S ribosomal protein S12 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPS12 PE=1 SV=1
+MSDVEEVVEVQEETVVEQTAEVTIEDALKVVLRTALVHDGLARGLRESTKALTRGEALLV
+VLVSSVTEANIIKLVEGLANDPENKVPLIKVADAKQLGEWAGLGKIDREGNARKVVGASV
+VVVKNWGAETDELSMIMEHFSQQ
+
+>sp|P14127|RS17B_YEAST 40S ribosomal protein S17-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPS17B PE=1 SV=1
+MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKR
+IQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLS
+VINVSAQRDRRYRKRN
+
+>sp|P05755|RS9B_YEAST 40S ribosomal protein S9-B OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=RPS9B PE=1 SV=4
+MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKREIYRISFQLSKIRRAARDLL
+TRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAK
+SVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARK
+AEASGEAAEEAEDEE
+
+>sp|P40075|SCS2_YEAST Vesicle-associated membrane protein-associated protein SCS2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=SCS2 PE=1 SV=3
+MSAVEISPDVLVYKSPLTEQSTEYASISNNSDQTIAFKVKTTAPKFYCVRPNAAVVAPGE
+TIQVQVIFLGLTEEPAADFKCRDKFLVITLPSPYDLNGKAVADVWSDLEAEFKQQAISKK
+IKVKYLISPDVHPAQNQNIQENKETVEPVVQDSEPKEVPAVVNEKEVPAEPETQPPVQVK
+KEEVPPVVQKTVPHENEKQTSNSTPAPQNQIKEAATVPAENESSSMGIFILVALLILVLG
+WFYR
+
+>sp|Q12118|SGT2_YEAST Small glutamine-rich tetratricopeptide repeat-containing protein 2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=SGT2 PE=1 SV=1
+MSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEF
+KGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYEL
+AINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAK
+YAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDA
+SQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAE
+GFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ
+
+>sp|P25582|SPB1_YEAST 27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=SPB1 PE=1 SV=2
+MGKTQKKNSKGRLDRYYYLAKEKGYRARSSFKIIQINEKYGHFLEKSKVVIDLCAAPGSW
+CQVASKLCPVNSLIIGVDIVPMKPMPNVITFQSDITTEDCRSKLRGYMKTWKADTVLHDG
+APNVGLGWVQDAFTQSQLTLQALKLAVENLVVNGTFVTKIFRSKDYNKLIWVFQQLFEKV
+EATKPPASRNVSAEIFVVCKGFKAPKRLDPRLLDPKEVFEELPDGQQNMESKIYNPEKKV
+RKRQGYEEGDNLLYHETSILDFVRTEDPISMLGEMNKFTIDENDHEWKILKKLKQTTDEF
+RSCIEDLKVLGKKDFKMILRWRKIAREILGIEVKDDAKTEIEVVPLTEEEQIEKDLQGLQ
+EKQRLNVKRERRRKNEMKQKELQRMQMNMITPTDIGIEAASLGKESLFNLKTAEKTGILN
+DLAKGKKRMIFTDDELAKDNDIYIDENIMIKDKDSAADADDLESELNAMYSDYKTRRSER
+DAKFRAKQARGGDNEEEWTGFNEGSLEKKEEEGKDYIEDNDDEGVEGDSDDDEAITNLIS
+KLKGQEGDHKLSSKARMIFNDPIFNNVEPDLPVNTVNDGIMSSESVGDISKLNKKRKHEE
+MHQKQDEADSSDESSSDDSDFEIVANDNASEEFDSDYDSEEEKNQTKKEKHSRDIDIATV
+EAMTLAHQLALGQKNKHDLVDEGFNRYTFRDTENLPDWFLEDEKEHSKINKPITKEAAMA
+IKEKIKAMNARPIKKVAEAKARKRMRAVARLEKIKKKAGLINDDSDKTEKDKAEEISRLM
+RKVTKKPKTKPKVTLVVASGRNKGLAGRPKGVKGKYKMVDGVMKNEQRALRRIAKKHHKK
+K
+
+>sp|P32558|SPT16_YEAST FACT complex subunit SPT16 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=SPT16 PE=1 SV=1
+MEELNIDFDVFKKRIELLYSKYNEFEGSPNSLLFVLGSSNAENPYQKTTILHNWLLSYEF
+PATLIALVPGKVIIITSSAKAKHLQKAIDLFKDPESKITLELWQRNNKEPELNKKLFDDV
+IALINSAGKTVGIPEKDSYQGKFMTEWNPVWEAAVKENEFNVIDISLGLSKVWEVKDVNE
+QAFLSVSSKGSDKFMDLLSNEMVRAVDEELKITNAKLSDKIENKIDDVKFLKQLSPDLSA
+LCPPNYKFNFDLLDWTYSPIIQSGKKFDLRVSARSTNDQLYGNGCILASCGIRYNNYCSN
+ITRTFLIDPSEEMANNYDFLLTLQKEIVTNILKPGRTPKEVYESVIEYIEKTKPELVPNF
+TKNIGSLIGLEFRDSNFILNVKNDYRKIQRGDCFNISFGFNNLKDSQSANNYALQLADTV
+QIPLDETEPPRFLTNYTKAKSQISFYFNNEEEDNNKKKSSPATKVPSKPDRNSKILRTKL
+RGEARGGAEDAQKEQIRKENQKKLHEKLEKNGLLRFSAADANGPDSEPRQYFKKYESYVR
+DSQLPTNIRDLRIHVDWKSQTIILPIYGRPVPFHINSYKNGSKNEEGEYTYLRLNFNSPG
+SSGGISKKVEELPYEESADNQFVRSITLRSKDGDRMSETFKQIADLKKEATKREQERKAL
+ADVVQQDKLIENKTGRTKRLDQIFVRPNPDTKRVPSTVFIHENGIRFQSPLRTDSRIDIL
+FSNIKNLIFQSCKGELIVVIHIHLKNPILMGKKKIQDVQFYREASDMSVDETGGGRRGQS
+RFRRYGDEDELEQEQEERRKRAALDKEFKYFADAIAEASNGLLTVENTFRDLGFQGVPNR
+SAVFCMPTTDCLVQLIEPPFLVINLEEVEICILERVQFGLKNFDMVFVYKDFNKPVTHIN
+TVPIESLDFLKQWLTDMDIPYTVSTINLNWATIMKSLQDDPYQFFLDGGWNFLATGSDDE
+ASDESEEEVSEYEASEDDVSDESAFSEDEEGSEVDDDISGDESEDYTGDESEEGEDWDEL
+EKKAARADRGANFRD
+
+>sp|P39015|STM1_YEAST Suppressor protein STM1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=STM1 PE=1 SV=3
+MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGA
+IRDKTAGRRNNRSKDVTDSATTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAE
+KEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQANNQFNKVPEAKKVELDAERIE
+TAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGR
+GARKGNNTANATNSANTVQKNRNIDVSNLPSLA
+
+>sp|P53312|SUCB_YEAST Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=LSC2 PE=1 SV=1
+MYSRKSLSLISKCGQLSRLNAQAALQARRHLSIHEYRSAQLLREYGIGTPEGFPAFTPEE
+AFEAAKKLNTNKLVIKAQALTGGRGKGHFDTGYKSGVHMIESPQQAEDVAKEMLNHNLIT
+KQTGIAGKPVSAVYIVKRVDTKHEAYLSILMDRQTKKPMIIASSQGGMNIEEVAERTPDA
+IKKFSIETSKGLSPQMAKDVAKSLGFSPDAQDEAAKAVSNLYKIFMERDATQVEINPLSE
+IEHDPTHKIMCTDAKFGFDDNASFRQEKIYSWRDLSQEDPDEVKAKKYDLNFVKLKGNIG
+CLVNGAGLAMATMDVIKLNGGDPANFLDCGGGATPETIKQGFELILSNKNVDAIFVNIFG
+GIVRCDYVALGLVEAARELEVRVPIVARLQGTKVEEGRDIINKSGVKIYSFDELDPAAKK
+VVELTQN
+
+>sp|P15705|STI1_YEAST Heat shock protein STI1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=STI1 PE=1 SV=1
+MSLTADEYKQQGNAAFTAKDYDKAIELFTKAIEVSETPNHVLYSNRSACYTSLKKFSDAL
+NDANECVKINPSWSKGYNRLGAAHLGLGDLDEAESNYKKALELDASNKAAKEGLDQVHRT
+QQARQAQPDLGLTQLFADPNLIENLKKNPKTSEMMKDPQLVAKLIGYKQNPQAIGQDLFT
+DPRLMTIMATLMGVDLNMDDINQSNSMPKEPETSKSTEQKKDAEPQSDSTTSKENSSKAP
+QKEESKESEPMEVDEDDSKIEADKEKAEGNKFYKARQFDEAIEHYNKAWELHKDITYLNN
+RAAAEYEKGEYETAISTLNDAVEQGREMRADYKVISKSFARIGNAYHKLGDLKKTIEYYQ
+KSLTEHRTADILTKLRNAEKELKKAEAEAYVNPEKAEEARLEGKEYFTKSDWPNAVKAYT
+EMIKRAPEDARGYSNRAAALAKLMSFPEAIADCNKAIEKDPNFVRAYIRKATAQIAVKEY
+ASALETLDAARTKDAEVNNGSSAREIDQLYYKASQQRFQPGTSNETPEETYQRAMKDPEV
+AAIMQDPVMQSILQQAQQNPAALQEHMKNPEVFKKIQTLIAAGIIRTGR
+
+>sp|P38825|TOM71_YEAST Protein TOM71 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TOM71 PE=1 SV=1
+MAENSLLRFITKNKVAILATVSAGTAAVGAYVYYQQIKQQQQQQLKGTKDNRRQSEAFAG
+QNEDEADLKDDGSVVSGSNKRKKKKNKRKRNNKAKSGEGFDYPSLPNGEPDIAQLKGLSP
+SQRQAYAVQLKNRGNHFFTAKNFNEAIKYYQYAIELDPNEPVFYSNISACYISTGDLEKV
+IEFTTKALEIKPDHSKALLRRASANESLGNFTDAMFDLSVLSLNGDFDGASIEPMLERNL
+NKQAMKVLNENLSKDEGRGSQVLPSNTSLASFFGIFDSHLEVSSVNTSSNYDTAYALLSD
+ALQRLYSATDEGYLVANDLLTKSTDMYHSLLSANTVDDPLRENAALALCYTGIFHFLKNN
+LLDAQVLLQESINLHPTPNSYIFLALTLADKENSQEFFKFFQKAVDLNPEYPPTYYHRGQ
+MYFILQDYKNAKEDFQKAQSLNPENVYPYIQLACLLYKQGKFTESEAFFNETKLKFPTLP
+EVPTFFAEILTDRGDFDTAIKQYDIAKRLEEVQEKIHVGIGPLIGKATILARQSSQDPTQ
+LDEEKFNAAIKLLTKACELDPRSEQAKIGLAQLKLQMEKIDEAIELFEDSAILARTMDEK
+LQATTFAEAAKIQKRLRADPIISAKMELTLARYRAKGML
+
+>sp|P38349|UBX7_YEAST UBX domain-containing protein 7 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=UBX7 PE=1 SV=1
+MLEALFRDSVEEAINDSIKEGVVLAVYNTARDDQWLKSWFKGDDVSLDTLAEHSIWLRLV
+KDTEQFQLFEQVFPNVVVPSIYLIRAGKIELIIQGEDDRHWEKLLACIGIKDKKAGESSS
+RETNPGLAREEKSSRDVHRKNARERIAETTLEIQRREQLKQRKLAEEERERIIRLVRADR
+AERKALDETHHRTLDDDKPLDVHDYIKDAQKLHSSKCVLQIRMTDGKTLKHEFNSSETLN
+DVRKWVDVNRTDGDCPYSFHRGIPRVTFKDSDELKTLETLELTPRSALLLKPLETQNSGL
+SVTGMEGPSLLGRLYKGFSTWWHNDKDPEVTSQREETSKPNRHEVRSSTPLSGAASSSCF
+QYNNVREPVQSSAHASPMLTPSGTRYPSETNLTTSRSVSPNVFQFVNNDHQEDPEDPTTF
+NGNNVHLEKKKDEDKK
+
+>sp|P17255|VATA_YEAST V-type proton ATPase catalytic subunit A OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=VMA1 PE=1 SV=3
+MAGAIENARKEIKRISLEDHAESEYGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGE
+VIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETIYDGIQRPLKAIKEES
+QSIYIPRGIDTPALDRTIKWQFTPGKFQVGDHISGGDIYGSVFENSLISSHKILLPPRSR
+GTITWIAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRV
+LDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKGTNVLMADGSIEC
+IENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHKSDSSREVPELLKFTCNA
+THELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYPISEGPE
+RANELVESYRKASNKAYFEWTIEARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSK
+FHLTIEGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKE
+PQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGVKNIPSFLSTDNIGTRET
+FLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVVSVNAEPAKVDMNGTKH
+KISYAIYMSGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFYFELQELKEDDYYGITLS
+DDSDHQFLLANQVVVHNCGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSNMP
+VAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLG
+AKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDKKL
+AQRKHFPSINTSVSYSKYTNVLNKFYDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKS
+ALSDSDKITLDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGA
+NWSKLADSTGDVKHAVSSSKFFEPSRGEKEVHGEFEKLLSTMQERFAESTD
+
+>sp|Q12141|YG11B_YEAST Transposon Ty1-GR1 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-GR1 PE=3 SV=1
+MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+LYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNK
+RIIDKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYK
+SQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITK
+GLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P0CX74|YJ11A_YEAST Transposon Ty1-JR1 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-JR1 PE=2 SV=1
+MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|P0CX70|YD15A_YEAST Transposon Ty1-DR6 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-DR6 PE=2 SV=1
+MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|P0CX71|YE11A_YEAST Transposon Ty1-ER1 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-ER1 PE=2 SV=1
+MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|Q12085|YG11A_YEAST Transposon Ty1-GR1 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-GR1 PE=2 SV=1
+MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|P0CF21|YI168_YEAST Putative truncated L-serine dehydratase YIL168W OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=YIL168W PE=5 SV=1
+MEMTYYEKTPLIRQFLNNGKTNSWFYVKHEMLQPGGSFKSRGIGHLIRKSNEEALSEGSG
+KLAVFSSSGGNAGLAAATACRSMALNCSVVVPKTTKPRMVKKIQSAGAKVIIHGDHWGEA
+DEYLRHE
+
+>sp|P0CX72|YL12A_YEAST Transposon Ty1-LR2 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-LR2 PE=2 SV=1
+MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|P0C2I6|YL13B_YEAST Transposon Ty1-LR3 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-LR3 PE=3 SV=1
+MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSASQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKPISEINLRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSNNETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDPPPEP
+PTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAAKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+HYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK
+KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYK
+SQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P0C2I8|YL14A_YEAST Transposon Ty1-LR4 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-LR4 PE=2 SV=1
+MESQQLSQHPHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|P36072|YKL8_YEAST Putative uncharacterized protein YKL118W OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=YKL118W PE=5 SV=1
+MSSSIPSFDFALFLNFRRNSVILSFSLISNIRVLLCDANRQLSYLTFSSFLSAFSCEICF
+IFASSFLILNIHTSVMSTLSQLNTQDFCKTEYFVNNIIVRIQS
+
+>sp|P0C2I5|YL12B_YEAST Transposon Ty1-LR2 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-LR2 PE=3 SV=1
+MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAPTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+LYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK
+KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYK
+SQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P0CX73|YP11A_YEAST Transposon Ty1-PL Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-PL PE=2 SV=1
+MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|Q12273|YO11B_YEAST Transposon Ty1-OL Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-OL PE=3 SV=1
+MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+LYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK
+KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYK
+SQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|Q03612|YE11B_YEAST Transposon Ty1-ER1 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-ER1 PE=3 SV=1
+MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+LYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK
+KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYK
+SQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P0C2J1|YP14B_YEAST Transposon Ty1-PR3 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-PR3 PE=1 SV=1
+MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSASQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKPISEINLRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSNNETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDPPPEP
+PTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDRYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+HYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK
+KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYK
+SQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITK
+GLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|Q07589|YD144_YEAST Uncharacterized protein YDL144C OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=YDL144C PE=1 SV=2
+MSRILVIGAGGVGVITALSLWLKKESDVSLVVRSDYDRVLKHGYTIESCDYGRLEGWRPH
+HIYSSVEDAASAADNQGYNYIVVTTKNIIDGPVNSRVSNIIRPVLEKNKELHGPQLTTHI
+LLVQNGIDIEKEIWAEFPREQYRYTVLSGIQLIGSTKIGSGHISQVGQDHLSCGAFDPQD
+AAAIQAANDFVRMYSNEGQNFVEFDPRVRYSRWKKLLYNAAINTSTALVGLDVPRCLEFG
+VNKKSTEIEVFHPAMREIIAIAASEGIIIEEEFITMFTEITRKKVFKPSMCVDCEKGQLM
+ELEVILGNPIRIAKRNGVATPTLSILYNLLVLVQAKLKERKGLLKFDEKTATLVDE
+
+>sp|Q6Q5H1|YP14A_YEAST Transposon Ty1-PR3 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-PR3 PE=1 SV=2
+MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|P0C2I3|YD15B_YEAST Transposon Ty1-DR6 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-DR6 PE=3 SV=1
+MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNYLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+LYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNK
+RIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYK
+SQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P47098|YJ11B_YEAST Transposon Ty1-JR1 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-JR1 PE=3 SV=3
+MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYQSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+HYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK
+KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYK
+SQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P0CX76|YM12A_YEAST Transposon Ty1-ML2 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-ML2 PE=2 SV=1
+MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|Q03434|YM12B_YEAST Transposon Ty1-ML2 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-ML2 PE=3 SV=2
+MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDRSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+LYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK
+KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYK
+SQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P0C2I7|YL14B_YEAST Transposon Ty1-LR4 Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-LR4 PE=5 SV=1
+MESQQLSQHPHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+LYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNK
+RIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYK
+SQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P38079|YRO2_YEAST Protein YRO2 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=YRO2 PE=1 SV=1
+MSDYVELLKRGGNEAIKINPPTGADFHITSRGSDWLFTVFCVNLLFGVILVPLMFRKPVK
+DRFVYYTAIAPNLFMSIAYFTMASNLGWIPVRAKYNHVQTSTQKEHPGYRQIFYARYVGW
+FLAFPWPIIQMSLLGGTPLWQIAFNVGMTEIFTVCWLIAACVHSTYKWGYYTIGIGAAIV
+VCISLMTTTFNLVKARGKDVSNVFITFMSVIMFLWLIAYPTCFGITDGGNVLQPDSATIF
+YGIIDLLILSILPVLFMPLANYLGIERLGLIFDEEPAEHVGPVAEKKMPSPASFKSSDSD
+SSIKEKLKLKKKHKKDKKKAKKAKKAKKAKKAQEEEEDVATDSE
+
+>sp|Q92392|YO11A_YEAST Transposon Ty1-OL Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-OL PE=2 SV=1
+MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+
+>sp|Q12414|YP11B_YEAST Transposon Ty1-PL Gag-Pol polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1B-PL PE=3 SV=1
+MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASS
+NPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITAC
+FTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHR
+MLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQN
+SYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILA
+FIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLD
+DCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPV
+IVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFN
+YDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVS
+PTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGM
+HKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQI
+SDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPES
+PTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKN
+MRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQ
+LLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQS
+NTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKS
+LYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANK
+KIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPL
+NPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINT
+LAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYK
+SQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIK
+GLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKP
+LPIKTFKLLTNKWIH
+
+>sp|P31111|ZIP1_YEAST Synaptonemal complex protein ZIP1 OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=ZIP1 PE=1 SV=2
+MSNFFRDSSMGFKPRPNIFAKLRVRDVDSDSSANTVVENSSNCLDVGSSIEGDDTFKKPH
+KTSTEQELITSMSLSQRNHGYSDDMEIGSPKKTTSTDQYNRILKNDVAAIENDTDEDFEI
+TEVREVSEGVAKETKESHGDPNDSETTLKDSKMHEYTMTNGKAPLHTSINNSSTSSNDVL
+LEAFTNTQRICSNLKQELQKQQQDNAKLKVRLQSYASNSDKINEKVGKYKSCLETLQERI
+ATLTSHKNNQETKLKDLRQNHQLYQRRISGFKTSIENLNKTINDLGKNKKEADAELMKKG
+KEIEYLKRELDDCSGQLSEEKIKNSSLIQEMGKNREEMIKSIENFFSEDKAHHLLQFNKF
+EERVHDLFEKKLQKHFDVAKDTLNVGLRNTTVELSSNTETMLKQQYEDIKENLEQKMSSS
+KDEMAKTINELSVTQKGLIMGVQEELLTSSGNIQTALVSEMNNTRQELLDDASQTAKNYA
+SLENLVKAYKAEIVQSNEYEERIKHLESERSTLSSQKNQIISSLGTKEAQYEDLVKKLEA
+KNIEISQISGKEQSLTEKNENLSNELKKVQDQLEKLNNLNITTKSNYENKISSQNEIVKA
+LVSENDTLKQRIQQLVEIKENEQKDHTTKLEAFQKNNEQLQKLNVEVVQLKAHELELEEQ
+NRHLKNCLEKKETGVEESLSDVKTLKQQVIVLKSEKQDITAEKLELQDNLESLEEVTKNL
+QQKVQSQKRELEQKIKELEEIKNHKRNEPSKKGTQNFTKPSDSPKKNATTSNLFPNNSAA
+IHSPMKKCPKVDHISKSRINSSKETSKFNDEFDLSSSSNDDLELTNPSPIQIKPVRGKIK
+KGSNCMKPPISSRKKLLLVEDEDQSLKISKKRRRK
+
+>sp|P0CX75|YL13A_YEAST Transposon Ty1-LR3 Gag polyprotein OS=Saccharomyces cerevisiae (strain ATCC 204508 / S288c) GN=TY1A-LR3 PE=2 SV=1
+MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPAS
+SAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPM
+YFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPND
+FPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDI
+LSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNN
+GIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNY
+RRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKS
+TTEPIQLNNKHDLHLRPGTY
+

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/test-data/SmallYeastGPTMD.xml	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,1911 @@
+<?xml version="1.0" encoding="utf-8"?>
+<mzLibProteinDb>
+  <modification>ID   Ammonia loss on N
+MT   Common Artifact
+TG   N
+PP   Anywhere.
+CF   H-3N-1
+MM   -17.026549101
+DR   Unimod; 385
+
+//</modification>
+  <modification>ID   Citrullination on R
+MT   Common Biological
+TG   R
+PP   Anywhere.
+CF   H-1N-1O
+MM   0.984015583
+DR   Unimod; 7
+NL   HCD:43.0058
+DI   HCD:129.090223533
+
+//</modification>
+  <modification>ID   Deamidation on N
+MT   Common Artifact
+TG   N
+PP   Anywhere.
+CF   H-1N-1O
+MM   0.984015583
+DR   Unimod; 7
+
+//</modification>
+  <modification>ID   Deamidation on Q
+MT   Common Artifact
+TG   Q
+PP   Anywhere.
+CF   H-1N-1O
+MM   0.984015583
+DR   Unimod; 7
+
+//</modification>
+  <modification>ID   Dimethylation on K
+MT   Common Biological
+TG   K
+PP   Anywhere.
+CF   C2H4
+MM   28.031300129
+DR   Unimod; 36
+
+//</modification>
+  <modification>ID   Hydroxylation on K
+MT   Common Biological
+TG   K
+PP   Anywhere.
+CF   O
+MM   15.99491462
+DR   Unimod; 35
+
+//</modification>
+  <modification>ID   Hydroxylation on N
+MT   Common Biological
+TG   N
+PP   Anywhere.
+CF   O
+MM   15.99491462
+DR   Unimod; 35
+
+//</modification>
+  <modification>ID   Hydroxylation on P
+MT   Common Biological
+TG   P
+PP   Anywhere.
+CF   O
+MM   15.99491462
+DR   Unimod; 35
+DI   HCD:170.060123533
+
+//</modification>
+  <modification>ID   Methylation on K
+MT   Common Biological
+TG   K
+PP   Anywhere.
+CF   CH2
+MM   14.015650064
+DR   Unimod; 34
+
+//</modification>
+  <modification>ID   Methylation on R
+MT   Common Biological
+TG   R
+PP   Anywhere.
+CF   CH2
+MM   14.015650064
+DR   Unimod; 34
+
+//</modification>
+  <modification>ID   Succinylation on K
+MT   Common Biological
+TG   K
+PP   Anywhere.
+CF   C4H4O3
+MM   100.016043988
+DR   Unimod; 64
+NL   ETD:101.0239
+DI   HCD:183.089523533
+
+//</modification>
+  <modification>ID   Trimethylation on K
+MT   Common Biological
+TG   K
+PP   Anywhere.
+CF   C3H6
+MM   42.046950193
+DR   Unimod; 37
+NL   ETD:45.0204
+
+//</modification>
+  <entry>
+    <accession>P38013</accession>
+    <name>Peroxiredoxin type-2</name>
+    <protein>
+      <recommendedName>
+        <fullName>Peroxiredoxin type-2</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">AHP1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="176">MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSPTCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGCAFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL</sequence>
+  </entry>
+  <entry>
+    <accession>P46672</accession>
+    <name>tRNA-aminoacylation cofactor ARC1</name>
+    <protein>
+      <recommendedName>
+        <fullName>tRNA-aminoacylation cofactor ARC1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">ARC1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="376">MSDLVTKFESLIISKYPVSFTKEQSAQAAQWESVLKSGQIQPHLDQLNLVLRDNTFIVSTLYPTSTDVHVFEVALPLIKDLVASSKDVKSTYTTYRHILRWIDYMQNLLEVSSTDKLEINHDLDLPHEVIEKKKKAPAGGAADAAAKADEDVSKKAKKQDHPRGKPDEETLKKLREEAKAKKAAKKAANAKQQQEQQNKAPEKPKPSAIDFRVGFIQKAIKHPDADSLYVSTIDVGDEEGPRTVCSGLVKHFPLDAMQERYVVVVCNLKPVNMRGIKSTAMVLCGSNDDKVEFVEPPKDSKAGDKVFFEGFGDEAPMKQLNPKKKIWEHLQPHFTTNDGLEVIFKDEEEKDHPVRKLTNAKGESFKVASIANAQVR</sequence>
+  </entry>
+  <entry>
+    <accession>Q01389</accession>
+    <name>Serine/threonine-protein kinase BCK1/SLK1/SSP31</name>
+    <protein>
+      <recommendedName>
+        <fullName>Serine/threonine-protein kinase BCK1/SLK1/SSP31</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">BCK1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1478">MPFLRKIAGTAHTHSRSDSNSSVKFGHQPTSSVASTKSSSKSPRATSRKSIYDDIRSQFPNLTPNSTSSQFYESTPVIEQSFNWTTDDHISAGTLENPTSFTNSSYKNDNGPSSLSDSRKSSGGNSVNSLSFDKLILSWDPTDPDEWTMHRVTSWFKFHDFPESWILFFKKHQLFGHRFIKLLAYDNFAVYEKYLPQTKTASYTRFQQLLKKTMTKNVTNSHIRQKSASKLKSSRSSSESIKSKLKNSKSQEDISNSRSTSESALSPTKSGPSKTDEKNFLHSTSTHQKTKSASSLYRRSFISLRGSSSSNASSAKSPSNIKLSIPARPHSIIESNSTLTKSASPPASPSYPSIFRRHHKSSSSESSLLNSLFGSGIGEEAPTKPNPQGHSLSSENLAKGKSKHYETNVSSPLKQSSLPTSDDKGNLWNKFKRKSQIGVPSPNTVAYVTSQETPSLKSNSSTATLTVQTADVNIPSPSSSPPPIPKTANRSLEVISTEDTPKISSTTASFKETYPDCINPDKTVPVPVNNQKYSVKNFLLDQKFYPLKKTGLNDSENKYILVTKDNVSFVPLNLKSVAKLSSFKESALTKLGINHKNVTFHMTDFDCDIGAAIPDDTLEFLKKSLFLNTSGKIYIKDQMKLQQKPKPAPLTSENNVPLKSVKSKSSMRSGTSSLIASTDDVSIVTSSSDITSFDEHASGSGRRYPQTPSYYYDRVSNTNPTEELNYWNIKEVLSHEENAPKMVFKTSPKLELNLPDKGSKLNIPTPITENESKSSFQVLRKDEGTEIDFNHRRESPYTKPELAPKREAPKPPANTSPQRTLSTSKQNKPIRLVRASTKISRSKRSKPLPPQLLSSPIEASSSSPDSLTSSYTPASTHVLIPQPYKGANDVMRRLKTDQDSTSTSPSLKMKQKVNRSNSTVSTSNSIFYSPSPLLKRGNSKRVVSSTSAADIFEENDITFADAPPMFDSDDSDDDSSSSDDIIWSKKKTAPETNNENKKDEKSDNSSTHSDEIFYDSQTQDKMERKMTFRPSPEVVYQNLEKFFPRANLDKPITEGIASPTSPKSLDSLLSPKNVASSRTEPSTPSRPVPPDSSYEFIQDGLNGKNKPLNQAKTPKRTKTIRTIAHEASLARKNSVKLKRQNTKMWGTRMVEVTENHMVSINKAKNSKGEYKEFAWMKGEMIGKGSFGAVYLCLNVTTGEMMAVKQVEVPKYSSQNEAILSTVEALRSEVSTLKDLDHLNIVQYLGFENKNNIYSLFLEYVAGGSVGSLIRMYGRFDEPLIKHLTTQVLKGLAYLHSKGILHRDMKADNLLLDQDGICKISDFGISRKSKDIYSNSDMTMRGTVFWMAPEMVDTKQGYSAKVDIWSLGCIVLEMFAGKRPWSNLEVVAAMFKIGKSKSAPPIPEDTLPLISQIGRNFLDACFEINPEKRPTANELLSHPFSEVNETFNFKSTRLAKFIKSNDKLNSSKLRITSQENKTE</sequence>
+  </entry>
+  <entry>
+    <accession>P07267</accession>
+    <name>Saccharopepsin</name>
+    <protein>
+      <recommendedName>
+        <fullName>Saccharopepsin</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">PEP4</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="405">MFSLKALLPLALLLVSANQVAAKVHKAKIYKHELSDEMKEVTFEQHLAHLGQKYLTQFEKANPEVVFSREHPFFTEGGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLACFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQDFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEKRFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEGIGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGWTGQYTLDCNTRDNLPDLIFNFNGYNFTIGPYDYTLEVSGSCISAITPMDFPEPVGPLAIVGDAFLRKYYSIYDLGNNAVGLAKAI</sequence>
+  </entry>
+  <entry>
+    <accession>P29547</accession>
+    <name>Elongation factor 1-gamma 1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Elongation factor 1-gamma 1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">CAM1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="415">MSQGTLYANFRIRTWVPRGLVKALKLDVKVVTPDAAAEQFARDFPLKKVPAFVGPKGYKLTEAMAINYYLVKLSQDDKMKTQLLGADDDLNAQAQIIRWQSLANSDLCIQIANTIVPLKGGAPYNKKSVDSAMDAVDKIVDIFENRLKNYTYLATENISLADLVAASIFTRYFESLFGTEWRAQHPAIVRWFNTVRASPFLKDEYKDFKFADKPLSPPQKKKEKKAPAAAPAASKKKEEAKPAATETETSSKKPKHPLELLGKSTFVLDDWKRKYSNEDTRPVALPWFWEHYNPEEYSLWKVTYKYNDELTLTFMSNNLVGGFFNRLSASTKYMFGCLVVYGENNNNGIVGAVMVRGQDYVPAFDVAPDWESYDYAKLDPTNDDDKEFINNMWAWDKPVSVNGEPKEIVDGKVLK</sequence>
+  </entry>
+  <entry>
+    <accession>P43616</accession>
+    <name>Cys-Gly metallodipeptidase DUG1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Cys-Gly metallodipeptidase DUG1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">DUG1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="481">MSHSLTSVFQKIDSLKPQFFSRLTKAIQIPAVSSDESLRSKVFDKAKFISEQLSQSGFHDIKMVDLGIQPPPISTPNLSLPPVILSRFGSDPSKKTVLVYGHYDVQPAQLEDGWDTEPFKLVIDEAKGIMKGRGVTDDTGPLLSWINVVDAFKASGQEFPVNLVTCFEGMEESGSLKLDELIKKEANGYFKGVDAVCISDNYWLGTKKPVLTYGLRGCNYYQTIIEGPSADLHSGIFGGVVAEPMIDLMQVLGSLVDSKGKILIDGIDEMVAPLTEKEKALYKDIEFSVEELNAATGSKTSLYDKKEDILMHRWRYPSLSIHGVEGAFSAQGAKTVIPAKVFGKFSIRTVPDMDSEKLTSLVQKHCDAKFKSLNSPNKCRTELIHDGAYWVSDPFNAQFTAAKKATKLVYGVDPDFTREGGSIPITLTFQDALNTSVLLLPMGRGDDGAHSINEKLDISNFVGGMKTMAAYLQYYSESPEN</sequence>
+  </entry>
+  <entry>
+    <accession>P02994</accession>
+    <name>Elongation factor 1-alpha</name>
+    <protein>
+      <recommendedName>
+        <fullName>Elongation factor 1-alpha</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TEF1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="384" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on P">
+      <location>
+        <position position="389" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="390" />
+      </location>
+    </feature>
+    <sequence length="458">MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKEIRRGNVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLDCHTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVKFVPSKPMCVEAFSEYPPLGRFAVRDMRQTVAVGVIKSVDKTEKAAKVTKAAQKAAKK</sequence>
+  </entry>
+  <entry>
+    <accession>P16521</accession>
+    <name>Elongation factor 3A</name>
+    <protein>
+      <recommendedName>
+        <fullName>Elongation factor 3A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">YEF3</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Dimethylation on K">
+      <location>
+        <position position="902" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Methylation on K">
+      <location>
+        <position position="902" />
+      </location>
+    </feature>
+    <sequence length="1044">MSDSQQSIKVLEELFQKLSVATADNRHEIASEVASFLNGNIIEHDVPEHFFGELAKGIKDKKTAANAMQAVAHIANQSNLSPSVEPYIVQLVPAICTNAGNKDKEIQSVASETLISIVNAVNPVAIKALLPHLTNAIVETNKWQEKIAILAAISAMVDAAKDQVALRMPELIPVLSETMWDTKKEVKAAATAAMTKATETVDNKDIERFIPSLIQCIADPTEVPETVHLLGATTFVAEVTPATLSIMVPLLSRGLNERETGIKRKSAVIIDNMCKLVEDPQVIAPFLGKLLPGLKSNFATIADPEAREVTLRALKTLRRVGNVGEDDAIPEVSHAGDVSTTLQVVNELLKDETVAPRFKIVVEYIAAIGADLIDERIIDQQAWFTHITPYMTIFLHEKKAKDILDEFRKRAVDNIPVGPNFDDEEDEGEDLCNCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVDGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVKKCPAAKAYEELSNTDLEFKFPEPGYLEGVKTKQKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAHIESHLDKTPSEYIQWRFQTGEDRETMDRANRQINENDAEAMNKIFKIEGTPRRIAGIHSRRKFKNTYEYECSFLLGENIGMKSERWVPMMSVDNAWIPRGELVESHSKMVAEVDMKEALASGQFRPLTRKEIEEHCSMLGLDPEIVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSGHNWVSGQGAGPRIEKKEDEEDKFDAMGNKIAGGKKKKKLSSAELRKKKKERMKKKKELGDAYVSSDEEF</sequence>
+  </entry>
+  <entry>
+    <accession>P53911</accession>
+    <name>Chromatin modification-related protein EAF7</name>
+    <protein>
+      <recommendedName>
+        <fullName>Chromatin modification-related protein EAF7</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">EAF7</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="425">MVVHWTIVDEIRLLRWASEFKPAGIHKHFHMFCIVERMNSPDKYPVTLLQKETMKLGKVFTAKDIWDKLSQSYNLEKIDEMENTYSLEATTESSRNGNGNGDDAEIHEETLLELNNRIRVRKQDFTLPWEEYGELILENARKSPNSNEEYPRVEDMNEKDSTIPKESPSTDLKNDNNKQEKNATIKVKELPEYHTEENDSPIDVQKEPIKEVQSDEKELQREHMSEEEQKMKSTNKTAAPVRKSQRLKRSKEVKFEDEEKEEIEEDNTKDEEQKEKKEEIQEPKITHNEEVDKEKNENEEGDDEREKSTSYENTNGSESEGVDEGVDEELGYESEREAEGKGKQIESEGGNLKKKTENKKGDDQQDDTKKDSKDKNEPLAKRTRHSSSTGNTSNETSPKRKRRKAGSRKNSPPATRVSSRLRNKK</sequence>
+  </entry>
+  <entry>
+    <accession>P00359</accession>
+    <name>Glyceraldehyde-3-phosphate dehydrogenase 3</name>
+    <protein>
+      <recommendedName>
+        <fullName>Glyceraldehyde-3-phosphate dehydrogenase 3</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TDH3</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="332">MVRVAINGFGRIGRLVMRIALSRPNVEVVALNDPFITNDYAAYMFKYDSTHGRYAGEVSHDDKHIIVDGKKIATYQERDPANLPWGSSNVDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSLTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSHSSIFDASAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA</sequence>
+  </entry>
+  <entry>
+    <accession>P00358</accession>
+    <name>Glyceraldehyde-3-phosphate dehydrogenase 2</name>
+    <protein>
+      <recommendedName>
+        <fullName>Glyceraldehyde-3-phosphate dehydrogenase 2</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TDH2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="332">MVRVAINGFGRIGRLVMRIALQRKNVEVVALNDPFISNDYSAYMFKYDSTHGRYAGEVSHDDKHIIVDGHKIATFQERDPANLPWASLNIDIAIDSTGVFKELDTAQKHIDAGAKKVVITAPSSTAPMFVMGVNEEKYTSDLKIVSNASCTTNCLAPLAKVINDAFGIEEGLMTTVHSMTATQKTVDGPSHKDWRGGRTASGNIIPSSTGAAKAVGKVLPELQGKLTGMAFRVPTVDVSVVDLTVKLNKETTYDEIKKVVKAAAEGKLKGVLGYTEDAVVSSDFLGDSNSSIFDAAAGIQLSPKFVKLVSWYDNEYGYSTRVVDLVEHVAKA</sequence>
+  </entry>
+  <entry>
+    <accession>P24583</accession>
+    <name>Protein kinase C-like 1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Protein kinase C-like 1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">PKC1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1151">MSFSQLEQNIKKKIAVEENIIRGASALKKKTSNVMVIQKCNTNIREARQNLEYLEDSLKKLRLKTAQQSQGENGSEDNERCNSKEYGFLSTKSPNEHIFSRLDLVKYDCPSLAQRIQYMLQQLEFKLQVEKQYQEANTKLTKLYQIDGDQRSSSAAEGGAMESKYRIQMLNKALKKYQAINVDFDQFKHQPNDIMDNQQPKFRRKQLTGVLTIGITAARDVDHIQSPMFARKPESYVTIKIDDTIKARTKPSRNDRWSEDFQIPVEKGNEIEITVYDKVNDSLIPVAIMWLLLSDIAEEIRKKKAGQTNEQQGWVNASNINGGSSLASEEGSTLTSTYSNSAIQSTSAKNVQGENTSTSQISTNSWFVLEPSGQILLTLGFHKSSQIERKQLMGGLHRHGAIINRKEEIFEQHGHHFVQKSFYNIMCCAYCGDFLRYTGFQCQDCKFLCHKKCYTNVVTKCIAKTSTDTDPDEAKLNHRIPHRFLPTSNRGTKWCCHCGYILPWGRHKVRKCSECGIMCHAQCAHLVPDFCGMSMEMANKILKTIQDTKRNQEKKKRTVPSAQLGSSIGTANGSDLSPSKLAERANAPLPPQPRKHDKTPSPQKVGRDSPTKQHDPIIDKRISLQTHGREKLNKFIDENEAYLNFTEGAQQTAEFSSPEKTLDPTSNRRSLGLTDLSIEHSQTWESKDDLMRDELELWKAQREEMELEIKQDSGEIQEDLEVDHIDLETKQKLDWENKNDFREADLTIDSTHTNPFRDMNSETFQIEQDHASKEVLQETVSLAPTSTHASRTTDQQSPQKSQTSTSAKHKKRAAKRRKVSLDNFVLLKVLGKGNFGKVILSKSKNTDRLCAIKVLKKDNIIQNHDIESARAEKKVFLLATKTKHPFLTNLYCSFQTENRIYFAMEFIGGGDLMWHVQNQRLSVRRAKFYAAEVLLALKYFHDNGVIYRDLKLENILLTPEGHIKIADYGLCKDEMWYGNRTSTFCGTPEFMAPEILKEQEYTKAVDWWAFGVLLYQMLLCQSPFSGDDEDEVFNAILTDEPLYPIDMAGEIVQIFQGLLTKDPEKRLGAGPRDADEVMEEPFFRNINFDDILNLRVKPPYIPEIKSPEDTSYFEQEFTSAPPTLTPLPSVLTTSQQEEFRGFSFMPDDLDL</sequence>
+  </entry>
+  <entry>
+    <accession>Q12460</accession>
+    <name>Nucleolar protein 56</name>
+    <protein>
+      <recommendedName>
+        <fullName>Nucleolar protein 56</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">NOP56</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="504">MAPIEYLLFEEPTGYAVFKVKLQQDDIGSRLKEVQEQINDFGAFTKLIELVSFAPFKGAAEALENANDISEGLVSESLKAILDLNLPKASSKKKNITLAISDKNLGPSIKEEFPYVDCISNELAQDLIRGVRLHGEKLFKGLQSGDLERAQLGLGHAYSRAKVKFSVQKNDNHIIQAIALLDQLDKDINTFAMRVKEWYGWHFPELAKLVPDNYTFAKLVLFIKDKASLNDDSLHDLAALLNEDSGIAQRVIDNARISMGQDISETDMENVCVFAQRVASLADYRRQLYDYLCEKMHTVAPNLSELIGEVIGARLISHAGSLTNLSKQAASTVQILGAEKALFRALKTKGNTPKYGLIYHSGFISKASAKNKGRISRYLANKCSMASRIDNYSEEPSNVFGSVLKKQVEQRLEFYNTGKPTLKNELAIQEAMELYNKDKPAAEVEETKEKESSKKRKLEDDDEEKKEKKEKKSKKEKKEKKEKKDKKEKKDKKEKKDKKKKSKD</sequence>
+  </entry>
+  <entry>
+    <accession>Q99207</accession>
+    <name>Nucleolar complex protein 14</name>
+    <protein>
+      <recommendedName>
+        <fullName>Nucleolar complex protein 14</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">NOP14</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="810">MAGSQLKNLKAALKARGLTGQTNVKSKNKKNSKRQAKEYDREEKKKAIAEIREEFNPFEIKAARNKRRDGLPSKTADRIAVGKPGISKQIGEEQRKRAFEARKMMKNKRGGVIDKRFGERDKLLTEEEKMLERFTRERQSQSKRNANLFNLEDDEDDGDMFGDGLTHLGQSLSLEDELANDEEDFLASKRFNEDDAELQQPQRKKTKAEVMKEVIAKSKFYKQERQKAQGIMEDQIDNLDDNFEDVMSELMMTQPKKNPMEPKTDLDKEYDIKVKELQLDKRAAPSDRTKTEEEKNAEAEEKKRELEQQRLDRMNGMIELEEGEERGVEDLDDGFWENEEDYEDDNDGIADSDDDIKFEDQGRDEGFSQILKKKNISISCPRTHDALLDQVKKLDLDDHPKIVKNIIKAYQPKLAEGNKEKLGKFTAVLLRHIIFLSNQNYLKNVQSFKRTQNALISILKSLSEKYNRELSEECRDYINEMQARYKKNHFDALSNGDLVFFSIIGILFSTSDQYHLVITPALILMSQFLEQIKFNSLKRIAFGAVLVRIVSQYQRISKRYIPEVVYFFQKILLTFIVEKENQEKPLDFENIRLDSYELGLPLDVDFTKKRSTIIPLHTLSTMDTEAHPVDQCVSVLLNVMESLDATISTVWKSLPAFNEIILPIQQLLSAYTSKYSDFEKPRNILNKVEKLTKFTEHIPLALQNHKPVSIPTHAPKYEENFNPDKKSYDPDRTRSEINKMKAQLKKERKFTMKEIRKDAKFEARQRIEEKNKESSDYHAKMAHIVNTINTEEGAEKNKYERERKLRGGKK</sequence>
+  </entry>
+  <entry>
+    <accession>P54784</accession>
+    <name>Origin recognition complex subunit 1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Origin recognition complex subunit 1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">ORC1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="914">MAKTLKDLQGWEIITTDEQGNIIDGGQKRLRRRGAKTEHYLKRSSDGIKLGRGDSVVMHNEAAGTYSVYMIQELRLNTLNNVVELWALTYLRWFEVNPLAHYRQFNPDANILNRPLNYYNKLFSETANKNELYLTAELAELQLFNFIRVANVMDGSKWEVLKGNVDPERDFTVRYICEPTGEKFVDINIEDVKAYIKKVEPREAQEYLKDLTLPSKKKEIKRGPQKKDKATQTAQISDAETRATDITDNEDGNEDESSDYESPSDIDVSEDMDSGEISADELEEEEDEEEDEDEEEKEARHTNSPRKRGRKIKLGKDDIDASVQPPPKKRGRKPKDPSKPRQMLLISSCRANNTPVIRKFTKKNVARAKKKYTPFSKRFKSIAAIPDLTSLPEFYGNSSELMASRFENKLKTTQKHQIVETIFSKVKKQLNSSYVKEEILKSANFQDYLPARENEFASIYLSAYSAIESDSATTIYVAGTPGVGKTLTVREVVKELLSSSAQREIPDFLYVEINGLKMVKPTDCYETLWNKVSGERLTWAASMESLEFYFKRVPKNKKKTIVVLLDELDAMVTKSQDIMYNFFNWTTYENAKLIVIAVANTMDLPERQLGNKITSRIGFTRIMFTGYTHEELKNIIDLRLKGLNDSFFYVDTKTGNAILIDAAGNDTTVKQTLPEDVRKVRLRMSADAIEIASRKVASVSGDARRALKVCKRAAEIAEKHYMAKHGYGYDGKTVIEDENEEQIYDDEDKDLIESNKAKDDNDDDDDNDGVQTVHITHVMKALNETLNSHVITFMTRLSFTAKLFIYALLNLMKKNGSQEQELGDIVDEIKLLIEVNGSNKFVMEIAKTLFQQGSDNISEQLRIISWDFVLNQLLDAGILFKQTMKNDRICCVKLNISVEEAKRAMNEDETLRNL</sequence>
+  </entry>
+  <entry>
+    <accession>P06169</accession>
+    <name>Pyruvate decarboxylase isozyme 1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Pyruvate decarboxylase isozyme 1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">PDC1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="563">MSEITLGKYLFERLKQVNVNTVFGLPGDFNLSLLDKIYEVEGMRWAGNANELNAAYAADGYARIKGMSCIITTFGVGELSALNGIAGSYAEHVGVLHVVGVPSISAQAKQLLLHHTLGNGDFTVFHRMSANISETTAMITDIATAPAEIDRCIRTTYVTQRPVYLGLPANLVDLNVPAKLLQTPIDMSLKPNDAESEKEVIDTILALVKDAKNPVILADACCSRHDVKAETKKLIDLTQFPAFVTPMGKGSIDEQHPRYGGVYVGTLSKPEVKEAVESADLILSVGALLSDFNTGSFSYSYKTKNIVEFHSDHMKIRNATFPGVQMKFVLQKLLTTIADAAKGYKPVAVPARTPANAAVPASTPLKQEWMWNQLGNFLQEGDVVIAETGTSAFGINQTTFPNNTYGISQVLWGSIGFTTGATLGAAFAAEEIDPKKRVILFIGDGSLQLTVQEISTMIRWGLKPYLFVLNNDGYTIEKLIHGPKAQYNEIQGWDHLSLLPTFGAKDYETHRVATTGEWDKLTQDKSFNDNSKIRMIEIMLPVFDAPQNLVEQAKLTAATNAKQ</sequence>
+  </entry>
+  <entry>
+    <accession>P02293</accession>
+    <name>Histone H2B.1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Histone H2B.1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">HTB1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="131">MSAKAEKKPASKAPAEKKPAAKKTSTSTDGKKRSKARKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA</sequence>
+  </entry>
+  <entry>
+    <accession>P02294</accession>
+    <name>Histone H2B.2</name>
+    <protein>
+      <recommendedName>
+        <fullName>Histone H2B.2</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">HTB2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Trimethylation on K">
+      <location>
+        <position position="23" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Dimethylation on K">
+      <location>
+        <position position="23" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Methylation on K">
+      <location>
+        <position position="23" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Trimethylation on K">
+      <location>
+        <position position="31" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Dimethylation on K">
+      <location>
+        <position position="31" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Methylation on K">
+      <location>
+        <position position="31" />
+      </location>
+    </feature>
+    <sequence length="131">MSSAAEKKPASKAPAEKKPAAKKTSTSVDGKKRSKVRKETYSSYIYKVLKQTHPDTGISQKSMSILNSFVNDIFERIATEASKLAAYNKKSTISAREIQTAVRLILPGELAKHAVSEGTRAVTKYSSSTQA</sequence>
+  </entry>
+  <entry>
+    <accession>P15108</accession>
+    <name>ATP-dependent molecular chaperone HSC82</name>
+    <protein>
+      <recommendedName>
+        <fullName>ATP-dependent molecular chaperone HSC82</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">HSC82</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="705">MAGETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYQALSDPKQLETEPDLFIRITPKPEEKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKNNEDEQYIWESNAGGSFTVTLDEVNERIGRGTVLRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLLVTKEVEKEVPIPEEEKKDEEKKDEDDKKPKLEEVDEEEEEKKPKTKKVKEEVQELEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFDKFYSAFAKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKDILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTNLLFETALLTSGFSLEEPTSFASRINRLISLGLNIDEDEETETAPEASTEAPVEEVPADTEMEEVD</sequence>
+  </entry>
+  <entry>
+    <accession>P10591</accession>
+    <name>Heat shock protein SSA1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Heat shock protein SSA1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">SSA1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="248" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on N">
+      <location>
+        <position position="253" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Ammonia loss on N">
+      <location>
+        <position position="253" />
+      </location>
+    </feature>
+    <sequence length="642">MSKAVGIDLGTTYSCVAHFANDRVDIIANDQGNRTTPSFVAFTDTERLIGDAAKNQAAMNPSNTVFDAKRLIGRNFNDPEVQADMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTKKSEIFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADKDTVTKKAEETISWLDSNTTASKEEFDDKLKELQDIANPIMSKLYQAGGAPGGAAGGAPGGFPGGAPPAPEAEGPTVEEVD</sequence>
+  </entry>
+  <entry>
+    <accession>P10592</accession>
+    <name>Heat shock protein SSA2</name>
+    <protein>
+      <recommendedName>
+        <fullName>Heat shock protein SSA2</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">SSA2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="248" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on N">
+      <location>
+        <position position="253" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Ammonia loss on N">
+      <location>
+        <position position="253" />
+      </location>
+    </feature>
+    <sequence length="639">MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGDMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADKDAVTKKAEETIAWLDSNTTATKEEFDDQLKELQEVANPIMSKLYQAGGAPEGAAPGGFPGGAPPAPEAEGPTVEEVD</sequence>
+  </entry>
+  <entry>
+    <accession>P0CS90</accession>
+    <name>Heat shock protein SSC1, mitochondrial</name>
+    <protein>
+      <recommendedName>
+        <fullName>Heat shock protein SSC1, mitochondrial</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">SSC1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="654">MLAAKNILNRSSLSSSFRIATRLQSTKVQGSVIGIDLGTTNSAVAIMEGKVPKIIENAEGSRTTPSVVAFTKEGERLVGIPAKRQAVVNPENTLFATKRLIGRRFEDAEVQRDIKQVPYKIVKHSNGDAWVEARGQTYSPAQIGGFVLNKMKETAEAYLGKPVKNAVVTVPAYFNDSQRQATKDAGQIVGLNVLRVVNEPTAAALAYGLEKSDSKVVAVFDLGGGTFDISILDIDNGVFEVKSTNGDTHLGGEDFDIYLLREIVSRFKTETGIDLENDRMAIQRIREAAEKAKIELSSTVSTEINLPFITADASGPKHINMKFSRAQFETLTAPLVKRTVDPVKKALKDAGLSTSDISEVLLVGGMSRMPKVVETVKSLFGKDPSKAVNPDEAVAIGAAVQGAVLSGEVTDVLLLDVTPLSLGIETLGGVFTRLIPRNTTIPTKKSQIFSTAAAGQTSVEIRVFQGERELVRDNKLIGNFTLAGIPPAPKGVPQIEVTFDIDADGIINVSARDKATNKDSSITVAGSSGLSENEIEQMVNDAEKFKSQDEARKQAIETANKADQLANDTENSLKEFEGKVDKAEAQKVRDQITSLKELVARVQGGEEVNAEELKTKTEELQTSSMKLFEQLYKNDSNNNNNNNGNNAESGETKQ</sequence>
+  </entry>
+  <entry>
+    <accession>P40576</accession>
+    <name>Inner membrane assembly complex subunit 22</name>
+    <protein>
+      <recommendedName>
+        <fullName>Inner membrane assembly complex subunit 22</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">INA22</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="216">MFMARQVLRNGLFLRSLAPIKITARTVASANAGIKRKSRFDKTMIKPLLLVMIFGSILNAVIAEKRNIIDMERKYKLKLDKLKELIRRVHDNNGKVDFDADDELKLVNLRLGIVGKNATGMKEDETDIVVPKEESLEEIWQSIIDEAKKEVIEKTPDAGVKNKEGIVTDLNVLKDLEKSKKEDEKVYLSGDVHMMMNQPGDLNEIAKEHDKIPKFL</sequence>
+  </entry>
+  <entry>
+    <accession>P02829</accession>
+    <name>ATP-dependent molecular chaperone HSP82</name>
+    <protein>
+      <recommendedName>
+        <fullName>ATP-dependent molecular chaperone HSP82</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">HSP82</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="709">MASETFEFQAEITQLMSLIINTVYSNKEIFLRELISNASDALDKIRYKSLSDPKQLETEPDLFIRITPKPEQKVLEIRDSGIGMTKAELINNLGTIAKSGTKAFMEALSAGADVSMIGQFGVGFYSLFLVADRVQVISKSNDDEQYIWESNAGGSFTVTLDEVNERIGRGTILRLFLKDDQLEYLEEKRIKEVIKRHSEFVAYPIQLVVTKEVEKEVPIPEEEKKDEEKKDEEKKDEDDKKPKLEEVDEEEEKKPKTKKVKEEVQEIEELNKTKPLWTRNPSDITQEEYNAFYKSISNDWEDPLYVKHFSVEGQLEFRAILFIPKRAPFDLFESKKKKNNIKLYVRRVFITDEAEDLIPEWLSFVKGVVDSEDLPLNLSREMLQQNKIMKVIRKNIVKKLIEAFNEIAEDSEQFEKFYSAFSKNIKLGVHEDTQNRAALAKLLRYNSTKSVDELTSLTDYVTRMPEHQKNIYYITGESLKAVEKSPFLDALKAKNFEVLFLTDPIDEYAFTQLKEFEGKTLVDITKDFELEETDEEKAEREKEIKEYEPLTKALKEILGDQVEKVVVSYKLLDAPAAIRTGQFGWSANMERIMKAQALRDSSMSSYMSSKKTFEISPKSPIIKELKKRVDEGGAQDKTVKDLTKLLYETALLTSGFSLDEPTSFASRINRLISLGLNIDEDEETETAPEASTAAPVEEVPADTEMEEVD</sequence>
+  </entry>
+  <entry>
+    <accession>P32589</accession>
+    <name>Heat shock protein homolog SSE1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Heat shock protein homolog SSE1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">SSE1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="693">MSTPFGLDLGNNNSVLAVARNRGIDIVVNEVSNRSTPSVVGFGPKNRYLGETGKNKQTSNIKNTVANLKRIIGLDYHHPDFEQESKHFTSKLVELDDKKTGAEVRFAGEKHVFSATQLAAMFIDKVKDTVKQDTKANITDVCIAVPPWYTEEQRYNIADAARIAGLNPVRIVNDVTAAGVSYGIFKTDLPEGEEKPRIVAFVDIGHSSYTCSIMAFKKGQLKVLGTACDKHFGGRDFDLAITEHFADEFKTKYKIDIRENPKAYNRILTAAEKLKKVLSANTNAPFSVESVMNDVDVSSQLSREELEELVKPLLERVTEPVTKALAQAKLSAEEVDFVEIIGGTTRIPTLKQSISEAFGKPLSTTLNQDEAIAKGAAFICAIHSPTLRVRPFKFEDIHPYSVSYSWDKQVEDEDHMEVFPAGSSFPSTKLITLNRTGDFSMAASYTDITQLPPNTPEQIANWEITGVQLPEGQDSVPVKLKLRCDPSGLHTIEEAYTIEDIEVEEPIPLPEDAPEDAEQEFKKVTKTVKKDDLTIVAHTFGLDAKKLNELIEKENEMLAQDKLVAETEDRKNTLEEYIYTLRGKLEEEYAPFASDAEKTKLQGMLNKAEEWLYDEGFDSIKAKYIAKYEELASLGNIIRGRYLAKEEEKKQAIRSKQEASQMAAMAEKLAAQRKAEAEKKEEKKDTEGDVDMD</sequence>
+  </entry>
+  <entry>
+    <accession>P46997</accession>
+    <name>J protein JJJ2</name>
+    <protein>
+      <recommendedName>
+        <fullName>J protein JJJ2</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">JJJ2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="583">MSQVIEPQLDRTTYYSILGLTSNATSSEVHKSYLKLARLLHPDKTKSDKSEELFKAVVHAHSILTDEDQKLRYDRDLKIKGLHTYQPKKNCHIFKTKAKESQGASPTLGQSEAYHRQNKPYEQQPYGFGVGKKMTSSSKSKVPIFKSFNLKSYQRNHYYSSKKERKHGSPDIDSLFHETNGASKVRMTDAGKMDTNSQFQEIWEILGKNAYTHKSYSEDPNSCLGSALSDHEEEEEAGKQQQQQQQQQQQQQHYGMTSKSSSPDEEKKNNKEPKRESRVSPEENGEEETGHKQFKLPKTSTFSSGSHDSNLQSPFYNHEYRHYARSKFECKNQFRKSVSPIKEIPATTSANEGWNILRDIIEKLNISNVDDRNKDLLFRRDEIGDKNHSDSIDIENLSIKEPKGMKRRKKDDISLEELFQSLPREKDYFMMDAINDSLESINLFKKPKTTQSHEQGGTFAQAESNRAKFKPLLEQCGITPEILDLEIPEIPEFDAVADLETLKLNVQLFNNQCNKLKETIHQVSLQRLRADTQFSDMLTQKQSIMVWKTYLEFDKSLMDKLNILQERQMQVIKIFSERCDGKV</sequence>
+  </entry>
+  <entry>
+    <accession>Q12230</accession>
+    <name>Sphingolipid long chain base-responsive protein LSP1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Sphingolipid long chain base-responsive protein LSP1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">LSP1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="341">MHRTYSLRNQRAPTAAELQAPPPPPSSTKSKFFGKASIASSFRKNAAGNFGPELARKLSQLVKTEKGVLRAMEVVASERREAAKQLSLWGADNDDDVSDVTDKLGVLIYELGELQDQFIDKYDQYRVTLKSIRNIEASVQPSRDRKEKITDEIAHLKYKDPQSTKIPVLEQELVRAEAESLVAEAQLSNITREKLKAAYSYMFDSLRELSEKFALIAGYGKALLELLDDSPVTPGEARPAYDGYEASRQIIMDAESALESWTLDMAAVKPTLSFHQTVDDVYEDEDGEEEEEPEIQNGDIPGQVVEEEEVEWTTEVPVDDEAHEADHHVSQNGHTSGSENI</sequence>
+  </entry>
+  <entry>
+    <accession>Q12117</accession>
+    <name>Protein MRH1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Protein MRH1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">MRH1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="320">MSTFETLIKRGGNEAIKINPPTGADFHITSRGSDWFWTCFCCYLLFGLILTFLMFRKPVNDRFFYLTGIAPNFFMCIAYFTMASNLGWIPVKAKYNHVQTSTQKEHPGYRQIFYSRFVGWFLALPWPIIQICMLAGTPFWQMAFNVCITEFFTVCWLIAACVHSTYKWGYYTIGLGAAIVVSISVMTTSYNLVKQRDNDIRLTFLVFFSIIMFLWIIAYPTCFGITDGGNVLQPDSAGIFYGIIDLILMCFIPTLLVPIANHFGADKLGYHFGPSDAEAVMAPKAPVASPRPAATPNLSKDKKKKSKKSKKSKKSKKSEE</sequence>
+  </entry>
+  <entry>
+    <accession>Q06820</accession>
+    <name>Mitochondrial distribution and morphology protein 36</name>
+    <protein>
+      <recommendedName>
+        <fullName>Mitochondrial distribution and morphology protein 36</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">MDM36</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="579">MDENGTVKPGYELKGLNSGNSRSNMDKDPIVSKFHRAGLNDSADEEDTDINGNRNTSWITSMISEEKRKVEGKSMLNDEEDLHLSKATLNKCDALVKILADIIKLEFVIHQSWYIRSLHKSVLIQFEVETSGGNKNSAGDSGDDDDDNHNGNLDDSFYKDLSLKCIKKCEKSSLALESLSRDIDQIRDFIMSNTIEDNRVDRLLQNSMTLLLECWIYSMKRLRRLRMKIAGIFVRSKLLLIDHELVTIWHFLQEQNEHETVNNENELKLAETIKSYRAFIKIFIQQLEDSESGSPSSSLFEECLHVFLDIESMYNSLNLNWLLNENKALQERLLSPSSTSENDHTNNLPVIDETKEIEDISSFVNSIVDASMLTHDLTPINSSDSDNLSNGEIDRLDGRRLSSSTSDMSLMMQRTSLQKQLPSLLTAFNNARRLEQELQNACKVNDNKHSTKDTDSNIRRNEHAMSSSVSSIISQNSTLASPSPPMSSSFISTAPSQSSSRMSTLPLSPSSSLLESQSQTLKNNMSQWLNQSRSGLNGTKLIPTNHIGFHSNVLNTLYGIGGGPVSKSYKSNQPSSQNT</sequence>
+  </entry>
+  <entry>
+    <accession>O14467</accession>
+    <name>Multiprotein-bridging factor 1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Multiprotein-bridging factor 1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">MBF1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="151">MSDWDTNTIIGSRARAGGSGPRANVARSQGQINAARRQGLVVSVDKKYGSTNTRGDNEGQRLTKVDRETDIVKPKKLDPNVGRAISRARTDKKMSQKDLATKINEKPTVVNDYEAARAIPNQQVLSKLERALGVKLRGNNIGSPLGAPKKK</sequence>
+  </entry>
+  <entry>
+    <accession>P00560</accession>
+    <name>Phosphoglycerate kinase</name>
+    <protein>
+      <recommendedName>
+        <fullName>Phosphoglycerate kinase</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">PGK1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="416">MSLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTDKEGIPAGWQGLDNGPESRKLFAATVAKAKTIVWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKK</sequence>
+  </entry>
+  <entry>
+    <accession>Q05568</accession>
+    <name>Peroxisome biogenesis factor 10</name>
+    <protein>
+      <recommendedName>
+        <fullName>Peroxisome biogenesis factor 10</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">PEX10</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="337">MKNDNKLQKEALMRLSQLRFPFADAPSIVQAHQKDEQIQGLLIMKVTELCKLIKSQLFVNSYPKELSIFAKLLYLLFTTGRRGRTLGEEYVDLTYTNRKGTRLAGRLKMIVFAFAYPLCPYFITKLYKKIMKNNKESKIEDTESVAAFCKGLLDFILDVHMTLFYFKGAFYSISKRIFGMRYVFKHILSKNEANFREEGSQKYKVLGYILLAQNVMKWYPVLTSTLGSWIYGRKRTNDSITRSSVGLQERSEHESIEGIPKESQLTHINLSDKNQLPFIPEASRKCILCLMNMSDPSCAPCGHLFCWSCLMSWCKERPECPLCRQHCQPQEILVLRQ</sequence>
+  </entry>
+  <entry>
+    <accession>P00950</accession>
+    <name>Phosphoglycerate mutase 1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Phosphoglycerate mutase 1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">GPM1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="247">MPKLVLVRHGQSEWNEKNLFTGWVDVKLSAKGQQEAARAGELLKEKKVYPDVLYTSKLSRAIQTANIALEKADRLWIPVNRSWRLNERHYGDLQGKDKAETLKKFGEEKFNTYRRSFDVPPPPIDASSPFSQKGDERYKYVDPNVLPETESLALVIDRLLPYWQDVIAKDLLSGKTVMIAAHGNSLRGLVKHLEGISDADIAKLNIPTGIPLVFELDENLKPSKPSYYLDPEAAAAGAAAVANQGKK</sequence>
+  </entry>
+  <entry>
+    <accession>O13516</accession>
+    <name>40S ribosomal protein S9-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>40S ribosomal protein S9-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPS9A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="197">MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKKEIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAADEADEADEE</sequence>
+  </entry>
+  <entry>
+    <accession>P02407</accession>
+    <name>40S ribosomal protein S17-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>40S ribosomal protein S17-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPS17A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="136">MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKRIQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLSVINVSAQRDRRYRKRV</sequence>
+  </entry>
+  <entry>
+    <accession>P05756</accession>
+    <name>40S ribosomal protein S13</name>
+    <protein>
+      <recommendedName>
+        <fullName>40S ribosomal protein S13</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPS13</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="151">MGRMHSAGKGISSSAIPYSRNAPAWFKLSSESVIEQIVKYARKGLTPSQIGVLLRDAHGVTQARVITGNKIMRILKSNGLAPEIPEDLYYLIKKAVSVRKHLERNRKDKDAKFRLILIESRIHRLARYYRTVAVLPPNWKYESATASALVN</sequence>
+  </entry>
+  <entry>
+    <accession>P46784</accession>
+    <name>40S ribosomal protein S10-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>40S ribosomal protein S10-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPS10B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Methylation on R">
+      <location>
+        <position position="100" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Methylation on R">
+      <location>
+        <position position="103" />
+      </location>
+    </feature>
+    <sequence length="105">MLMPKQERNKIHQYLFQEGVVVAKKDFNQAKHEEIDTKNLYVIKALQSLTSKGYVKTQFSWQYYYYTLTEEGVEYLREYLNLPEHIVPGTYIQERNPSQRPQRRY</sequence>
+  </entry>
+  <entry>
+    <accession>Q05911</accession>
+    <name>Adenylosuccinate lyase</name>
+    <protein>
+      <recommendedName>
+        <fullName>Adenylosuccinate lyase</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">ADE13</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="482">MPDYDNYTTPLSSRYASKEMSATFSLRNRFSTWRKLWLNLAIAEKELGLTVVTDEAIEQMRKHVEITDDEIAKASAQEAIVRHDVMAHVHTFGETCPAAAGIIHLGATSCFVTDNADLIFIRDAYDIIIPKLVNVINRLAKFAMEYKDLPVLGWTHFQPAQLTTLGKRATLWIQELLWDLRNFERARNDIGLRGVKGTTGTQASFLALFHGNHDKVEALDERVTELLGFDKVYPVTGQTYSRKIDIDVLAPLSSFAATAHKMATDIRLLANLKEVEEPFEKSQIGSSAMAYKRNPMRCERVCSLARHLGSLFSDAVQTASVQWFERTLDDSAIRRISLPSAFLTADILLSTLLNISSGLVVYPKVIERRIKGELPFMATENIIMAMVEKNASRQEVHERIRVLSHQAAAVVKEEGGENDLIERVKRDEFFKPIWEELDSLLEPSTFVGRAPQQVEKFVQKDVNNALQPFQKYLNDEQVKLNV</sequence>
+  </entry>
+  <entry>
+    <accession>P28272</accession>
+    <name>Dihydroorotate dehydrogenase (fumarate)</name>
+    <protein>
+      <recommendedName>
+        <fullName>Dihydroorotate dehydrogenase (fumarate)</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">URA1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="314">MTASLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLSYVLNRQKNYPDAPAIFFSVAGMSIDENLNLLRKIQDSEFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKKPLGVKLPPYFDFAHFDIMAKILNEFPLAYVNSINSIGNGLFIDVEKESVVVKPKNGFGGIGGEYVKPTALANVRAFYTRLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTSIDQFRGKLNSI</sequence>
+  </entry>
+  <entry>
+    <accession>Q00816</accession>
+    <name>Resistance to glucose repression protein 1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Resistance to glucose repression protein 1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">REG1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1014">MSTNLANYFAGKKDIENEHVNRNASHESNSKSDVKISGNDNDNDEDMGPSVSMAVQAKNDDDFHKSTFNLKRTRSMGLLDEYIDPTKKLLGRSDDLYDNDNEYYDNSSNNSSSNSSDDDYDDGYQEHSTSVSPPPADNDSYLIPQDDNDVVVEPERHVDYLSHEWKESEISNSWKYIILKKKKRDVDLVNAARLENASWRTWAKARNNLKTVSPEVVNWSKDSDVTWLYGPIVRDSEGNAQSEEEHDLERGYGSDDENSKRISMPTKNSKSIAAAPKPILKKRTVTEIIEDNALWKLNEARKHMTEMKHASVIMDPNGNKNVHDDFDALAAQVNAQYYHYPKESNSSVSLKSQHSDKKDNSTIPNPVGENSNGGGDKGEEDLHLKSALHVQNNRSTAQSNKSILENSTNDRKANLDQNLNSPDNNRFPSSTSSSNRDNENNSMGLSSILTSNPSEKSNKPTKNRHIHFNDRVEQCMALRYPASQSEDDESDDENKQYVDVNNNANVTTINNNRTPLLAIQHKSIPINSATEHLNKNTSDDDTSSQSSSSSHSDDEEHGGLYINARFSRRSDSGVHSPITDNSSVASSTTSRAHVRPIIKLLPDTTLNYGSDEESDNGEFNGYGNAVSHNVNTSRGYDYIYDYNSVYTGDTSSFLPVDSCDIVDVPEGMDLQTAIADDNASNYEFNNAVESKEKHVPQLHKASANNTTRQHGSHMLLYDDDNYSSSSDSEQQFIEDSQYNSSDDEEEEDDDDQEVDDNHDEGLSLRRTLSLGKSGSTNSLYDLAQPSLSSATPQQKNPTNFTGGKTDVDKDAQLAVRPYPLKRNSSSGNFIFNSDSEEESSSEEEQRPLPANSQLVNRSVLKGSVTPANISSQKKKALPKQPKASDSSQSFRIVNNTPSPAEVGASDVAIEGYFSPRNESIKSVVSGGNMMDHQDHSEMDTLAKGFENCHINNASKLKDKKVDSVQTTRKEASLTDSSNESLHKVVQNARGMASKYLHSWKKSDVKPQENGNDSS</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX50</accession>
+    <name>60S ribosomal protein L18-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L18-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL18B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="186">MGIDHTSKQHKRSGHRTAPKSDNVYLKLLVKLYTFLARRTDAPFNKVVLKALFLSKINRPPVSVSRIARALKQEGAANKTVVVVGTVTDDARIFEFPKTTVAALRFTAGARAKIVKAGGECITLDQLAVRAPKGQNTLILRGPRNSREAVRHFGMGPHKGKAPRILSTGRKFERARGRRRSKGFKV</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX82</accession>
+    <name>60S ribosomal protein L19-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L19-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL19A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="189">MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA</sequence>
+  </entry>
+  <entry>
+    <accession>P40212</accession>
+    <name>60S ribosomal protein L13-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L13-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL13B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Succinylation on K">
+      <location>
+        <position position="16" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Succinylation on K">
+      <location>
+        <position position="23" />
+      </location>
+    </feature>
+    <sequence length="199">MAISKNLPILKNHFRKHWQERVKVHFDQAGKKVSRRNARAARAAKIAPRPLDLLRPVVRAPTVKYNRKVRAGRGFTLAEVKAAGLTAAYARTIGIAVDHRRQNRNQEIFDANVQRLKEYQSKIIVFPRDGKAPEAEQVLSAAATFPIAQPATDVEARAVQDNGESAFRTLRLARSEKKFRGIREKRAREKAEAEAEKKK</sequence>
+  </entry>
+  <entry>
+    <accession>Q12690</accession>
+    <name>60S ribosomal protein L13-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L13-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL13A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Succinylation on K">
+      <location>
+        <position position="16" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Succinylation on K">
+      <location>
+        <position position="23" />
+      </location>
+    </feature>
+    <sequence length="199">MAISKNLPILKNHFRKHWQERVKVHFDQAGKKVSRRNARATRAAKIAPRPLDLLRPVVRAPTVKYNRKVRAGRGFTLAEVKAAGLTAAYARTIGIAVDHRRQNRNQEIFDANVQRLKEYQSKIIVFPRNGKAPEAEQVLSAAATFPIAQPATDVEARAVQDNGESAFRTLRLARSEKKFRGIREKRAREKAEAEAEKKK</sequence>
+  </entry>
+  <entry>
+    <accession>P26784</accession>
+    <name>60S ribosomal protein L16-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L16-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL16A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="199">MSVEPVVVIDGKGHLVGRLASVVAKQLLNGQKIVVVRAEELNISGEFFRNKLKYHDFLRKATAFNKTRGPFHFRAPSRIFYKALRGMVSHKTARGKAALERLKVFEGIPPPYDKKKRVVVPQALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEAKRKVSSAEYYAKKRAFTKKVASANATAAESDVAKQLAALGY</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX83</accession>
+    <name>60S ribosomal protein L19-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L19-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL19B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="189">MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA</sequence>
+  </entry>
+  <entry>
+    <accession>Q02753</accession>
+    <name>60S ribosomal protein L21-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L21-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL21A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="160">MGKSHGYRSRTRYMFQRDFRKHGAVHLSTYLKVYKVGDIVDIKANGSIQKGMPHKFYQGKTGVVYNVTKSSVGVIINKMVGNRYLEKRLNLRVEHIKHSKCRQEFLERVKANAAKRAEAKAQGVAVQLKRQPAQPRESRIVSTEGNVPQTLAPVPYETFI</sequence>
+  </entry>
+  <entry>
+    <accession>P26785</accession>
+    <name>60S ribosomal protein L16-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L16-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL16B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="198">MSQPVVVIDAKDHLLGRLASTIAKQVLNGQKIVVVRAEALNISGEFFRNKLKYHDFLRKATAFNKTRGPFHFRAPSRILYKAIRGMVSHKTARGKAALERLKIFEGIPPPYDKKKRVVVPQALRVLRLKPGRKYTTLGKLSTSVGWKYEDVVAKLEDKRKVRSAEYYAKKRAFTKKVSSASAAASESDVAKQLASFGY</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX49</accession>
+    <name>60S ribosomal protein L18-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L18-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL18A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="186">MGIDHTSKQHKRSGHRTAPKSDNVYLKLLVKLYTFLARRTDAPFNKVVLKALFLSKINRPPVSVSRIARALKQEGAANKTVVVVGTVTDDARIFEFPKTTVAALRFTAGARAKIVKAGGECITLDQLAVRAPKGQNTLILRGPRNSREAVRHFGMGPHKGKAPRILSTGRKFERARGRRRSKGFKV</sequence>
+  </entry>
+  <entry>
+    <accession>Q08961</accession>
+    <name>Ribosomal lysine N-methyltransferase 1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Ribosomal lysine N-methyltransferase 1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RKM1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="583">MSSDALKALLQWGASFGVIVPEELKFLYTDLKGIICVCEKDIDNPSIKIPPEIVISRNLPMKFFGLSESTKNINGWLKLFFAKIKFDRDNDTIVDNVRVNDKFKPYLDALPSRLNSPLVWNPSELKRLSSTNIGNSIHEKFEGIFKEWFELVSSSDMFDLERVADDVQTFHNLDELTYEALYEKILKITELQRPTIWYSFPAFLWSHLIFISRAFPEYVLNRNCPDNSIVLLPIVDLLNHDYRSKVKWYPENGWFCYEKIGTASQSRELSNNYGGKGNEELLSGYGFVLEDNIFDSVALKVKLPLDVVSTILETEPSLKLPLLSDYTTYAFENKDCVQQEKKATRSATDYINGVTYFINIQNEQCLEPLLDLFTYLSKAEEEDLHDLRARLQGIQMLRNALQSKLNSITGPPATDDSYAIDPYRVYCADVYTKGQKQILKEALTRLKKLEKTMLSENKHQLLTMSKILKNDPAFAETELPSLFSNEDGEEVIFESTYDLLILWILLKTKKNSYPTKYEWVGQQYTNFKQTAYISDDAKAFHTAYFEKQDDVDLAEVDHAIQFVVDNSFTRTSSTTEETILVRK</sequence>
+  </entry>
+  <entry>
+    <accession>P26321</accession>
+    <name>60S ribosomal protein L5</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L5</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL5</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="297">MAFQKDAKSSAYSSRFQTPFRRRREGKTDYYQRKRLVTQHKAKYNTPKYRLVVRFTNKDIICQIISSTITGDVVLAAAYSHELPRYGITHGLTNWAAAYATGLLIARRTLQKLGLDETYKGVEEVEGEYELTEAVEDGPRPFKVFLDIGLQRTTTGARVFGALKGASDGGLYVPHSENRFPGWDFETEEIDPELLRSYIFGGHVSQYMEELADDDEERFSELFKGYLADDIDADSLEDIYTSAHEAIRADPAFKPTEKKFTKEQYAAESKKYRQTKLSKEERAARVAAKIAALAGQQ</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX24</accession>
+    <name>60S ribosomal protein L20-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L20-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL20B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="172">MAHFKEYQVIGRRLPTESVPEPKLFRMRIFASNEVIAKSRYWYFLQKLHKVKKASGEIVSINQINEAHPTKVKNFGVWVRYDSRSGTHNMYKEIRDVSRVAAVETLYQDMAARHRARFRSIHILKVAEIEKTADVKRQYVKQFLTKDLKFPLPHRVQKSTKTFSYKRPSTFY</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX46</accession>
+    <name>60S ribosomal protein L2-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L2-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL2B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="28" />
+      </location>
+    </feature>
+    <sequence length="254">MGRVIRNQRKGAGSIFTSHTRLRQGAAKLRTLDYAERHGYIRGIVKQIVHDSGRGAPLAKVVFRDPYKYRLREEIFIANEGVHTGQFIYAGKKASLNVGNVLPLGSVPEGTIVSNVEEKPGDRGALARASGNYVIIIGHNPDENKTRVRLPSGAKKVISSDARGVIGVIAGGGRVDKPLLKAGRAFHKYRLKRNSWPKTRGVAMNPVDHPHGGGNHQHIGKASTISRGAVSGQKAGLIAARRTGLLRGSQKTQD</sequence>
+  </entry>
+  <entry>
+    <accession>Q12672</accession>
+    <name>60S ribosomal protein L21-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L21-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL21B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="160">MGKSHGYRSRTRYMFQRDFRKHGAVHMSTYLKIYKVGDIVDIKANGSIQKGMPHKFYQGKTGVVYNVTKSSVGVIINKMVGNRYLEKRLNLRVEHIKHSKCRQEFLERVKANAAKRAEAKAQGVAVQLKRQPAQPRESRIVSTEGNVPQTLAPVPYETFI</sequence>
+  </entry>
+  <entry>
+    <accession>P41056</accession>
+    <name>60S ribosomal protein L33-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L33-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL33B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="107">MAESHRLYVKGKHLSYQRSKRVNNPNVSLIKIEGVATPQEAQFYLGKRIAYVYRASKEVRGSKIRVMWGKVTRTHGNSGVVRATFRNNLPAKTFGASVRIFLYPSNI</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX23</accession>
+    <name>60S ribosomal protein L20-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L20-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL20A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="172">MAHFKEYQVIGRRLPTESVPEPKLFRMRIFASNEVIAKSRYWYFLQKLHKVKKASGEIVSINQINEAHPTKVKNFGVWVRYDSRSGTHNMYKEIRDVSRVAAVETLYQDMAARHRARFRSIHILKVAEIEKTADVKRQYVKQFLTKDLKFPLPHRVQKSTKTFSYKRPSTFY</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX45</accession>
+    <name>60S ribosomal protein L2-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L2-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL2A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="28" />
+      </location>
+    </feature>
+    <sequence length="254">MGRVIRNQRKGAGSIFTSHTRLRQGAAKLRTLDYAERHGYIRGIVKQIVHDSGRGAPLAKVVFRDPYKYRLREEIFIANEGVHTGQFIYAGKKASLNVGNVLPLGSVPEGTIVSNVEEKPGDRGALARASGNYVIIIGHNPDENKTRVRLPSGAKKVISSDARGVIGVIAGGGRVDKPLLKAGRAFHKYRLKRNSWPKTRGVAMNPVDHPHGGGNHQHIGKASTISRGAVSGQKAGLIAARRTGLLRGSQKTQD</sequence>
+  </entry>
+  <entry>
+    <accession>P05744</accession>
+    <name>60S ribosomal protein L33-A</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L33-A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL33A</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="107">MAESHRLYVKGKHLSYQRSKRVNNPNVSLIKIEGVATPQDAQFYLGKRIAYVYRASKEVRGSKIRVMWGKVTRTHGNSGVVRATFRNNLPAKTFGASVRIFLYPSNI</sequence>
+  </entry>
+  <entry>
+    <accession>P05739</accession>
+    <name>60S ribosomal protein L6-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>60S ribosomal protein L6-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPL6B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="176">MTAQQAPKWYPSEDVAAPKKTRKAVRPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLEDNTLLVTGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEANLFPEQQTKEIKTERVEDQKVVDKALLAEIKKTPLLKQYLSASFSLKNGDKPHLLKF</sequence>
+  </entry>
+  <entry>
+    <accession>P48589</accession>
+    <name>40S ribosomal protein S12</name>
+    <protein>
+      <recommendedName>
+        <fullName>40S ribosomal protein S12</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPS12</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="143">MSDVEEVVEVQEETVVEQTAEVTIEDALKVVLRTALVHDGLARGLRESTKALTRGEALLVVLVSSVTEANIIKLVEGLANDPENKVPLIKVADAKQLGEWAGLGKIDREGNARKVVGASVVVVKNWGAETDELSMIMEHFSQQ</sequence>
+  </entry>
+  <entry>
+    <accession>P14127</accession>
+    <name>40S ribosomal protein S17-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>40S ribosomal protein S17-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPS17B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="136">MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKRIQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLSVINVSAQRDRRYRKRN</sequence>
+  </entry>
+  <entry>
+    <accession>P05755</accession>
+    <name>40S ribosomal protein S9-B</name>
+    <protein>
+      <recommendedName>
+        <fullName>40S ribosomal protein S9-B</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">RPS9B</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="195">MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKREIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAAEEAEDEE</sequence>
+  </entry>
+  <entry>
+    <accession>P40075</accession>
+    <name>Vesicle-associated membrane protein-associated protein SCS2</name>
+    <protein>
+      <recommendedName>
+        <fullName>Vesicle-associated membrane protein-associated protein SCS2</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">SCS2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="244">MSAVEISPDVLVYKSPLTEQSTEYASISNNSDQTIAFKVKTTAPKFYCVRPNAAVVAPGETIQVQVIFLGLTEEPAADFKCRDKFLVITLPSPYDLNGKAVADVWSDLEAEFKQQAISKKIKVKYLISPDVHPAQNQNIQENKETVEPVVQDSEPKEVPAVVNEKEVPAEPETQPPVQVKKEEVPPVVQKTVPHENEKQTSNSTPAPQNQIKEAATVPAENESSSMGIFILVALLILVLGWFYR</sequence>
+  </entry>
+  <entry>
+    <accession>Q12118</accession>
+    <name>Small glutamine-rich tetratricopeptide repeat-containing protein 2</name>
+    <protein>
+      <recommendedName>
+        <fullName>Small glutamine-rich tetratricopeptide repeat-containing protein 2</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">SGT2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="346">MSASKEEIAALIVNYFSSIVEKKEISEDGADSLNVAMDCISEAFGFEREAVSGILGKSEFKGQHLADILNSASRVPESNKKDDAENVEINIPEDDAETKAKAEDLKMQGNKAMANKDYELAINKYTEAIKVLPTNAIYYANRAAAHSSLKEYDQAVKDAESAISIDPSYFRGYSRLGFAKYAQGKPEEALEAYKKVLDIEGDNATEAMKRDYESAKKKVEQSLNLEKTVPEQSRDADVDASQGASAGGLPDLGSLLGGGLGGLMNNPQLMQAAQKMMSNPGAMQNIQKMMQDPSIRQMAEGFASGGGTPNLSDLMNNPALRNMAGNLFGGAGAQSTDETPDNENKQ</sequence>
+  </entry>
+  <entry>
+    <accession>P25582</accession>
+    <name>27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase</name>
+    <protein>
+      <recommendedName>
+        <fullName>27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">SPB1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Hydroxylation on N">
+      <location>
+        <position position="420" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="424" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="426" />
+      </location>
+    </feature>
+    <sequence length="841">MGKTQKKNSKGRLDRYYYLAKEKGYRARSSFKIIQINEKYGHFLEKSKVVIDLCAAPGSWCQVASKLCPVNSLIIGVDIVPMKPMPNVITFQSDITTEDCRSKLRGYMKTWKADTVLHDGAPNVGLGWVQDAFTQSQLTLQALKLAVENLVVNGTFVTKIFRSKDYNKLIWVFQQLFEKVEATKPPASRNVSAEIFVVCKGFKAPKRLDPRLLDPKEVFEELPDGQQNMESKIYNPEKKVRKRQGYEEGDNLLYHETSILDFVRTEDPISMLGEMNKFTIDENDHEWKILKKLKQTTDEFRSCIEDLKVLGKKDFKMILRWRKIAREILGIEVKDDAKTEIEVVPLTEEEQIEKDLQGLQEKQRLNVKRERRRKNEMKQKELQRMQMNMITPTDIGIEAASLGKESLFNLKTAEKTGILNDLAKGKKRMIFTDDELAKDNDIYIDENIMIKDKDSAADADDLESELNAMYSDYKTRRSERDAKFRAKQARGGDNEEEWTGFNEGSLEKKEEEGKDYIEDNDDEGVEGDSDDDEAITNLISKLKGQEGDHKLSSKARMIFNDPIFNNVEPDLPVNTVNDGIMSSESVGDISKLNKKRKHEEMHQKQDEADSSDESSSDDSDFEIVANDNASEEFDSDYDSEEEKNQTKKEKHSRDIDIATVEAMTLAHQLALGQKNKHDLVDEGFNRYTFRDTENLPDWFLEDEKEHSKINKPITKEAAMAIKEKIKAMNARPIKKVAEAKARKRMRAVARLEKIKKKAGLINDDSDKTEKDKAEEISRLMRKVTKKPKTKPKVTLVVASGRNKGLAGRPKGVKGKYKMVDGVMKNEQRALRRIAKKHHKKK</sequence>
+  </entry>
+  <entry>
+    <accession>P32558</accession>
+    <name>FACT complex subunit SPT16</name>
+    <protein>
+      <recommendedName>
+        <fullName>FACT complex subunit SPT16</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">SPT16</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1035">MEELNIDFDVFKKRIELLYSKYNEFEGSPNSLLFVLGSSNAENPYQKTTILHNWLLSYEFPATLIALVPGKVIIITSSAKAKHLQKAIDLFKDPESKITLELWQRNNKEPELNKKLFDDVIALINSAGKTVGIPEKDSYQGKFMTEWNPVWEAAVKENEFNVIDISLGLSKVWEVKDVNEQAFLSVSSKGSDKFMDLLSNEMVRAVDEELKITNAKLSDKIENKIDDVKFLKQLSPDLSALCPPNYKFNFDLLDWTYSPIIQSGKKFDLRVSARSTNDQLYGNGCILASCGIRYNNYCSNITRTFLIDPSEEMANNYDFLLTLQKEIVTNILKPGRTPKEVYESVIEYIEKTKPELVPNFTKNIGSLIGLEFRDSNFILNVKNDYRKIQRGDCFNISFGFNNLKDSQSANNYALQLADTVQIPLDETEPPRFLTNYTKAKSQISFYFNNEEEDNNKKKSSPATKVPSKPDRNSKILRTKLRGEARGGAEDAQKEQIRKENQKKLHEKLEKNGLLRFSAADANGPDSEPRQYFKKYESYVRDSQLPTNIRDLRIHVDWKSQTIILPIYGRPVPFHINSYKNGSKNEEGEYTYLRLNFNSPGSSGGISKKVEELPYEESADNQFVRSITLRSKDGDRMSETFKQIADLKKEATKREQERKALADVVQQDKLIENKTGRTKRLDQIFVRPNPDTKRVPSTVFIHENGIRFQSPLRTDSRIDILFSNIKNLIFQSCKGELIVVIHIHLKNPILMGKKKIQDVQFYREASDMSVDETGGGRRGQSRFRRYGDEDELEQEQEERRKRAALDKEFKYFADAIAEASNGLLTVENTFRDLGFQGVPNRSAVFCMPTTDCLVQLIEPPFLVINLEEVEICILERVQFGLKNFDMVFVYKDFNKPVTHINTVPIESLDFLKQWLTDMDIPYTVSTINLNWATIMKSLQDDPYQFFLDGGWNFLATGSDDEASDESEEEVSEYEASEDDVSDESAFSEDEEGSEVDDDISGDESEDYTGDESEEGEDWDELEKKAARADRGANFRD</sequence>
+  </entry>
+  <entry>
+    <accession>P39015</accession>
+    <name>Suppressor protein STM1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Suppressor protein STM1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">STM1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Deamidation on N">
+      <location>
+        <position position="246" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Deamidation on N">
+      <location>
+        <position position="247" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Deamidation on N">
+      <location>
+        <position position="250" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Deamidation on N">
+      <location>
+        <position position="253" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Deamidation on N">
+      <location>
+        <position position="256" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Deamidation on Q">
+      <location>
+        <position position="259" />
+      </location>
+    </feature>
+    <sequence length="273">MSNPFDLLGNDVEDADVVVLPPKEIVKSNTSSKKADVPPPSADPSKARKNRPRPSGNEGAIRDKTAGRRNNRSKDVTDSATTKKSNTRRATDRHSRTGKTDTKKKVNQGWGDDKKELSAEKEAQADAAAEIAEDAAEAEDAGKPKTAQLSLQDYLNQQANNQFNKVPEAKKVELDAERIETAEKEAYVPATKVKNVKSKQLKTKEYLEFDATFVESNTRKNFGDRNNNSRNNFNNRRGGRGARKGNNTANATNSANTVQKNRNIDVSNLPSLA</sequence>
+  </entry>
+  <entry>
+    <accession>P53312</accession>
+    <name>Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial</name>
+    <protein>
+      <recommendedName>
+        <fullName>Succinate--CoA ligase [ADP-forming] subunit beta, mitochondrial</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">LSC2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="427">MYSRKSLSLISKCGQLSRLNAQAALQARRHLSIHEYRSAQLLREYGIGTPEGFPAFTPEEAFEAAKKLNTNKLVIKAQALTGGRGKGHFDTGYKSGVHMIESPQQAEDVAKEMLNHNLITKQTGIAGKPVSAVYIVKRVDTKHEAYLSILMDRQTKKPMIIASSQGGMNIEEVAERTPDAIKKFSIETSKGLSPQMAKDVAKSLGFSPDAQDEAAKAVSNLYKIFMERDATQVEINPLSEIEHDPTHKIMCTDAKFGFDDNASFRQEKIYSWRDLSQEDPDEVKAKKYDLNFVKLKGNIGCLVNGAGLAMATMDVIKLNGGDPANFLDCGGGATPETIKQGFELILSNKNVDAIFVNIFGGIVRCDYVALGLVEAARELEVRVPIVARLQGTKVEEGRDIINKSGVKIYSFDELDPAAKKVVELTQN</sequence>
+  </entry>
+  <entry>
+    <accession>P15705</accession>
+    <name>Heat shock protein STI1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Heat shock protein STI1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">STI1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="354" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="361" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Deamidation on N">
+      <location>
+        <position position="377" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on N">
+      <location>
+        <position position="377" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="380" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Hydroxylation on K">
+      <location>
+        <position position="383" />
+      </location>
+    </feature>
+    <sequence length="589">MSLTADEYKQQGNAAFTAKDYDKAIELFTKAIEVSETPNHVLYSNRSACYTSLKKFSDALNDANECVKINPSWSKGYNRLGAAHLGLGDLDEAESNYKKALELDASNKAAKEGLDQVHRTQQARQAQPDLGLTQLFADPNLIENLKKNPKTSEMMKDPQLVAKLIGYKQNPQAIGQDLFTDPRLMTIMATLMGVDLNMDDINQSNSMPKEPETSKSTEQKKDAEPQSDSTTSKENSSKAPQKEESKESEPMEVDEDDSKIEADKEKAEGNKFYKARQFDEAIEHYNKAWELHKDITYLNNRAAAEYEKGEYETAISTLNDAVEQGREMRADYKVISKSFARIGNAYHKLGDLKKTIEYYQKSLTEHRTADILTKLRNAEKELKKAEAEAYVNPEKAEEARLEGKEYFTKSDWPNAVKAYTEMIKRAPEDARGYSNRAAALAKLMSFPEAIADCNKAIEKDPNFVRAYIRKATAQIAVKEYASALETLDAARTKDAEVNNGSSAREIDQLYYKASQQRFQPGTSNETPEETYQRAMKDPEVAAIMQDPVMQSILQQAQQNPAALQEHMKNPEVFKKIQTLIAAGIIRTGR</sequence>
+  </entry>
+  <entry>
+    <accession>P38825</accession>
+    <name>Protein TOM71</name>
+    <protein>
+      <recommendedName>
+        <fullName>Protein TOM71</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TOM71</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <feature type="modified residue" description="Deamidation on N">
+      <location>
+        <position position="4" />
+      </location>
+    </feature>
+    <feature type="modified residue" description="Citrullination on R">
+      <location>
+        <position position="8" />
+      </location>
+    </feature>
+    <sequence length="639">MAENSLLRFITKNKVAILATVSAGTAAVGAYVYYQQIKQQQQQQLKGTKDNRRQSEAFAGQNEDEADLKDDGSVVSGSNKRKKKKNKRKRNNKAKSGEGFDYPSLPNGEPDIAQLKGLSPSQRQAYAVQLKNRGNHFFTAKNFNEAIKYYQYAIELDPNEPVFYSNISACYISTGDLEKVIEFTTKALEIKPDHSKALLRRASANESLGNFTDAMFDLSVLSLNGDFDGASIEPMLERNLNKQAMKVLNENLSKDEGRGSQVLPSNTSLASFFGIFDSHLEVSSVNTSSNYDTAYALLSDALQRLYSATDEGYLVANDLLTKSTDMYHSLLSANTVDDPLRENAALALCYTGIFHFLKNNLLDAQVLLQESINLHPTPNSYIFLALTLADKENSQEFFKFFQKAVDLNPEYPPTYYHRGQMYFILQDYKNAKEDFQKAQSLNPENVYPYIQLACLLYKQGKFTESEAFFNETKLKFPTLPEVPTFFAEILTDRGDFDTAIKQYDIAKRLEEVQEKIHVGIGPLIGKATILARQSSQDPTQLDEEKFNAAIKLLTKACELDPRSEQAKIGLAQLKLQMEKIDEAIELFEDSAILARTMDEKLQATTFAEAAKIQKRLRADPIISAKMELTLARYRAKGML</sequence>
+  </entry>
+  <entry>
+    <accession>P38349</accession>
+    <name>UBX domain-containing protein 7</name>
+    <protein>
+      <recommendedName>
+        <fullName>UBX domain-containing protein 7</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">UBX7</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="436">MLEALFRDSVEEAINDSIKEGVVLAVYNTARDDQWLKSWFKGDDVSLDTLAEHSIWLRLVKDTEQFQLFEQVFPNVVVPSIYLIRAGKIELIIQGEDDRHWEKLLACIGIKDKKAGESSSRETNPGLAREEKSSRDVHRKNARERIAETTLEIQRREQLKQRKLAEEERERIIRLVRADRAERKALDETHHRTLDDDKPLDVHDYIKDAQKLHSSKCVLQIRMTDGKTLKHEFNSSETLNDVRKWVDVNRTDGDCPYSFHRGIPRVTFKDSDELKTLETLELTPRSALLLKPLETQNSGLSVTGMEGPSLLGRLYKGFSTWWHNDKDPEVTSQREETSKPNRHEVRSSTPLSGAASSSCFQYNNVREPVQSSAHASPMLTPSGTRYPSETNLTTSRSVSPNVFQFVNNDHQEDPEDPTTFNGNNVHLEKKKDEDKK</sequence>
+  </entry>
+  <entry>
+    <accession>P17255</accession>
+    <name>V-type proton ATPase catalytic subunit A</name>
+    <protein>
+      <recommendedName>
+        <fullName>V-type proton ATPase catalytic subunit A</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">VMA1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1071">MAGAIENARKEIKRISLEDHAESEYGAIYSVSGPVVIAENMIGCAMYELVKVGHDNLVGEVIRIDGDKATIQVYEETAGLTVGDPVLRTGKPLSVELGPGLMETIYDGIQRPLKAIKEESQSIYIPRGIDTPALDRTIKWQFTPGKFQVGDHISGGDIYGSVFENSLISSHKILLPPRSRGTITWIAPAGEYTLDEKILEVEFDGKKSDFTLYHTWPVRVPRPVTEKLSADYPLLTGQRVLDALFPCVQGGTTCIPGAFGCGKTVISQSLSKYSNSDAIIYVGCFAKGTNVLMADGSIECIENIEVGNKVMGKDGRPREVIKLPRGRETMYSVVQKSQHRAHKSDSSREVPELLKFTCNATHELVVRTPRSVRRLSRTIKGVEYFEVITFEMGQKKAPDGRIVELVKEVSKSYPISEGPERANELVESYRKASNKAYFEWTIEARDLSLLGSHVRKATYQTYAPILYENDHFFDYMQKSKFHLTIEGPKVLAYLLGLWIGDGLSDRATFSVDSRDTSLMERVTEYAEKLNLCAEYKDRKEPQVAKTVNLYSKVVRGNGIRNNLNTENPLWDAIVGLGFLKDGVKNIPSFLSTDNIGTRETFLAGLIDSDGYVTDEHGIKATIKTIHTSVRDGLVSLARSLGLVVSVNAEPAKVDMNGTKHKISYAIYMSGGDVLLNVLSKCAGSKKFRPAPAAAFARECRGFYFELQELKEDDYYGITLSDDSDHQFLLANQVVVHNCGERGNEMAEVLMEFPELYTEMSGTKEPIMKRTTLVANTSNMPVAAREASIYTGITLAEYFRDQGKNVSMIADSSSRWAEALREISGRLGEMPADQGFPAYLGAKLASFYERAGKAVALGSPDRTGSVSIVAAVSPAGGDFSDPVTTATLGITQVFWGLDKKLAQRKHFPSINTSVSYSKYTNVLNKFYDSNYPEFPVLRDRMKEILSNAEELEQVVQLVGKSALSDSDKITLDVATLIKEDFLQQNGYSTYDAFCPIWKTFDMMRAFISYHDEAQKAVANGANWSKLADSTGDVKHAVSSSKFFEPSRGEKEVHGEFEKLLSTMQERFAESTD</sequence>
+  </entry>
+  <entry>
+    <accession>Q12141</accession>
+    <name>Transposon Ty1-GR1 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-GR1 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-GR1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIDKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX74</accession>
+    <name>Transposon Ty1-JR1 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-JR1 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-JR1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX70</accession>
+    <name>Transposon Ty1-DR6 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-DR6 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-DR6</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX71</accession>
+    <name>Transposon Ty1-ER1 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-ER1 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-ER1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>Q12085</accession>
+    <name>Transposon Ty1-GR1 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-GR1 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-GR1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>P0CF21</accession>
+    <name>Putative truncated L-serine dehydratase YIL168W</name>
+    <protein>
+      <recommendedName>
+        <fullName>Putative truncated L-serine dehydratase YIL168W</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">YIL168W</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="127">MEMTYYEKTPLIRQFLNNGKTNSWFYVKHEMLQPGGSFKSRGIGHLIRKSNEEALSEGSGKLAVFSSSGGNAGLAAATACRSMALNCSVVVPKTTKPRMVKKIQSAGAKVIIHGDHWGEADEYLRHE</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX72</accession>
+    <name>Transposon Ty1-LR2 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-LR2 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-LR2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>P0C2I6</accession>
+    <name>Transposon Ty1-LR3 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-LR3 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-LR3</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSASQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKPISEINLRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSNNETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDPPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAAKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P0C2I8</accession>
+    <name>Transposon Ty1-LR4 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-LR4 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-LR4</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHPHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>P36072</accession>
+    <name>Putative uncharacterized protein YKL118W</name>
+    <protein>
+      <recommendedName>
+        <fullName>Putative uncharacterized protein YKL118W</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">YKL118W</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="103">MSSSIPSFDFALFLNFRRNSVILSFSLISNIRVLLCDANRQLSYLTFSSFLSAFSCEICFIFASSFLILNIHTSVMSTLSQLNTQDFCKTEYFVNNIIVRIQS</sequence>
+  </entry>
+  <entry>
+    <accession>P0C2I5</accession>
+    <name>Transposon Ty1-LR2 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-LR2 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-LR2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAPTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX73</accession>
+    <name>Transposon Ty1-PL Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-PL Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-PL</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>Q12273</accession>
+    <name>Transposon Ty1-OL Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-OL Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-OL</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>Q03612</accession>
+    <name>Transposon Ty1-ER1 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-ER1 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-ER1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P0C2J1</accession>
+    <name>Transposon Ty1-PR3 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-PR3 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-PR3</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSASQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKPISEINLRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSNNETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDPPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDRYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>Q07589</accession>
+    <name>Uncharacterized protein YDL144C</name>
+    <protein>
+      <recommendedName>
+        <fullName>Uncharacterized protein YDL144C</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">YDL144C</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="356">MSRILVIGAGGVGVITALSLWLKKESDVSLVVRSDYDRVLKHGYTIESCDYGRLEGWRPHHIYSSVEDAASAADNQGYNYIVVTTKNIIDGPVNSRVSNIIRPVLEKNKELHGPQLTTHILLVQNGIDIEKEIWAEFPREQYRYTVLSGIQLIGSTKIGSGHISQVGQDHLSCGAFDPQDAAAIQAANDFVRMYSNEGQNFVEFDPRVRYSRWKKLLYNAAINTSTALVGLDVPRCLEFGVNKKSTEIEVFHPAMREIIAIAASEGIIIEEEFITMFTEITRKKVFKPSMCVDCEKGQLMELEVILGNPIRIAKRNGVATPTLSILYNLLVLVQAKLKERKGLLKFDEKTATLVDE</sequence>
+  </entry>
+  <entry>
+    <accession>Q6Q5H1</accession>
+    <name>Transposon Ty1-PR3 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-PR3 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-PR3</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>P0C2I3</accession>
+    <name>Transposon Ty1-DR6 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-DR6 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-DR6</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNYLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P47098</accession>
+    <name>Transposon Ty1-JR1 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-JR1 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-JR1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX76</accession>
+    <name>Transposon Ty1-ML2 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-ML2 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-ML2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>Q03434</accession>
+    <name>Transposon Ty1-ML2 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-ML2 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-ML2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDRSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P0C2I7</accession>
+    <name>Transposon Ty1-LR4 Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-LR4 Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-LR4</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHPHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P38079</accession>
+    <name>Protein YRO2</name>
+    <protein>
+      <recommendedName>
+        <fullName>Protein YRO2</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">YRO2</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="344">MSDYVELLKRGGNEAIKINPPTGADFHITSRGSDWLFTVFCVNLLFGVILVPLMFRKPVKDRFVYYTAIAPNLFMSIAYFTMASNLGWIPVRAKYNHVQTSTQKEHPGYRQIFYARYVGWFLAFPWPIIQMSLLGGTPLWQIAFNVGMTEIFTVCWLIAACVHSTYKWGYYTIGIGAAIVVCISLMTTTFNLVKARGKDVSNVFITFMSVIMFLWLIAYPTCFGITDGGNVLQPDSATIFYGIIDLLILSILPVLFMPLANYLGIERLGLIFDEEPAEHVGPVAEKKMPSPASFKSSDSDSSIKEKLKLKKKHKKDKKKAKKAKKAKKAKKAQEEEEDVATDSE</sequence>
+  </entry>
+  <entry>
+    <accession>Q92392</accession>
+    <name>Transposon Ty1-OL Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-OL Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-OL</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+  <entry>
+    <accession>Q12414</accession>
+    <name>Transposon Ty1-PL Gag-Pol polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-PL Gag-Pol polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1B-PL</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="1755">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+  </entry>
+  <entry>
+    <accession>P31111</accession>
+    <name>Synaptonemal complex protein ZIP1</name>
+    <protein>
+      <recommendedName>
+        <fullName>Synaptonemal complex protein ZIP1</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">ZIP1</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="875">MSNFFRDSSMGFKPRPNIFAKLRVRDVDSDSSANTVVENSSNCLDVGSSIEGDDTFKKPHKTSTEQELITSMSLSQRNHGYSDDMEIGSPKKTTSTDQYNRILKNDVAAIENDTDEDFEITEVREVSEGVAKETKESHGDPNDSETTLKDSKMHEYTMTNGKAPLHTSINNSSTSSNDVLLEAFTNTQRICSNLKQELQKQQQDNAKLKVRLQSYASNSDKINEKVGKYKSCLETLQERIATLTSHKNNQETKLKDLRQNHQLYQRRISGFKTSIENLNKTINDLGKNKKEADAELMKKGKEIEYLKRELDDCSGQLSEEKIKNSSLIQEMGKNREEMIKSIENFFSEDKAHHLLQFNKFEERVHDLFEKKLQKHFDVAKDTLNVGLRNTTVELSSNTETMLKQQYEDIKENLEQKMSSSKDEMAKTINELSVTQKGLIMGVQEELLTSSGNIQTALVSEMNNTRQELLDDASQTAKNYASLENLVKAYKAEIVQSNEYEERIKHLESERSTLSSQKNQIISSLGTKEAQYEDLVKKLEAKNIEISQISGKEQSLTEKNENLSNELKKVQDQLEKLNNLNITTKSNYENKISSQNEIVKALVSENDTLKQRIQQLVEIKENEQKDHTTKLEAFQKNNEQLQKLNVEVVQLKAHELELEEQNRHLKNCLEKKETGVEESLSDVKTLKQQVIVLKSEKQDITAEKLELQDNLESLEEVTKNLQQKVQSQKRELEQKIKELEEIKNHKRNEPSKKGTQNFTKPSDSPKKNATTSNLFPNNSAAIHSPMKKCPKVDHISKSRINSSKETSKFNDEFDLSSSSNDDLELTNPSPIQIKPVRGKIKKGSNCMKPPISSRKKLLLVEDEDQSLKISKKRRRK</sequence>
+  </entry>
+  <entry>
+    <accession>P0CX75</accession>
+    <name>Transposon Ty1-LR3 Gag polyprotein</name>
+    <protein>
+      <recommendedName>
+        <fullName>Transposon Ty1-LR3 Gag polyprotein</fullName>
+      </recommendedName>
+    </protein>
+    <gene>
+      <name type="primary">TY1A-LR3</name>
+    </gene>
+    <organism>
+      <name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+    </organism>
+    <sequence length="440">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+  </entry>
+</mzLibProteinDb>
\ No newline at end of file

--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/test-data/SmallYeast_uniprot.xml	Wed May 26 15:42:20 2021 +0000
@@ -0,0 +1,84141 @@
+<?xml version='1.0' encoding='UTF-8'?>
+<uniprot xmlns="http://uniprot.org/uniprot" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" xsi:schemaLocation="http://uniprot.org/uniprot http://www.uniprot.org/support/docs/uniprot.xsd">
+<entry dataset="Swiss-Prot" created="1994-10-01" modified="2021-04-07" version="203">
+<accession>P38013</accession>
+<accession>D6VYA9</accession>
+<name>AHP1_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="16">Peroxiredoxin AHP1</fullName>
+<shortName>Prx</shortName>
+<ecNumber evidence="2 10">1.11.1.24</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName evidence="15">Alkyl hydroperoxide reductase</fullName>
+<shortName>AHPC1</shortName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="13">Cytoplasmic thiol peroxidase 3</fullName>
+<shortName evidence="13">cTPx 3</shortName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="13">Thiol-specific antioxidant II</fullName>
+<shortName evidence="13">TSA II</shortName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="14">Thioredoxin peroxidase type II</fullName>
+<shortName>TPx type II</shortName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="16">Thioredoxin-dependent peroxiredoxin AHP1</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="15">AHP1</name>
+<name type="ordered locus">YLR109W</name>
+<name type="ORF">L2916</name>
+<name type="ORF">L9354.5</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Yeast" volume="13" first="241" last="250">
+<title>Sequence analysis of a 37.6 kbp cosmid clone from the right arm of Saccharomyces cerevisiae chromosome XII, carrying YAP3, HOG1, SNR6, tRNA-Arg3 and 23 new open reading frames, among which several homologies to proteins involved in cell division control and to mammalian growth factors and other animal proteins are found.</title>
+<authorList>
+<person name="Verhasselt P."/>
+<person name="Volckaert G."/>
+</authorList>
+<dbReference type="PubMed" id="9090053"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19970315)13:3&lt;241::aid-yea61>3.0.co;2-#"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 90840 / EAY235 / FY23</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
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+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
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+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
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+<person name="Schwager C."/>
+<person name="Schwarz S."/>
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+<person name="Urrestarazu L.A."/>
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+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
+<person name="Zollner A."/>
+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
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+<authorList>
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+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="submission" date="2005-05" db="UniProtKB">
+<authorList>
+<person name="Bienvenut W.V."/>
+<person name="Peters C."/>
+</authorList>
+</citation>
+<scope>PROTEIN SEQUENCE OF 2-8; 16-48; 80-102 AND 114-176</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE</scope>
+<scope>ACETYLATION AT SER-2</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2003" name="Eukaryot. Cell" volume="2" first="930" last="936">
+<title>Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p.</title>
+<authorList>
+<person name="Goehring A.S."/>
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+</authorList>
+<dbReference type="PubMed" id="14555475"/>
+<dbReference type="DOI" id="10.1128/ec.2.5.930-936.2003"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 8-15; 33-41; 80-102 AND 125-176</scope>
+<scope>URMYLATION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1999" name="Biochemistry" volume="38" first="776" last="783">
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+</authorList>
+<dbReference type="PubMed" id="9888818"/>
+<dbReference type="DOI" id="10.1021/bi9817818"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 16-41; 49-68; 82-96; 114-123 AND 142-150</scope>
+<scope>POST-TRANSLATIONAL MODIFICATION</scope>
+<scope>DISULFIDE BONDS</scope>
+<scope>CATALYTIC ACTIVITY</scope>
+<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="1999" name="J. Biol. Chem." volume="274" first="19714" last="19722">
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+</authorList>
+<dbReference type="PubMed" id="10391912"/>
+<dbReference type="DOI" id="10.1074/jbc.274.28.19714"/>
+</citation>
+<scope>PARTIAL PROTEIN SEQUENCE OF 33-37; 82-96; 126-139 AND 157-170</scope>
+<scope>FUNCTION</scope>
+<scope>CATALYTIC ACTIVITY</scope>
+<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="1994" name="Electrophoresis" volume="15" first="1466" last="1486">
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+<authorList>
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+</authorList>
+<dbReference type="PubMed" id="7895733"/>
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+</citation>
+<scope>PROTEIN SEQUENCE OF 82-99</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="9">
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+<authorList>
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+</authorList>
+<dbReference type="PubMed" id="10635552"/>
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+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="10">
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+</authorList>
+<dbReference type="PubMed" id="9988687"/>
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+</citation>
+<scope>FUNCTION</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="11">
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+</authorList>
+<dbReference type="PubMed" id="10681558"/>
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+</citation>
+<scope>FUNCTION</scope>
+<scope>INDUCTION</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="12">
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+<authorList>
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+</authorList>
+<dbReference type="PubMed" id="14562106"/>
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+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
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+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
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+<authorList>
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+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28 AND SER-116</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="15">
+<citation type="journal article" date="2010" name="J. Biol. Chem." volume="285" first="10597" last="10604">
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+<authorList>
+<person name="Iwai K."/>
+<person name="Naganuma A."/>
+<person name="Kuge S."/>
+</authorList>
+<dbReference type="PubMed" id="20145245"/>
+<dbReference type="DOI" id="10.1074/jbc.m109.090142"/>
+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="16">
+<citation type="journal article" date="2011" name="Proc. Natl. Acad. Sci. U.S.A." volume="108" first="1763" last="1770">
+<title>Role of the ubiquitin-like protein Urm1 as a noncanonical lysine-directed protein modifier.</title>
+<authorList>
+<person name="Van der Veen A.G."/>
+<person name="Schorpp K."/>
+<person name="Schlieker C."/>
+<person name="Buti L."/>
+<person name="Damon J.R."/>
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+<person name="Ploegh H.L."/>
+<person name="Jentsch S."/>
+</authorList>
+<dbReference type="PubMed" id="21209336"/>
+<dbReference type="DOI" id="10.1073/pnas.1014402108"/>
+</citation>
+<scope>URMYLATION AT LYS-32</scope>
+<scope>MUTAGENESIS OF LYS-32</scope>
+</reference>
+<reference key="17">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48 AND LYS-113</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="18">
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+<authorList>
+<person name="Trivelli X."/>
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+<dbReference type="PubMed" id="14640681"/>
+<dbReference type="DOI" id="10.1021/bi035551r"/>
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+<scope>3D-STRUCTURE MODELING</scope>
+<scope>STRUCTURE BY NMR</scope>
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+<person name="Ma X.X."/>
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+<person name="Chen Y."/>
+<person name="Zhou C.Z."/>
+</authorList>
+<dbReference type="PubMed" id="22474296"/>
+<dbReference type="DOI" id="10.1074/jbc.m112.357368"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH TRX2</scope>
+<scope>ACTIVE SITE</scope>
+<scope>DISULFIDE BOND</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="20">
+<citation type="submission" date="2012-09" db="PDB data bank">
+<title>Crystal structure of Ahp1 from Saccharomyces cerevisiae in reduced form.</title>
+<authorList>
+<person name="Liu M."/>
+<person name="Wang F."/>
+<person name="Qiu R."/>
+<person name="Wu T."/>
+<person name="Gu S."/>
+<person name="Tang R."/>
+<person name="Ji C."/>
+</authorList>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS)</scope>
+</reference>
+<reference key="21">
+<citation type="submission" date="2014-02" db="PDB data bank">
+<title>Crystal structure of Ahp1 from Saccharomyces cerevisiae. Investigating the electron transfers.</title>
+<authorList>
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+<person name="Genu V."/>
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+<person name="Guimaraes B.G."/>
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+<person name="Netto L.E.S."/>
+</authorList>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS)</scope>
+<scope>DISULFIDE BONDS</scope>
+</reference>
+<comment type="function">
+<text evidence="2 3 4 7 11">Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Preferentially eliminates organic peroxides rather than hydrogen peroxide (PubMed:10391912, PubMed:9988687, PubMed:10681558). Relays alkyl hydroperoxides as a signal to the transcription factor CAD1/YAP2 by inducing the formation of intramolecular disulfide bonds in CAD1, which causes its nuclear accumulation and activation (PubMed:20145245). Involved in cellular Mn(2+) homeostasis (PubMed:10635552).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="2 10">
+<text>[thioredoxin]-dithiol + a hydroperoxide = [thioredoxin]-disulfide + an alcohol + H2O</text>
+<dbReference type="Rhea" id="RHEA:62620"/>
+<dbReference type="Rhea" id="RHEA-COMP:10698"/>
+<dbReference type="Rhea" id="RHEA-COMP:10700"/>
+<dbReference type="ChEBI" id="CHEBI:15377"/>
+<dbReference type="ChEBI" id="CHEBI:29950"/>
+<dbReference type="ChEBI" id="CHEBI:30879"/>
+<dbReference type="ChEBI" id="CHEBI:35924"/>
+<dbReference type="ChEBI" id="CHEBI:50058"/>
+<dbReference type="EC" id="1.11.1.24"/>
+</reaction>
+</comment>
+<comment type="biophysicochemical properties">
+<kinetics>
+<KM evidence="10">150 uM for H(2)O(2)</KM>
+<KM evidence="2">14 uM for H(2)O(2)</KM>
+<KM evidence="10">8 uM for cumene hydroperoxide</KM>
+<KM evidence="10">45 uM for tert-butyl hydroperoxide</KM>
+<KM evidence="9">76.9 uM for tert-butyl hydroperoxide</KM>
+<KM evidence="10">3 uM for TRX1</KM>
+<KM evidence="10">2 uM for TRX2</KM>
+<KM evidence="9">1.3 uM for TRX2</KM>
+<Vmax evidence="10">20 umol/min/mg enzyme for H(2)O(2)</Vmax>
+<Vmax evidence="10">14 umol/min/mg enzyme for cumene hydroperoxide</Vmax>
+<Vmax evidence="10">17 umol/min/mg enzyme for tert-butyl hydroperoxide</Vmax>
+<Vmax evidence="10">17 umol/min/mg enzyme for TRX1</Vmax>
+<Vmax evidence="10">16 umol/min/mg enzyme for TRX2</Vmax>
+</kinetics>
+<phDependence>
+<text evidence="10">Optimum pH is 6.5.</text>
+</phDependence>
+</comment>
+<comment type="subunit">
+<text evidence="2 9 10 11">Homodimer; disulfide-linked, upon oxidation.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-2382">
+<id>P38013</id>
+</interactant>
+<interactant intactId="EBI-2464632">
+<id>P34230</id>
+<label>PXA2</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="4">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="induction">
+<text evidence="4">By H(2)O(2).</text>
+</comment>
+<comment type="PTM">
+<text evidence="5 8">Conjugated to URM1, a ubiquitin-like protein.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="18">The active site is a conserved redox-active cysteine residue, the peroxidatic cysteine (C(P)), which makes the nucleophilic attack on the peroxide substrate. The peroxide oxidizes the C(P)-SH to cysteine sulfenic acid (C(P)-SOH), which then reacts with another cysteine residue, the resolving cysteine (C(R)), to form a disulfide bridge. The disulfide is subsequently reduced by an appropriate electron donor to complete the catalytic cycle. In this typical 2-Cys Prx, C(R) is provided by the other dimeric subunit to form an intersubunit disulfide. The disulfide is subsequently reduced by thioredoxin.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="6">Present with 16228 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="16">Belongs to the peroxiredoxin family. Prx5 subfamily.</text>
+</comment>
+<comment type="caution">
+<text evidence="18 19 20">Biochemical and mutational analysis assigned Cys-120 as the resolving cysteine (C(R)) (PubMed:9888818). However, crystal structures showed that Cys-120 is deeply buried within the protein and revealed formation of a disulfide bond between the peroxidatic cysteine Cys-62 and the therefore more likely C(R) Cys-31 (PubMed:22474296, Ref.21).</text>
+</comment>
+<dbReference type="EC" id="1.11.1.24" evidence="2 10"/>
+<dbReference type="EMBL" id="X89514">
+<property type="protein sequence ID" value="CAA61687.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z73281">
+<property type="protein sequence ID" value="CAA97676.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="U53878">
+<property type="protein sequence ID" value="AAB67554.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09425.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S64946">
+<property type="entry name" value="S64946"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013210.1">
+<property type="nucleotide sequence ID" value="NM_001181996.1"/>
+</dbReference>
+<dbReference type="PDB" id="4DSQ">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.40"/>
+<property type="chains" value="A/B/C/D=1-176"/>
+</dbReference>
+<dbReference type="PDB" id="4DSR">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.91"/>
+<property type="chains" value="A/B/C/D=1-176"/>
+</dbReference>
+<dbReference type="PDB" id="4DSS">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.10"/>
+<property type="chains" value="A=1-176"/>
+</dbReference>
+<dbReference type="PDB" id="4H86">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.00"/>
+<property type="chains" value="A=1-176"/>
+</dbReference>
+<dbReference type="PDB" id="4OWY">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.20"/>
+<property type="chains" value="A/B/C/D=1-176"/>
+</dbReference>
+<dbReference type="PDB" id="7BVV">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.12"/>
+<property type="chains" value="A=1-176"/>
+</dbReference>
+<dbReference type="PDBsum" id="4DSQ"/>
+<dbReference type="PDBsum" id="4DSR"/>
+<dbReference type="PDBsum" id="4DSS"/>
+<dbReference type="PDBsum" id="4H86"/>
+<dbReference type="PDBsum" id="4OWY"/>
+<dbReference type="PDBsum" id="7BVV"/>
+<dbReference type="BMRB" id="P38013"/>
+<dbReference type="SMR" id="P38013"/>
+<dbReference type="BioGRID" id="31382">
+<property type="interactions" value="114"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-6375N"/>
+<dbReference type="IntAct" id="P38013">
+<property type="interactions" value="15"/>
+</dbReference>
+<dbReference type="MINT" id="P38013"/>
+<dbReference type="STRING" id="4932.YLR109W"/>
+<dbReference type="iPTMnet" id="P38013"/>
+<dbReference type="COMPLUYEAST-2DPAGE" id="P38013"/>
+<dbReference type="MaxQB" id="P38013"/>
+<dbReference type="PaxDb" id="P38013"/>
+<dbReference type="PRIDE" id="P38013"/>
+<dbReference type="TopDownProteomics" id="P38013"/>
+<dbReference type="EnsemblFungi" id="YLR109W_mRNA">
+<property type="protein sequence ID" value="YLR109W"/>
+<property type="gene ID" value="YLR109W"/>
+</dbReference>
+<dbReference type="GeneID" id="850799"/>
+<dbReference type="KEGG" id="sce:YLR109W"/>
+<dbReference type="SGD" id="S000004099">
+<property type="gene designation" value="AHP1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YLR109W"/>
+<dbReference type="eggNOG" id="KOG0541">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00390000018173"/>
+<dbReference type="HOGENOM" id="CLU_072440_1_1_1"/>
+<dbReference type="InParanoid" id="P38013"/>
+<dbReference type="OMA" id="ARHVPEY"/>
+<dbReference type="PRO" id="PR:P38013"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XII"/>
+</dbReference>
+<dbReference type="RNAct" id="P38013">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005886">
+<property type="term" value="C:plasma membrane"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008379">
+<property type="term" value="F:thioredoxin peroxidase activity"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0045454">
+<property type="term" value="P:cell redox homeostasis"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0034599">
+<property type="term" value="P:cellular response to oxidative stress"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0042744">
+<property type="term" value="P:hydrogen peroxide catabolic process"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0010038">
+<property type="term" value="P:response to metal ion"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="CDD" id="cd03013">
+<property type="entry name" value="PRX5_like"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.40.30.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR037944">
+<property type="entry name" value="PRX5-like"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013740">
+<property type="entry name" value="Redoxin"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036249">
+<property type="entry name" value="Thioredoxin-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013766">
+<property type="entry name" value="Thioredoxin_domain"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR10430">
+<property type="entry name" value="PTHR10430"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF08534">
+<property type="entry name" value="Redoxin"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF52833">
+<property type="entry name" value="SSF52833"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS51352">
+<property type="entry name" value="THIOREDOXIN_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0049">Antioxidant</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-1015">Disulfide bond</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0560">Oxidoreductase</keyword>
+<keyword id="KW-0575">Peroxidase</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0676">Redox-active center</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="12">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="Peroxiredoxin AHP1" id="PRO_0000056610">
+<location>
+<begin position="2"/>
+<end position="176"/>
+</location>
+</feature>
+<feature type="domain" description="Thioredoxin" evidence="1">
+<location>
+<begin position="9"/>
+<end position="176"/>
+</location>
+</feature>
+<feature type="active site" description="Cysteine sulfenic acid (-SOH) intermediate" evidence="18">
+<location>
+<position position="62"/>
+</location>
+</feature>
+<feature type="modified residue" description="N-acetylserine" evidence="12">
+<location>
+<position position="2"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="25">
+<location>
+<position position="28"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="24">
+<location>
+<position position="59"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="25">
+<location>
+<position position="116"/>
+</location>
+</feature>
+<feature type="disulfide bond" description="Interchain (with C-31 in TRX2); transient" evidence="9">
+<location>
+<position position="31"/>
+</location>
+</feature>
+<feature type="disulfide bond" description="Interchain (with C-62); in linked form" evidence="9 21 23">
+<location>
+<position position="31"/>
+</location>
+</feature>
+<feature type="disulfide bond" description="Interchain (with C-31); in linked form" evidence="9 21 23">
+<location>
+<position position="62"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in URM1)" evidence="17">
+<location>
+<position position="32"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="26">
+<location>
+<position position="48"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="26">
+<location>
+<position position="113"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Abolishes catalytic activity." evidence="9">
+<original>C</original>
+<variation>S</variation>
+<location>
+<position position="31"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Prevents urmylation of AHP1." evidence="8">
+<original>K</original>
+<variation>R</variation>
+<location>
+<position position="32"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Abolishes catalytic activity." evidence="9">
+<original>C</original>
+<variation>S</variation>
+<location>
+<position position="62"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="No effect on tert-butyl hydroperoxide consumption." evidence="9">
+<original>C</original>
+<variation>S</variation>
+<location>
+<position position="120"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 6; AA sequence." ref="6" evidence="16">
+<original>I</original>
+<variation>T</variation>
+<location>
+<position position="21"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 6; AA sequence." ref="6" evidence="16">
+<original>S</original>
+<variation>V</variation>
+<location>
+<position position="65"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 6; AA sequence." ref="6" evidence="16">
+<original>I</original>
+<variation>E</variation>
+<location>
+<position position="87"/>
+</location>
+</feature>
+<feature type="turn" evidence="22">
+<location>
+<begin position="3"/>
+<end position="6"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="15"/>
+<end position="18"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="23"/>
+<end position="25"/>
+</location>
+</feature>
+<feature type="strand" evidence="23">
+<location>
+<begin position="26"/>
+<end position="28"/>
+</location>
+</feature>
+<feature type="helix" evidence="22">
+<location>
+<begin position="29"/>
+<end position="31"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="35"/>
+<end position="38"/>
+</location>
+</feature>
+<feature type="helix" evidence="22">
+<location>
+<begin position="39"/>
+<end position="45"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="47"/>
+<end position="53"/>
+</location>
+</feature>
+<feature type="helix" evidence="22">
+<location>
+<begin position="60"/>
+<end position="64"/>
+</location>
+</feature>
+<feature type="helix" evidence="22">
+<location>
+<begin position="67"/>
+<end position="80"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="85"/>
+<end position="92"/>
+</location>
+</feature>
+<feature type="helix" evidence="22">
+<location>
+<begin position="94"/>
+<end position="103"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="110"/>
+<end position="116"/>
+</location>
+</feature>
+<feature type="helix" evidence="22">
+<location>
+<begin position="118"/>
+<end position="120"/>
+</location>
+</feature>
+<feature type="helix" evidence="22">
+<location>
+<begin position="121"/>
+<end position="125"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="129"/>
+<end position="133"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="136"/>
+<end position="139"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="141"/>
+<end position="147"/>
+</location>
+</feature>
+<feature type="strand" evidence="22">
+<location>
+<begin position="150"/>
+<end position="156"/>
+</location>
+</feature>
+<feature type="turn" evidence="22">
+<location>
+<begin position="160"/>
+<end position="162"/>
+</location>
+</feature>
+<feature type="helix" evidence="22">
+<location>
+<begin position="169"/>
+<end position="173"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00691"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="10391912"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="10635552"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="10681558"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14555475"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="7" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="20145245"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="21209336"/>
+</source>
+</evidence>
+<evidence key="9" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22474296"/>
+</source>
+</evidence>
+<evidence key="10" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="9888818"/>
+</source>
+</evidence>
+<evidence key="11" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="9988687"/>
+</source>
+</evidence>
+<evidence key="12" type="ECO:0000269">
+<source ref="4"/>
+</evidence>
+<evidence key="13" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="10681558"/>
+</source>
+</evidence>
+<evidence key="14" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9888818"/>
+</source>
+</evidence>
+<evidence key="15" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9988687"/>
+</source>
+</evidence>
+<evidence key="16" type="ECO:0000305"/>
+<evidence key="17" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="21209336"/>
+</source>
+</evidence>
+<evidence key="18" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="22474296"/>
+</source>
+</evidence>
+<evidence key="19" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9888818"/>
+</source>
+</evidence>
+<evidence key="20" type="ECO:0000305">
+<source ref="21"/>
+</evidence>
+<evidence key="21" type="ECO:0007744">
+<source>
+<dbReference type="PDB" id="4DSQ"/>
+</source>
+</evidence>
+<evidence key="22" type="ECO:0007744">
+<source>
+<dbReference type="PDB" id="4H86"/>
+</source>
+</evidence>
+<evidence key="23" type="ECO:0007744">
+<source>
+<dbReference type="PDB" id="4OWY"/>
+</source>
+</evidence>
+<evidence key="24" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="18407956"/>
+</source>
+</evidence>
+<evidence key="25" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="19779198"/>
+</source>
+</evidence>
+<evidence key="26" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22106047"/>
+</source>
+</evidence>
+<sequence length="176" mass="19115" checksum="11B730781306A015" modified="2007-01-23" version="4">MSDLVNKKFPAGDYKFQYIAISQSDADSESCKMPQTVEWSKLISENKKVIITGAPAAFSPTCTVSHIPGYINYLDELVKEKEVDQVIVVTVDNPFANQAWAKSLGVKDTTHIKFASDPGCAFTKSIGFELAVGDGVYWSGRWAMVVENGIVTYAAKETNPGTDVTVSSVESVLAHL</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1995-11-01" modified="2021-04-07" version="187">
+<accession>P46672</accession>
+<accession>D6VU41</accession>
+<name>ARC1_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>tRNA-aminoacylation cofactor ARC1</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Acyl-RNA-complex protein 1</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>GU4 nucleic-binding protein 1</fullName>
+<shortName>G4p1 protein</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>P42</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>tRNA-interacting factor ARC1</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">ARC1</name>
+<name type="synonym">G4P1</name>
+<name type="ordered locus">YGL105W</name>
+<name type="ORF">G3085</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="J. Biol. Chem." volume="270" first="20692" last="20697">
+<title>A novel yeast gene product, G4p1, with a specific affinity for quadruplex nucleic acids.</title>
+<authorList>
+<person name="Frantz J.D."/>
+<person name="Gilbert W."/>
+</authorList>
+<dbReference type="PubMed" id="7657649"/>
+<dbReference type="DOI" id="10.1074/jbc.270.35.20692"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<scope>PROTEIN SEQUENCE OF 53-75 AND 102-123</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1996" name="EMBO J." volume="15" first="5437" last="5448">
+<title>The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases.</title>
+<authorList>
+<person name="Simos G."/>
+<person name="Segref A."/>
+<person name="Fasiolo F."/>
+<person name="Hellmuth K."/>
+<person name="Shevshenko A."/>
+<person name="Mann M."/>
+<person name="Hurt E.C."/>
+</authorList>
+<dbReference type="PubMed" id="8895587"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1996.tb00927.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<scope>FUNCTION</scope>
+<scope>TRNA-BINDING</scope>
+<scope>INTERACTION WITH GUS1 AND MES1</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+<source>
+<strain>JU4.2XJR26.19B</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1997" name="Yeast" volume="13" first="85" last="91">
+<title>The genes encoding the transcription factor yTAFII60, the G4p1 protein and a putative glucose transporter are contained in a 12.3 kb DNA fragment on the left arm of Saccharomyces cerevisiae chromosome VII.</title>
+<authorList>
+<person name="Paoluzi S."/>
+<person name="Minenkova O."/>
+<person name="Castagnoli L."/>
+</authorList>
+<dbReference type="PubMed" id="9046090"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199701)13:1&lt;85::aid-yea53>3.0.co;2-e"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="81" last="84">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.</title>
+<authorList>
+<person name="Tettelin H."/>
+<person name="Agostoni-Carbone M.L."/>
+<person name="Albermann K."/>
+<person name="Albers M."/>
+<person name="Arroyo J."/>
+<person name="Backes U."/>
+<person name="Barreiros T."/>
+<person name="Bertani I."/>
+<person name="Bjourson A.J."/>
+<person name="Brueckner M."/>
+<person name="Bruschi C.V."/>
+<person name="Carignani G."/>
+<person name="Castagnoli L."/>
+<person name="Cerdan E."/>
+<person name="Clemente M.L."/>
+<person name="Coblenz A."/>
+<person name="Coglievina M."/>
+<person name="Coissac E."/>
+<person name="Defoor E."/>
+<person name="Del Bino S."/>
+<person name="Delius H."/>
+<person name="Delneri D."/>
+<person name="de Wergifosse P."/>
+<person name="Dujon B."/>
+<person name="Durand P."/>
+<person name="Entian K.-D."/>
+<person name="Eraso P."/>
+<person name="Escribano V."/>
+<person name="Fabiani L."/>
+<person name="Fartmann B."/>
+<person name="Feroli F."/>
+<person name="Feuermann M."/>
+<person name="Frontali L."/>
+<person name="Garcia-Gonzalez M."/>
+<person name="Garcia-Saez M.I."/>
+<person name="Goffeau A."/>
+<person name="Guerreiro P."/>
+<person name="Hani J."/>
+<person name="Hansen M."/>
+<person name="Hebling U."/>
+<person name="Hernandez K."/>
+<person name="Heumann K."/>
+<person name="Hilger F."/>
+<person name="Hofmann B."/>
+<person name="Indge K.J."/>
+<person name="James C.M."/>
+<person name="Klima R."/>
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+<person name="Kramer W."/>
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+<person name="Leuther H."/>
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+<person name="Maillier E."/>
+<person name="Marconi A."/>
+<person name="Martegani E."/>
+<person name="Mazon M.J."/>
+<person name="Mazzoni C."/>
+<person name="McReynolds A.D.K."/>
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+<person name="Mewes H.-W."/>
+<person name="Minenkova O."/>
+<person name="Mueller-Auer S."/>
+<person name="Nawrocki A."/>
+<person name="Netter P."/>
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+<person name="Paoluzi S."/>
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+<person name="Riles L."/>
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+<person name="Rodrigues-Pousada C."/>
+<person name="Rodriguez-Belmonte E."/>
+<person name="Rodriguez-Torres A.M."/>
+<person name="Rose M."/>
+<person name="Ruzzi M."/>
+<person name="Saliola M."/>
+<person name="Sanchez-Perez M."/>
+<person name="Schaefer B."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Schmidheini T."/>
+<person name="Schreer A."/>
+<person name="Skala J."/>
+<person name="Souciet J.-L."/>
+<person name="Steensma H.Y."/>
+<person name="Talla E."/>
+<person name="Thierry A."/>
+<person name="Vandenbol M."/>
+<person name="van der Aart Q.J.M."/>
+<person name="Van Dyck L."/>
+<person name="Vanoni M."/>
+<person name="Verhasselt P."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Wambutt R."/>
+<person name="Watson M.D."/>
+<person name="Weber N."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Wipfli P."/>
+<person name="Wolf K."/>
+<person name="Wright L.F."/>
+<person name="Zaccaria P."/>
+<person name="Zimmermann M."/>
+<person name="Zollner A."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="9169869"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
+<person name="Rolfs A."/>
+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
+<person name="Zhu C."/>
+<person name="Berger M.F."/>
+<person name="Camargo A.A."/>
+<person name="Kelley F."/>
+<person name="McCarron S."/>
+<person name="Jepson D."/>
+<person name="Richardson A."/>
+<person name="Raphael J."/>
+<person name="Moreira D."/>
+<person name="Taycher E."/>
+<person name="Zuo D."/>
+<person name="Mohr S."/>
+<person name="Kane M.F."/>
+<person name="Williamson J."/>
+<person name="Simpson A.J.G."/>
+<person name="Bulyk M.L."/>
+<person name="Harlow E."/>
+<person name="Marsischky G."/>
+<person name="Kolodner R.D."/>
+<person name="LaBaer J."/>
+</authorList>
+<dbReference type="PubMed" id="17322287"/>
+<dbReference type="DOI" id="10.1101/gr.6037607"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="7">
+<citation type="journal article" date="1998" name="Mol. Cell" volume="1" first="235" last="242">
+<title>A conserved domain within Arc1p delivers tRNA to aminoacyl-tRNA synthetases.</title>
+<authorList>
+<person name="Simos G."/>
+<person name="Sauer A."/>
+<person name="Fasiolo F."/>
+<person name="Hurt E.C."/>
+</authorList>
+<dbReference type="PubMed" id="9659920"/>
+<dbReference type="DOI" id="10.1016/s1097-2765(00)80024-6"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>TRNA BINDING</scope>
+<scope>INTERACTION WITH GUS1 AND MES1</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2001" name="EMBO J." volume="20" first="6889" last="6898">
+<title>The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p.</title>
+<authorList>
+<person name="Galani K."/>
+<person name="Grosshans H."/>
+<person name="Deinert K."/>
+<person name="Hurt E.C."/>
+<person name="Simos G."/>
+</authorList>
+<dbReference type="PubMed" id="11726524"/>
+<dbReference type="DOI" id="10.1093/emboj/20.23.6889"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>INTERACTION WITH GUS1 AND MES1</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="6000" last="6008">
+<title>Arc1p organizes the yeast aminoacyl-tRNA synthetase complex and stabilizes its interaction with the cognate tRNAs.</title>
+<authorList>
+<person name="Deinert K."/>
+<person name="Fasiolo F."/>
+<person name="Hurt E.C."/>
+<person name="Simos G."/>
+</authorList>
+<dbReference type="PubMed" id="11069915"/>
+<dbReference type="DOI" id="10.1074/jbc.m008682200"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>TRNA-BINDING</scope>
+<scope>INTERACTION WITH GUS1 AND MES1</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2005" name="FEBS Lett." volume="579" first="969" last="975">
+<title>The tRNA aminoacylation co-factor Arc1p is excluded from the nucleus by an Xpo1p-dependent mechanism.</title>
+<authorList>
+<person name="Galani K."/>
+<person name="Hurt E."/>
+<person name="Simos G."/>
+</authorList>
+<dbReference type="PubMed" id="15710377"/>
+<dbReference type="DOI" id="10.1016/j.febslet.2004.11.112"/>
+</citation>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2007" name="Mol. Cell. Biochem." volume="300" first="47" last="59">
+<title>Arc1p is required for cytoplasmic confinement of synthetases and tRNA.</title>
+<authorList>
+<person name="Golinelli-Cohen M.P."/>
+<person name="Mirande M."/>
+</authorList>
+<dbReference type="PubMed" id="17131041"/>
+<dbReference type="DOI" id="10.1007/s11010-006-9367-4"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2006" name="Acta Crystallogr. D" volume="62" first="1510" last="1519">
+<title>Structures of the interacting domains from yeast glutamyl-tRNA synthetase and tRNA-aminoacylation and nuclear-export cofactor Arc1p reveal a novel function for an old fold.</title>
+<authorList>
+<person name="Simader H."/>
+<person name="Hothorn M."/>
+<person name="Suck D."/>
+</authorList>
+<dbReference type="PubMed" id="17139087"/>
+<dbReference type="DOI" id="10.1107/s0907444906039850"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-122</scope>
+<scope>INTERACTION WITH GUS1</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2006" name="Nucleic Acids Res." volume="34" first="3968" last="3979">
+<title>Structural basis of yeast aminoacyl-tRNA synthetase complex formation revealed by crystal structures of two binary sub-complexes.</title>
+<authorList>
+<person name="Simader H."/>
+<person name="Hothorn M."/>
+<person name="Koehler C."/>
+<person name="Basquin J."/>
+<person name="Simos G."/>
+<person name="Suck D."/>
+</authorList>
+<dbReference type="PubMed" id="16914447"/>
+<dbReference type="DOI" id="10.1093/nar/gkl560"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-122 IN COMPLEXES WITH GUS1 AND MES1</scope>
+<scope>MUTAGENESIS OF ALA-26 AND ARG-100</scope>
+</reference>
+<comment type="function">
+<text evidence="2 7 9 10">Binds to tRNA and functions as a cofactor for the methionyl-tRNA synthetase (MetRS) and glutamyl-tRNA synthetase (GluRS). Forms a complex with MetRS and GluRS and increases their affinity for cognate tRNAs due to the presence of a tRNA binding domain in its middle and C-terminal part. Binds specifically G4 quadruplex nucleic acid structures (these are four-stranded right-handed helices, stabilized by guanine base quartets). Also required for cytoplasmic confinement of the synthetases and tRNA.</text>
+</comment>
+<comment type="subunit">
+<text evidence="2 3 8 9 10">Component of a yeast aminoacyl-tRNA synthase (aaRS) complex formed by methionyl-tRNA synthase MES1, glutamyl-tRNA synthase GUS1 and the tRNA aminoacylation cofactor ARC1 in a stoichiometric complex. Interacts (via N-ter) with MES1 (via N-ter) and GUS1 (via N-ter). Can also form a stable binary complex with either MES1 or GUS1 that is functional in terms of aminoacylation.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-7224">
+<id>P46672</id>
+</interactant>
+<interactant intactId="EBI-18665">
+<id>P46655</id>
+<label>GUS1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>7</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-7224">
+<id>P46672</id>
+</interactant>
+<interactant intactId="EBI-18762">
+<id>P00958</id>
+<label>MES1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>7</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="3 5 7 9">Cytoplasm</location>
+</subcellularLocation>
+<text>Largely excluded from the nucleus.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 57700 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="11">Belongs to the tRNA-aminoacylation cofactor ARC1 family.</text>
+</comment>
+<dbReference type="EMBL" id="U31348">
+<property type="protein sequence ID" value="AAC49072.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X97644">
+<property type="protein sequence ID" value="CAA66247.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="Z72627">
+<property type="protein sequence ID" value="CAA96812.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="protein sequence ID" value="CAA64750.1"/>
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+<property type="protein sequence ID" value="AAS56824.1"/>
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+<property type="protein sequence ID" value="DAA08002.1"/>
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+<property type="entry name" value="S64113"/>
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+<dbReference type="RefSeq" id="NP_011410.1">
+<property type="nucleotide sequence ID" value="NM_001180970.1"/>
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+<dbReference type="PDB" id="2HQT">
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+<property type="resolution" value="1.90"/>
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+<property type="resolution" value="2.20"/>
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+<dbReference type="PDB" id="4R1J">
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+<dbReference type="PDBsum" id="2HQT"/>
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+<dbReference type="PDBsum" id="2HSM"/>
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+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1947">
+<property type="entry name" value="Methionyl glutamyl tRNA synthetase complex"/>
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+<dbReference type="DIP" id="DIP-2210N"/>
+<dbReference type="IntAct" id="P46672">
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+</dbReference>
+<dbReference type="MINT" id="P46672"/>
+<dbReference type="STRING" id="4932.YGL105W"/>
+<dbReference type="iPTMnet" id="P46672"/>
+<dbReference type="MaxQB" id="P46672"/>
+<dbReference type="PaxDb" id="P46672"/>
+<dbReference type="PRIDE" id="P46672"/>
+<dbReference type="TopDownProteomics" id="P46672"/>
+<dbReference type="EnsemblFungi" id="YGL105W_mRNA">
+<property type="protein sequence ID" value="YGL105W"/>
+<property type="gene ID" value="YGL105W"/>
+</dbReference>
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+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-407; SER-411; SER-491; SER-816; SER-1058 AND SER-1061</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text>Serine/threonine protein kinase involved in a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act on this kinase. BCK1 probably phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]</text>
+<dbReference type="Rhea" id="RHEA:17989"/>
+<dbReference type="Rhea" id="RHEA-COMP:9863"/>
+<dbReference type="Rhea" id="RHEA-COMP:11604"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:29999"/>
+<dbReference type="ChEBI" id="CHEBI:30616"/>
+<dbReference type="ChEBI" id="CHEBI:83421"/>
+<dbReference type="ChEBI" id="CHEBI:456216"/>
+<dbReference type="EC" id="2.7.11.1"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]</text>
+<dbReference type="Rhea" id="RHEA:46608"/>
+<dbReference type="Rhea" id="RHEA-COMP:11060"/>
+<dbReference type="Rhea" id="RHEA-COMP:11605"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:30013"/>
+<dbReference type="ChEBI" id="CHEBI:30616"/>
+<dbReference type="ChEBI" id="CHEBI:61977"/>
+<dbReference type="ChEBI" id="CHEBI:456216"/>
+<dbReference type="EC" id="2.7.11.1"/>
+</reaction>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-3470">
+<id>Q01389</id>
+</interactant>
+<interactant intactId="EBI-4192">
+<id>Q00684</id>
+<label>CDC14</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>4</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-3470">
+<id>Q01389</id>
+</interactant>
+<interactant intactId="EBI-11670">
+<id>P36006</id>
+<label>MYO3</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>6</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-3470">
+<id>Q01389</id>
+</interactant>
+<interactant intactId="EBI-11687">
+<id>Q04439</id>
+<label>MYO5</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>6</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="6">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 112 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the protein kinase superfamily. STE Ser/Thr protein kinase family. MAP kinase kinase kinase subfamily.</text>
+</comment>
+<comment type="sequence caution" evidence="6">
+<conflict type="erroneous initiation">
+<sequence resource="EMBL-CDS" id="AAA21179" version="1"/>
+</conflict>
+<text>Truncated N-terminus.</text>
+</comment>
+<comment type="sequence caution" evidence="6">
+<conflict type="frameshift">
+<sequence resource="EMBL-CDS" id="AAA21179" version="1"/>
+</conflict>
+</comment>
+<dbReference type="EC" id="2.7.11.1"/>
+<dbReference type="EMBL" id="M84389">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="D10389">
+<property type="protein sequence ID" value="BAA01226.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X60227">
+<property type="protein sequence ID" value="CAA42788.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X77923">
+<property type="protein sequence ID" value="CAA54896.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z49370">
+<property type="protein sequence ID" value="CAA89389.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z49369">
+<property type="protein sequence ID" value="CAA89388.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="M88604">
+<property type="protein sequence ID" value="AAA21179.1"/>
+<property type="status" value="ALT_SEQ"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006943">
+<property type="protein sequence ID" value="DAA08705.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S20117">
+<property type="entry name" value="S20117"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_012440.1">
+<property type="nucleotide sequence ID" value="NM_001181528.1"/>
+</dbReference>
+<dbReference type="SMR" id="Q01389"/>
+<dbReference type="BioGRID" id="33662">
+<property type="interactions" value="823"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-2223N"/>
+<dbReference type="IntAct" id="Q01389">
+<property type="interactions" value="56"/>
+</dbReference>
+<dbReference type="MINT" id="Q01389"/>
+<dbReference type="STRING" id="4932.YJL095W"/>
+<dbReference type="CarbonylDB" id="Q01389"/>
+<dbReference type="iPTMnet" id="Q01389"/>
+<dbReference type="MaxQB" id="Q01389"/>
+<dbReference type="PaxDb" id="Q01389"/>
+<dbReference type="PRIDE" id="Q01389"/>
+<dbReference type="EnsemblFungi" id="YJL095W_mRNA">
+<property type="protein sequence ID" value="YJL095W"/>
+<property type="gene ID" value="YJL095W"/>
+</dbReference>
+<dbReference type="GeneID" id="853350"/>
+<dbReference type="KEGG" id="sce:YJL095W"/>
+<dbReference type="SGD" id="S000003631">
+<property type="gene designation" value="BCK1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YJL095W"/>
+<dbReference type="eggNOG" id="KOG0198">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00980000202011"/>
+<dbReference type="HOGENOM" id="CLU_002516_0_0_1"/>
+<dbReference type="InParanoid" id="Q01389"/>
+<dbReference type="OMA" id="RFVRYAM"/>
+<dbReference type="Reactome" id="R-SCE-389357">
+<property type="pathway name" value="CD28 dependent PI3K/Akt signaling"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-5607761">
+<property type="pathway name" value="Dectin-1 mediated noncanonical NF-kB signaling"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-5668541">
+<property type="pathway name" value="TNFR2 non-canonical NF-kB pathway"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-5676590">
+<property type="pathway name" value="NIK-->noncanonical NF-kB signaling"/>
+</dbReference>
+<dbReference type="PRO" id="PR:Q01389"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome X"/>
+</dbReference>
+<dbReference type="RNAct" id="Q01389">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005935">
+<property type="term" value="C:cellular bud neck"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0043332">
+<property type="term" value="C:mating projection tip"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004709">
+<property type="term" value="F:MAP kinase kinase kinase activity"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004672">
+<property type="term" value="F:protein kinase activity"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0106310">
+<property type="term" value="F:protein serine kinase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0106311">
+<property type="term" value="F:protein threonine kinase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004713">
+<property type="term" value="F:protein tyrosine kinase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0030242">
+<property type="term" value="P:autophagy of peroxisome"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000196">
+<property type="term" value="P:cell wall integrity MAPK cascade"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0030968">
+<property type="term" value="P:endoplasmic reticulum unfolded protein response"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0030010">
+<property type="term" value="P:establishment of cell polarity"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0035556">
+<property type="term" value="P:intracellular signal transduction"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006468">
+<property type="term" value="P:protein phosphorylation"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0060237">
+<property type="term" value="P:regulation of fungal-type cell wall organization"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0010447">
+<property type="term" value="P:response to acidic pH"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0007584">
+<property type="term" value="P:response to nutrient"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR011009">
+<property type="entry name" value="Kinase-like_dom_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000719">
+<property type="entry name" value="Prot_kinase_dom"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR017441">
+<property type="entry name" value="Protein_kinase_ATP_BS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR008271">
+<property type="entry name" value="Ser/Thr_kinase_AS"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00069">
+<property type="entry name" value="Pkinase"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM00220">
+<property type="entry name" value="S_TKc"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56112">
+<property type="entry name" value="SSF56112"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00107">
+<property type="entry name" value="PROTEIN_KINASE_ATP"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50011">
+<property type="entry name" value="PROTEIN_KINASE_DOM"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00108">
+<property type="entry name" value="PROTEIN_KINASE_ST"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0418">Kinase</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0723">Serine/threonine-protein kinase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0829">Tyrosine-protein kinase</keyword>
+<feature type="chain" description="Serine/threonine-protein kinase BCK1/SLK1/SSP31" id="PRO_0000085662">
+<location>
+<begin position="1"/>
+<end position="1478"/>
+</location>
+</feature>
+<feature type="domain" description="Protein kinase" evidence="2">
+<location>
+<begin position="1175"/>
+<end position="1440"/>
+</location>
+</feature>
+<feature type="nucleotide phosphate-binding region" description="ATP" evidence="2">
+<location>
+<begin position="1181"/>
+<end position="1189"/>
+</location>
+</feature>
+<feature type="active site" description="Proton acceptor" evidence="2 3">
+<location>
+<position position="1303"/>
+</location>
+</feature>
+<feature type="binding site" description="ATP" evidence="2">
+<location>
+<position position="1204"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphothreonine" evidence="9">
+<location>
+<position position="407"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="9">
+<location>
+<position position="411"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="8 9">
+<location>
+<position position="491"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="7">
+<location>
+<position position="747"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="9">
+<location>
+<position position="816"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="7 9">
+<location>
+<position position="1058"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="9">
+<location>
+<position position="1061"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine; by PKC" evidence="1">
+<location>
+<position position="1134"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In BCK1-19; Dominant active." evidence="5">
+<original>T</original>
+<variation>P</variation>
+<location>
+<position position="1119"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In BCK1-11; Dominant active." evidence="5">
+<original>I</original>
+<variation>K</variation>
+<location>
+<position position="1120"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In BCK1-16; Dominant active." evidence="5">
+<original>I</original>
+<variation>T</variation>
+<location>
+<position position="1120"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In BCK1-10; Dominant active." evidence="5">
+<original>G</original>
+<variation>V</variation>
+<location>
+<position position="1146"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In BCK1-20; Dominant active." evidence="5">
+<original>A</original>
+<variation>P</variation>
+<location>
+<position position="1174"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>F</original>
+<variation>I</variation>
+<location>
+<position position="59"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 2; BAA01226." ref="2" evidence="6">
+<original>E</original>
+<variation>V</variation>
+<location>
+<position position="79"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>A</original>
+<variation>P</variation>
+<location>
+<position position="264"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>N</original>
+<variation>I</variation>
+<location>
+<position position="279"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>RYPQTPSYYYDR</original>
+<variation>STPKPRVITMTE</variation>
+<location>
+<begin position="703"/>
+<end position="714"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>S</original>
+<variation>A</variation>
+<location>
+<position position="795"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>L</original>
+<variation>V</variation>
+<location>
+<position position="802"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>A</original>
+<variation>S</variation>
+<location>
+<position position="808"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>T</original>
+<variation>N</variation>
+<location>
+<position position="903"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; CAA42788." ref="3" evidence="6">
+<original>T</original>
+<variation>N</variation>
+<location>
+<position position="919"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 7; AAA21179." ref="7" evidence="6">
+<original>A</original>
+<variation>R</variation>
+<location>
+<position position="960"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 7; AAA21179." ref="7" evidence="6">
+<original>A</original>
+<variation>R</variation>
+<location>
+<position position="962"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000255"/>
+<evidence key="2" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00159"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10027"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="1729597"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000305"/>
+<evidence key="7" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="17330950"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="18407956"/>
+</source>
+</evidence>
+<evidence key="9" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="19779198"/>
+</source>
+</evidence>
+<sequence length="1478" mass="164195" checksum="D586C3A497A5BB33" modified="1993-10-01" version="1">MPFLRKIAGTAHTHSRSDSNSSVKFGHQPTSSVASTKSSSKSPRATSRKSIYDDIRSQFPNLTPNSTSSQFYESTPVIEQSFNWTTDDHISAGTLENPTSFTNSSYKNDNGPSSLSDSRKSSGGNSVNSLSFDKLILSWDPTDPDEWTMHRVTSWFKFHDFPESWILFFKKHQLFGHRFIKLLAYDNFAVYEKYLPQTKTASYTRFQQLLKKTMTKNVTNSHIRQKSASKLKSSRSSSESIKSKLKNSKSQEDISNSRSTSESALSPTKSGPSKTDEKNFLHSTSTHQKTKSASSLYRRSFISLRGSSSSNASSAKSPSNIKLSIPARPHSIIESNSTLTKSASPPASPSYPSIFRRHHKSSSSESSLLNSLFGSGIGEEAPTKPNPQGHSLSSENLAKGKSKHYETNVSSPLKQSSLPTSDDKGNLWNKFKRKSQIGVPSPNTVAYVTSQETPSLKSNSSTATLTVQTADVNIPSPSSSPPPIPKTANRSLEVISTEDTPKISSTTASFKETYPDCINPDKTVPVPVNNQKYSVKNFLLDQKFYPLKKTGLNDSENKYILVTKDNVSFVPLNLKSVAKLSSFKESALTKLGINHKNVTFHMTDFDCDIGAAIPDDTLEFLKKSLFLNTSGKIYIKDQMKLQQKPKPAPLTSENNVPLKSVKSKSSMRSGTSSLIASTDDVSIVTSSSDITSFDEHASGSGRRYPQTPSYYYDRVSNTNPTEELNYWNIKEVLSHEENAPKMVFKTSPKLELNLPDKGSKLNIPTPITENESKSSFQVLRKDEGTEIDFNHRRESPYTKPELAPKREAPKPPANTSPQRTLSTSKQNKPIRLVRASTKISRSKRSKPLPPQLLSSPIEASSSSPDSLTSSYTPASTHVLIPQPYKGANDVMRRLKTDQDSTSTSPSLKMKQKVNRSNSTVSTSNSIFYSPSPLLKRGNSKRVVSSTSAADIFEENDITFADAPPMFDSDDSDDDSSSSDDIIWSKKKTAPETNNENKKDEKSDNSSTHSDEIFYDSQTQDKMERKMTFRPSPEVVYQNLEKFFPRANLDKPITEGIASPTSPKSLDSLLSPKNVASSRTEPSTPSRPVPPDSSYEFIQDGLNGKNKPLNQAKTPKRTKTIRTIAHEASLARKNSVKLKRQNTKMWGTRMVEVTENHMVSINKAKNSKGEYKEFAWMKGEMIGKGSFGAVYLCLNVTTGEMMAVKQVEVPKYSSQNEAILSTVEALRSEVSTLKDLDHLNIVQYLGFENKNNIYSLFLEYVAGGSVGSLIRMYGRFDEPLIKHLTTQVLKGLAYLHSKGILHRDMKADNLLLDQDGICKISDFGISRKSKDIYSNSDMTMRGTVFWMAPEMVDTKQGYSAKVDIWSLGCIVLEMFAGKRPWSNLEVVAAMFKIGKSKSAPPIPEDTLPLISQIGRNFLDACFEINPEKRPTANELLSHPFSEVNETFNFKSTRLAKFIKSNDKLNSSKLRITSQENKTE</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1988-04-01" modified="2021-04-07" version="215">
+<accession>P07267</accession>
+<accession>D6W3L4</accession>
+<name>CARP_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Saccharopepsin</fullName>
+<ecNumber>3.4.23.25</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Aspartate protease</fullName>
+<shortName>PrA</shortName>
+<shortName>Proteinase A</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>Carboxypeptidase Y-deficient protein 4</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Proteinase YSCA</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">PEP4</name>
+<name type="synonym">PHO9</name>
+<name type="synonym">PRA1</name>
+<name type="ordered locus">YPL154C</name>
+<name type="ORF">P2585</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1986" name="Mol. Cell. Biol." volume="6" first="2500" last="2510">
+<title>The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases.</title>
+<authorList>
+<person name="Woolford C.A."/>
+<person name="Daniels L.B."/>
+<person name="Park F.J."/>
+<person name="Jones E.W."/>
+<person name="van Arsdell J.N."/>
+<person name="Innis M.A."/>
+</authorList>
+<dbReference type="PubMed" id="3537721"/>
+<dbReference type="DOI" id="10.1128/mcb.6.7.2500"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1986" name="Mol. Cell. Biol." volume="6" first="2490" last="2499">
+<title>PEP4 gene of Saccharomyces cerevisiae encodes proteinase A, a vacuolar enzyme required for processing of vacuolar precursors.</title>
+<authorList>
+<person name="Ammerer G."/>
+<person name="Hunter C.P."/>
+<person name="Rothman J.H."/>
+<person name="Saari G.C."/>
+<person name="Valls L.A."/>
+<person name="Stevens T.H."/>
+</authorList>
+<dbReference type="PubMed" id="3023936"/>
+<dbReference type="DOI" id="10.1128/mcb.6.7.2490"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1996" name="Yeast" volume="12" first="1483" last="1492">
+<title>The sequence of 55 kb on the left arm of yeast chromosome XVI identifies a small nuclear RNA, a new putative protein kinase and two new putative regulators.</title>
+<authorList>
+<person name="Purnelle B."/>
+<person name="Coster F."/>
+<person name="Goffeau A."/>
+</authorList>
+<dbReference type="PubMed" id="8948103"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199611)12:14&lt;1483::aid-yea34>3.0.co;2-o"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204511 / S288c / AB972</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
+<person name="Albermann K."/>
+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
+<person name="Brueckner M."/>
+<person name="Carpenter J."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Churcher C.M."/>
+<person name="Coster F."/>
+<person name="Davis K."/>
+<person name="Davis R.W."/>
+<person name="Dietrich F.S."/>
+<person name="Delius H."/>
+<person name="DiPaolo T."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Duncan M."/>
+<person name="Floeth M."/>
+<person name="Fortin N."/>
+<person name="Friesen J.D."/>
+<person name="Fritz C."/>
+<person name="Goffeau A."/>
+<person name="Hall J."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Hilbert H."/>
+<person name="Hillier L.W."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Johnston M."/>
+<person name="Kalman S."/>
+<person name="Kleine K."/>
+<person name="Komp C."/>
+<person name="Kurdi O."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin A."/>
+<person name="Lin D."/>
+<person name="Louis E.J."/>
+<person name="Marathe R."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
+<person name="Nentwich U."/>
+<person name="Oefner P."/>
+<person name="Pearson D."/>
+<person name="Petel F.X."/>
+<person name="Pohl T.M."/>
+<person name="Purnelle B."/>
+<person name="Rajandream M.A."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Roberts D."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
+<person name="Ushinsky S."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Voss H."/>
+<person name="Walsh S.V."/>
+<person name="Wambutt R."/>
+<person name="Wang Y."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Winnett E."/>
+<person name="Zhong W.-W."/>
+<person name="Zollner A."/>
+<person name="Vo D.H."/>
+<person name="Hani J."/>
+</authorList>
+<dbReference type="PubMed" id="9169875"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1986" name="Carlsberg Res. Commun." volume="51" first="27" last="41">
+<title>Primary structure of the aspartic proteinase A from Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Dreyer T."/>
+<person name="Halkier B."/>
+<person name="Svendsen I."/>
+<person name="Ottesen M."/>
+</authorList>
+</citation>
+<scope>PROTEIN SEQUENCE OF 77-405</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="1992" name="J. Cell Biol." volume="118" first="95" last="108">
+<title>Kinesin-related proteins required for assembly of the mitotic spindle.</title>
+<authorList>
+<person name="Roof D.M."/>
+<person name="Meluh P.B."/>
+<person name="Rose M.D."/>
+</authorList>
+<dbReference type="PubMed" id="1618910"/>
+<dbReference type="DOI" id="10.1083/jcb.118.1.95"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 373-405</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="8">
+<citation type="journal article" date="1996" name="Yeast" volume="12" first="823" last="832">
+<title>Vacuolar and extracellular maturation of Saccharomyces cerevisiae proteinase A.</title>
+<authorList>
+<person name="Wolff A.M."/>
+<person name="Dimn N."/>
+<person name="Petersen J.G.L."/>
+</authorList>
+<dbReference type="PubMed" id="8840499"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199607)12:9&lt;823::aid-yea975>3.0.co;2-j"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 23-31 AND 68-86</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="1991" name="FEBS Lett." volume="293" first="62" last="66">
+<title>Biogenesis of the yeast vacuole (lysosome). Active site mutation in the vacuolar aspartate proteinase yscA blocks maturation of vacuolar proteinases.</title>
+<authorList>
+<person name="Rupp S."/>
+<person name="Hirsch H.H."/>
+<person name="Wolf D.H."/>
+</authorList>
+<dbReference type="PubMed" id="1959673"/>
+<dbReference type="DOI" id="10.1016/0014-5793(91)81153-y"/>
+</citation>
+<scope>MUTAGENESIS OF ASP-294</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="1997" name="J. Mol. Biol." volume="267" first="899" last="915">
+<title>The three-dimensional structure at 2.4-A resolution of glycosylated proteinase A from the lysosome-like vacuole of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Aguilar C.F."/>
+<person name="Cronin N.B."/>
+<person name="Badasso M."/>
+<person name="Dreyer T."/>
+<person name="Newman M.P."/>
+<person name="Cooper J.B."/>
+<person name="Hoover D.J."/>
+<person name="Wood S.P."/>
+<person name="Johnson M.S."/>
+<person name="Blundell T.L."/>
+</authorList>
+<dbReference type="PubMed" id="9135120"/>
+<dbReference type="DOI" id="10.1006/jmbi.1996.0880"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS)</scope>
+</reference>
+<comment type="function">
+<text>Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.</text>
+<dbReference type="EC" id="3.4.23.25"/>
+</reaction>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Vacuole</location>
+</subcellularLocation>
+<text>Lysosome-like vacuoles.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the peptidase A1 family.</text>
+</comment>
+<dbReference type="EC" id="3.4.23.25"/>
+<dbReference type="EMBL" id="M13358">
+<property type="protein sequence ID" value="AAB63975.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X96770">
+<property type="protein sequence ID" value="CAA65567.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z73510">
+<property type="protein sequence ID" value="CAA97859.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z11963">
+<property type="protein sequence ID" value="CAA78020.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11280.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="A25379">
+<property type="entry name" value="A25379"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_015171.1">
+<property type="nucleotide sequence ID" value="NM_001183968.1"/>
+</dbReference>
+<dbReference type="PDB" id="1DP5">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.20"/>
+<property type="chains" value="A=77-405"/>
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+</dbReference>
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+<dbReference type="SGD" id="S000006075">
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+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YPL154C"/>
+<dbReference type="eggNOG" id="KOG1339">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
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+</dbReference>
+<dbReference type="Reactome" id="R-SCE-2132295">
+<property type="pathway name" value="MHC class II antigen presentation"/>
+</dbReference>
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+<property type="pathway name" value="Neutrophil degranulation"/>
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+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XVI"/>
+</dbReference>
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+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
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+<property type="project" value="CAFA"/>
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+<property type="project" value="CAFA"/>
+</dbReference>
+<dbReference type="GO" id="GO:0070492">
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="8199" last="8204">
+<title>A homologue of elongation factor 1 gamma regulates methionine sulfoxide reductase A gene expression in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hanbauer I."/>
+<person name="Boja E.S."/>
+<person name="Moskovitz J."/>
+</authorList>
+<dbReference type="PubMed" id="12824466"/>
+<dbReference type="DOI" id="10.1073/pnas.1432898100"/>
+</citation>
+<scope>FUNCTION IN TRANSCRIPTIONAL REGULATION</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-32</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="47190" last="47198">
+<title>The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Jeppesen M.G."/>
+<person name="Ortiz P.A."/>
+<person name="Shepard W."/>
+<person name="Kinzy T.G."/>
+<person name="Nyborg J."/>
+<person name="Andersen G.R."/>
+</authorList>
+<dbReference type="PubMed" id="12972429"/>
+<dbReference type="DOI" id="10.1074/jbc.m306630200"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 2-219</scope>
+<scope>INTERACTION WITH EFB1</scope>
+<scope>PUTATIVE STRUCTURE OF THE EEF1 COMPLEX</scope>
+</reference>
+<comment type="function">
+<text evidence="2">Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components. May be involved in transcriptional regulation of MXR1.</text>
+</comment>
+<comment type="pathway">
+<text>Protein biosynthesis; polypeptide chain elongation.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3">The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. The eEF1B subcomplex with the GEF activity is formed of eEF1Balpha and eEF1Bgamma. CAM1 interacts with EFB1. Component of a complex bound to MXR1 promoter region.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="domain">
+<text>Ths GST-like domain mediates the interaction to eEFB1 and may be responsible for dimerization of the eEF1 complex.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 60865 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text>There are 2 isoforms for eEF1Bgamma in yeast.</text>
+</comment>
+<dbReference type="EMBL" id="L01879">
+<property type="protein sequence ID" value="AAA16892.1"/>
+<property type="molecule type" value="Unassigned_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X67917">
+<property type="protein sequence ID" value="CAA48116.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="U44030">
+<property type="protein sequence ID" value="AAB68173.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11382.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S29345">
+<property type="entry name" value="S29345"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_015277.1">
+<property type="nucleotide sequence ID" value="NM_001183862.1"/>
+</dbReference>
+<dbReference type="PDB" id="1NHY">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="3.00"/>
+<property type="chains" value="A=1-219"/>
+</dbReference>
+<dbReference type="PDBsum" id="1NHY"/>
+<dbReference type="SMR" id="P29547"/>
+<dbReference type="BioGRID" id="36132">
+<property type="interactions" value="179"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-2854">
+<property type="entry name" value="Elongation Factor eEF1 complex, variant CAM1"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-6813N"/>
+<dbReference type="IntAct" id="P29547">
+<property type="interactions" value="12"/>
+</dbReference>
+<dbReference type="MINT" id="P29547"/>
+<dbReference type="STRING" id="4932.YPL048W"/>
+<dbReference type="CarbonylDB" id="P29547"/>
+<dbReference type="iPTMnet" id="P29547"/>
+<dbReference type="MaxQB" id="P29547"/>
+<dbReference type="PaxDb" id="P29547"/>
+<dbReference type="PRIDE" id="P29547"/>
+<dbReference type="EnsemblFungi" id="YPL048W_mRNA">
+<property type="protein sequence ID" value="YPL048W"/>
+<property type="gene ID" value="YPL048W"/>
+</dbReference>
+<dbReference type="GeneID" id="856059"/>
+<dbReference type="KEGG" id="sce:YPL048W"/>
+<dbReference type="SGD" id="S000005969">
+<property type="gene designation" value="CAM1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YPL048W"/>
+<dbReference type="eggNOG" id="KOG0867">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="eggNOG" id="KOG1627">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00940000176354"/>
+<dbReference type="HOGENOM" id="CLU_011226_3_0_1"/>
+<dbReference type="InParanoid" id="P29547"/>
+<dbReference type="OMA" id="QIDYEVY"/>
+<dbReference type="Reactome" id="R-SCE-156842">
+<property type="pathway name" value="Eukaryotic Translation Elongation"/>
+</dbReference>
+<dbReference type="UniPathway" id="UPA00345"/>
+<dbReference type="EvolutionaryTrace" id="P29547"/>
+<dbReference type="PRO" id="PR:P29547"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XVI"/>
+</dbReference>
+<dbReference type="RNAct" id="P29547">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0010494">
+<property type="term" value="C:cytoplasmic stress granule"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005509">
+<property type="term" value="F:calcium ion binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0001046">
+<property type="term" value="F:core promoter sequence-specific DNA binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003700">
+<property type="term" value="F:DNA-binding transcription factor activity"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005085">
+<property type="term" value="F:guanyl-nucleotide exchange factor activity"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005543">
+<property type="term" value="F:phospholipid binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003746">
+<property type="term" value="F:translation elongation factor activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006749">
+<property type="term" value="P:glutathione metabolic process"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="InterPro"/>
+</dbReference>
+<dbReference type="GO" id="GO:0045944">
+<property type="term" value="P:positive regulation of transcription by RNA polymerase II"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006449">
+<property type="term" value="P:regulation of translational termination"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006414">
+<property type="term" value="P:translational elongation"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.70.1010">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.40.30.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001662">
+<property type="entry name" value="EF1B_G_C"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036433">
+<property type="entry name" value="EF1B_G_C_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR010987">
+<property type="entry name" value="Glutathione-S-Trfase_C-like"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036282">
+<property type="entry name" value="Glutathione-S-Trfase_C_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR040079">
+<property type="entry name" value="Glutathione_S-Trfase"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR004045">
+<property type="entry name" value="Glutathione_S-Trfase_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR004046">
+<property type="entry name" value="GST_C"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036249">
+<property type="entry name" value="Thioredoxin-like_sf"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00647">
+<property type="entry name" value="EF1G"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00043">
+<property type="entry name" value="GST_C"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF02798">
+<property type="entry name" value="GST_N"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SFLD" id="SFLDS00019">
+<property type="entry name" value="Glutathione_Transferase_(cytos"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM01183">
+<property type="entry name" value="EF1G"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF47616">
+<property type="entry name" value="SSF47616"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF52833">
+<property type="entry name" value="SSF52833"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF89942">
+<property type="entry name" value="SSF89942"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50040">
+<property type="entry name" value="EF1G_C"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50405">
+<property type="entry name" value="GST_CTER"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50404">
+<property type="entry name" value="GST_NTER"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0251">Elongation factor</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0648">Protein biosynthesis</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<feature type="initiator methionine" description="Removed" evidence="8">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="Elongation factor 1-gamma 1" id="PRO_0000208831">
+<location>
+<begin position="2"/>
+<end position="415"/>
+</location>
+</feature>
+<feature type="domain" description="GST N-terminal">
+<location>
+<begin position="2"/>
+<end position="78"/>
+</location>
+</feature>
+<feature type="domain" description="GST C-terminal">
+<location>
+<begin position="89"/>
+<end position="215"/>
+</location>
+</feature>
+<feature type="domain" description="EF-1-gamma C-terminal" evidence="1">
+<location>
+<begin position="254"/>
+<end position="415"/>
+</location>
+</feature>
+<feature type="modified residue" description="N-acetylserine" evidence="8">
+<location>
+<position position="2"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphothreonine" evidence="7">
+<location>
+<position position="32"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 1; AAA16892." ref="1" evidence="5">
+<original>W</original>
+<variation>C</variation>
+<location>
+<position position="191"/>
+</location>
+</feature>
+<feature type="strand" evidence="6">
+<location>
+<begin position="5"/>
+<end position="7"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="12"/>
+<end position="24"/>
+</location>
+</feature>
+<feature type="strand" evidence="6">
+<location>
+<begin position="29"/>
+<end position="31"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="33"/>
+<end position="35"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="37"/>
+<end position="43"/>
+</location>
+</feature>
+<feature type="strand" evidence="6">
+<location>
+<begin position="49"/>
+<end position="53"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="55"/>
+<end position="57"/>
+</location>
+</feature>
+<feature type="strand" evidence="6">
+<location>
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+<end position="62"/>
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+</feature>
+<feature type="helix" evidence="6">
+<location>
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+<end position="73"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="77"/>
+<end position="83"/>
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+</feature>
+<feature type="helix" evidence="6">
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+<begin position="90"/>
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+</feature>
+<feature type="turn" evidence="6">
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+<begin position="105"/>
+<end position="108"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="109"/>
+<end position="113"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="115"/>
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+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="126"/>
+<end position="147"/>
+</location>
+</feature>
+<feature type="strand" evidence="6">
+<location>
+<begin position="151"/>
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+</feature>
+<feature type="helix" evidence="6">
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+<begin position="160"/>
+<end position="175"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
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+</location>
+</feature>
+<feature type="helix" evidence="6">
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+</location>
+</feature>
+<feature type="turn" evidence="6">
+<location>
+<begin position="199"/>
+<end position="201"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="202"/>
+<end position="204"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00519"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="12824466"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="12972429"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000305"/>
+<evidence key="6" type="ECO:0007744">
+<source>
+<dbReference type="PDB" id="1NHY"/>
+</source>
+</evidence>
+<evidence key="7" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="18407956"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22814378"/>
+</source>
+</evidence>
+<sequence length="415" mass="47088" checksum="17BCE60FFB7B2890" modified="1996-10-01" version="2">MSQGTLYANFRIRTWVPRGLVKALKLDVKVVTPDAAAEQFARDFPLKKVPAFVGPKGYKLTEAMAINYYLVKLSQDDKMKTQLLGADDDLNAQAQIIRWQSLANSDLCIQIANTIVPLKGGAPYNKKSVDSAMDAVDKIVDIFENRLKNYTYLATENISLADLVAASIFTRYFESLFGTEWRAQHPAIVRWFNTVRASPFLKDEYKDFKFADKPLSPPQKKKEKKAPAAAPAASKKKEEAKPAATETETSSKKPKHPLELLGKSTFVLDDWKRKYSNEDTRPVALPWFWEHYNPEEYSLWKVTYKYNDELTLTFMSNNLVGGFFNRLSASTKYMFGCLVVYGENNNNGIVGAVMVRGQDYVPAFDVAPDWESYDYAKLDPTNDDDKEFINNMWAWDKPVSVNGEPKEIVDGKVLK</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1995-11-01" modified="2021-04-07" version="182">
+<accession>P43616</accession>
+<accession>D6VTS7</accession>
+<name>DUG1_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Cys-Gly metallodipeptidase DUG1</fullName>
+<ecNumber>3.4.13.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Deficient in utilization of glutathione protein 1</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>GSH degradosomal complex subunit DUG1</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">DUG1</name>
+<name type="ordered locus">YFR044C</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
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+<citation type="journal article" date="1995" name="Nat. Genet." volume="10" first="261" last="268">
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+<authorList>
+<person name="Murakami Y."/>
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+<dbReference type="PubMed" id="7670463"/>
+<dbReference type="DOI" id="10.1038/ng0795-261"/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
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+<authorList>
+<person name="Engel S.R."/>
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+</authorList>
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+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1996" name="Yeast" volume="12" first="149" last="167">
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+<authorList>
+<person name="Eki T."/>
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+</authorList>
+<dbReference type="PubMed" id="8686379"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199602)12:2&lt;149::aid-yea893>3.0.co;2-g"/>
+</citation>
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+<strain>ATCC 204511 / S288c / AB972</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
+<person name="Rolfs A."/>
+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
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+<person name="LaBaer J."/>
+</authorList>
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+<dbReference type="DOI" id="10.1101/gr.6037607"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1996" name="Proc. Natl. Acad. Sci. U.S.A." volume="93" first="14440" last="14445">
+<title>Linking genome and proteome by mass spectrometry: large-scale identification of yeast proteins from two dimensional gels.</title>
+<authorList>
+<person name="Shevchenko A."/>
+<person name="Jensen O.N."/>
+<person name="Podtelejnikov A.V."/>
+<person name="Sagliocco F."/>
+<person name="Wilm M."/>
+<person name="Vorm O."/>
+<person name="Mortensen P."/>
+<person name="Shevchenko A."/>
+<person name="Boucherie H."/>
+<person name="Mann M."/>
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+<dbReference type="PubMed" id="8962070"/>
+<dbReference type="DOI" id="10.1073/pnas.93.25.14440"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
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+<dbReference type="DOI" id="10.1038/nature02046"/>
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+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2006" name="J. Proteome Res." volume="5" first="1543" last="1554">
+<title>Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.</title>
+<authorList>
+<person name="Reinders J."/>
+<person name="Zahedi R.P."/>
+<person name="Pfanner N."/>
+<person name="Meisinger C."/>
+<person name="Sickmann A."/>
+</authorList>
+<dbReference type="PubMed" id="16823961"/>
+<dbReference type="DOI" id="10.1021/pr050477f"/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2007" name="Genetics" volume="175" first="1137" last="1151">
+<title>The alternative pathway of glutathione degradation is mediated by a novel protein complex involving three new genes in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Ganguli D."/>
+<person name="Kumar C."/>
+<person name="Bachhawat A.K."/>
+</authorList>
+<dbReference type="PubMed" id="17179087"/>
+<dbReference type="DOI" id="10.1534/genetics.106.066944"/>
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+<scope>FUNCTION</scope>
+<scope>IDENTIFICATION IN THE GSH DEGRADOSOMAL COMPLEX</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-451</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2009" name="J. Biol. Chem." volume="284" first="14493" last="14502">
+<title>Dug1p Is a Cys-Gly peptidase of the gamma-glutamyl cycle of Saccharomyces cerevisiae and represents a novel family of Cys-Gly peptidases.</title>
+<authorList>
+<person name="Kaur H."/>
+<person name="Kumar C."/>
+<person name="Junot C."/>
+<person name="Toledano M.B."/>
+<person name="Bachhawat A.K."/>
+</authorList>
+<dbReference type="PubMed" id="19346245"/>
+<dbReference type="DOI" id="10.1074/jbc.m808952200"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>FUNCTION</scope>
+<scope>COFACTOR</scope>
+<scope>DISRUPTION PHENOTYPE</scope>
+</reference>
+<comment type="function">
+<text evidence="5 6">Catalytic component of the GSH degradosomal complex involved in the degradation of glutathione (GSH) and other peptides containing a gamma-glu-X bond. Functions also in a DUG2-DUG3-independent manner as a dipeptidase with high specificity for Cys-Gly and no activity toward tri- or tetrapeptides.</text>
+</comment>
+<comment type="cofactor">
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+<cofactor evidence="6">
+<name>Mn(2+)</name>
+<dbReference type="ChEBI" id="CHEBI:29035"/>
+</cofactor>
+</comment>
+<comment type="biophysicochemical properties">
+<kinetics>
+<KM>0.4 mM for Cys-Gly (at pH 8.0 and in the presence of 20 uM manganese ions)</KM>
+<KM>0.8 mM for Cys-Gly (at pH 8.0 and in the presence of 200 uM zinc ions)</KM>
+</kinetics>
+</comment>
+<comment type="subunit">
+<text evidence="5 6">Homodimer. Component of the GSH degradosomal complex composed of at least DUG1, DUG2 and DUG3.</text>
+</comment>
+<comment type="interaction">
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+<interactant intactId="EBI-5137">
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+<experiments>2</experiments>
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+</subcellularLocation>
+<subcellularLocation>
+<location evidence="4">Mitochondrion</location>
+</subcellularLocation>
+</comment>
+<comment type="disruption phenotype">
+<text evidence="6">Accumulation of Cys-Gly dipeptide and enhanced GSH toxicity.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 22300 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="7">Belongs to the peptidase M20A family.</text>
+</comment>
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+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0862">Zinc</keyword>
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+<title>Two-dimensional electrophoretic separation of yeast proteins using a non-linear wide range (pH 3-10) immobilized pH gradient in the first dimension; reproducibility and evidence for isoelectric focusing of alkaline (pI > 7) proteins.</title>
+<authorList>
+<person name="Norbeck J."/>
+<person name="Blomberg A."/>
+</authorList>
+<dbReference type="PubMed" id="9509572"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199712)13:16&lt;1519::aid-yea211>3.0.co;2-u"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 56-61 AND 265-280</scope>
+<source>
+<strain>ATCC 44827 / SKQ2N</strain>
+</source>
+</reference>
+<reference key="14">
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+<authorList>
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+<person name="Buhler J.-M."/>
+<person name="Sentenac A."/>
+<person name="Fromageot P."/>
+</authorList>
+<dbReference type="PubMed" id="3882705"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 70-77 AND 80-87</scope>
+</reference>
+<reference key="15">
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+<title>Interaction of Rho1p target Bni1p with F-actin-binding elongation factor 1alpha: implication in Rho1p-regulated reorganization of the actin cytoskeleton in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Umikawa M."/>
+<person name="Tanaka K."/>
+<person name="Kamei T."/>
+<person name="Shimizu K."/>
+<person name="Imamura H."/>
+<person name="Sasaki T."/>
+<person name="Takai Y."/>
+</authorList>
+<dbReference type="PubMed" id="9591785"/>
+<dbReference type="DOI" id="10.1038/sj.onc.1201724"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 211-214 AND 289-308</scope>
+<scope>INTERACTION WITH BNI1</scope>
+<scope>IDENTIFICATION IN A COMPLEX WITH BNI1 AND PROFILIN</scope>
+</reference>
+<reference key="16">
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+<authorList>
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+<person name="Robnett C.J."/>
+</authorList>
+<dbReference type="PubMed" id="12748053"/>
+<dbReference type="DOI" id="10.1016/s1567-1356(03)00012-6"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 22-397</scope>
+<source>
+<strain>ATCC 13507 / CBS 459 / NRRL Y-12649</strain>
+<strain>ATCC 18824 / CBS 1171 / DSM 70449 / IFO 10217 / NRRL Y-12632</strain>
+<strain>ATCC 24702 / NRRL Y-2034</strain>
+<strain>Diastaticus / ATCC 13007 / CBS 1782 / IFO 1046 / NRRL Y-2416</strain>
+<strain>NRRL YB-210</strain>
+</source>
+</reference>
+<reference key="17">
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+<title>Mutations in elongation factor EF-1 alpha affect the frequency of frameshifting and amino acid misincorporation in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Sandbaken M.G."/>
+<person name="Culbertson M.R."/>
+</authorList>
+<dbReference type="PubMed" id="3066688"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>MUTAGENESIS OF GLU-286 AND GLU-317</scope>
+</reference>
+<reference key="18">
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+<title>Competition and cooperation amongst yeast elongation factors.</title>
+<authorList>
+<person name="Kovalchuke O."/>
+<person name="Kambampati R."/>
+<person name="Pladies E."/>
+<person name="Chakraburtty K."/>
+</authorList>
+<dbReference type="PubMed" id="9990316"/>
+<dbReference type="DOI" id="10.1046/j.1432-1327.1998.2580986.x"/>
+</citation>
+<scope>INTERACTION WITH YEF3</scope>
+<scope>MUTAGENESIS OF GLU-122</scope>
+</reference>
+<reference key="19">
+<citation type="journal article" date="1998" name="J. Biol. Chem." volume="273" first="28752" last="28758">
+<title>Site-directed mutagenesis of yeast eEF1A. Viable mutants with altered nucleotide specificity.</title>
+<authorList>
+<person name="Cavallius J."/>
+<person name="Merrick W.C."/>
+</authorList>
+<dbReference type="PubMed" id="9786872"/>
+<dbReference type="DOI" id="10.1074/jbc.273.44.28752"/>
+</citation>
+<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
+<scope>MUTAGENESIS OF ASN-153 AND ASP-156</scope>
+</reference>
+<reference key="20">
+<citation type="journal article" date="1998" name="J. Cell Biol." volume="143" first="1471" last="1484">
+<title>Interaction of ZPR1 with translation elongation factor-1alpha in proliferating cells.</title>
+<authorList>
+<person name="Gangwani L."/>
+<person name="Mikrut M."/>
+<person name="Galcheva-Gargova Z."/>
+<person name="Davis R.J."/>
+</authorList>
+<dbReference type="PubMed" id="9852145"/>
+<dbReference type="DOI" id="10.1083/jcb.143.6.1471"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+<scope>INTERACTION WITH ZPR1</scope>
+</reference>
+<reference key="21">
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+<title>Mutations in a GTP-binding motif of eukaryotic elongation factor 1A reduce both translational fidelity and the requirement for nucleotide exchange.</title>
+<authorList>
+<person name="Carr-Schmid A."/>
+<person name="Durko N."/>
+<person name="Cavallius J."/>
+<person name="Merrick W.C."/>
+<person name="Kinzy T.G."/>
+</authorList>
+<dbReference type="PubMed" id="10514524"/>
+<dbReference type="DOI" id="10.1074/jbc.274.42.30297"/>
+</citation>
+<scope>MUTAGENESIS OF ASN-153 AND ASP-156</scope>
+</reference>
+<reference key="22">
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+<title>An aminoacylation-dependent nuclear tRNA export pathway in yeast.</title>
+<authorList>
+<person name="Grosshans H."/>
+<person name="Hurt E.C."/>
+<person name="Simos G."/>
+</authorList>
+<dbReference type="PubMed" id="10766739"/>
+</citation>
+<scope>FUNCTION IN NUCLEAR EXPORT OF AMINOACYL-TRNAS</scope>
+</reference>
+<reference key="23">
+<citation type="journal article" date="2000" name="J. Biol. Chem." volume="275" first="37150" last="37158">
+<title>A novel post-translational modification of yeast elongation factor 1A. Methylesterification at the C-terminus.</title>
+<authorList>
+<person name="Zobel-Thropp P."/>
+<person name="Yang M.C."/>
+<person name="Machado L."/>
+<person name="Clarke S."/>
+</authorList>
+<dbReference type="PubMed" id="10973948"/>
+<dbReference type="DOI" id="10.1074/jbc.m001005200"/>
+</citation>
+<scope>METHYLATION AT LYS-458</scope>
+</reference>
+<reference key="24">
+<citation type="journal article" date="2001" name="Genetics" volume="157" first="1425" last="1436">
+<title>Overexpression of translation elongation factor 1A affects the organization and function of the actin cytoskeleton in yeast.</title>
+<authorList>
+<person name="Munshi R."/>
+<person name="Kandl K.A."/>
+<person name="Carr-Schmid A."/>
+<person name="Whitacre J.L."/>
+<person name="Adams A.E.M."/>
+<person name="Kinzy T.G."/>
+</authorList>
+<dbReference type="PubMed" id="11290701"/>
+</citation>
+<scope>INTERACTION WITH ACTIN</scope>
+</reference>
+<reference key="25">
+<citation type="journal article" date="2003" name="Biochem. J." volume="374" first="513" last="519">
+<title>Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Shenton D."/>
+<person name="Grant C.M."/>
+</authorList>
+<dbReference type="PubMed" id="12755685"/>
+<dbReference type="DOI" id="10.1042/bj20030414"/>
+</citation>
+<scope>S-THIOLATION</scope>
+</reference>
+<reference key="26">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="27">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
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+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="28">
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+<title>Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A.</title>
+<authorList>
+<person name="Chuang S.-M."/>
+<person name="Chen L."/>
+<person name="Lambertson D."/>
+<person name="Anand M."/>
+<person name="Kinzy T.G."/>
+<person name="Madura K."/>
+</authorList>
+<dbReference type="PubMed" id="15601860"/>
+<dbReference type="DOI" id="10.1128/mcb.25.1.403-413.2005"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>MUTAGENESIS OF ASP-156</scope>
+<scope>INTERACTION WITH RPT1</scope>
+</reference>
+<reference key="29">
+<citation type="journal article" date="2007" name="EMBO J." volume="26" first="288" last="300">
+<title>Cex1p is a novel cytoplasmic component of the Saccharomyces cerevisiae nuclear tRNA export machinery.</title>
+<authorList>
+<person name="McGuire A.T."/>
+<person name="Mangroo D."/>
+</authorList>
+<dbReference type="PubMed" id="17203074"/>
+<dbReference type="DOI" id="10.1038/sj.emboj.7601493"/>
+</citation>
+<scope>INTERACTION WITH CEX1</scope>
+</reference>
+<reference key="30">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18; THR-72; THR-82; SER-163 AND THR-430</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="31">
+<citation type="journal article" date="2008" name="Mol. Cell. Biol." volume="28" first="1313" last="1325">
+<title>Phosphorylation by casein kinase 2 regulates Nap1 localization and function.</title>
+<authorList>
+<person name="Calvert M.E.K."/>
+<person name="Keck K.M."/>
+<person name="Ptak C."/>
+<person name="Shabanowitz J."/>
+<person name="Hunt D.F."/>
+<person name="Pemberton L.F."/>
+</authorList>
+<dbReference type="PubMed" id="18086883"/>
+<dbReference type="DOI" id="10.1128/mcb.01035-07"/>
+</citation>
+<scope>INTERACTION WITH NAP1</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="32">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-259 AND SER-414</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="33">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="34">
+<citation type="journal article" date="2010" name="Arch. Biochem. Biophys." volume="500" first="137" last="143">
+<title>Two novel methyltransferases acting upon eukaryotic elongation factor 1A in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Lipson R.S."/>
+<person name="Webb K.J."/>
+<person name="Clarke S.G."/>
+</authorList>
+<dbReference type="PubMed" id="20510667"/>
+<dbReference type="DOI" id="10.1016/j.abb.2010.05.023"/>
+</citation>
+<scope>METHYLATION</scope>
+</reference>
+<reference key="35">
+<citation type="journal article" date="2011" name="J. Biol. Chem." volume="286" first="36568" last="36579">
+<title>Evidence that eukaryotic translation elongation factor 1A (eEF1A) binds the Gcn2 protein C terminus and inhibits Gcn2 activity.</title>
+<authorList>
+<person name="Visweswaraiah J."/>
+<person name="Lageix S."/>
+<person name="Castilho B.A."/>
+<person name="Izotova L."/>
+<person name="Kinzy T.G."/>
+<person name="Hinnebusch A.G."/>
+<person name="Sattlegger E."/>
+</authorList>
+<dbReference type="PubMed" id="21849502"/>
+<dbReference type="DOI" id="10.1074/jbc.m111.248898"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH GCN2</scope>
+<scope>ASSOCIATION WITH RIBOSOMES</scope>
+</reference>
+<reference key="36">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-224; LYS-242; LYS-253; LYS-271; LYS-393 AND LYS-437</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="37">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="960" last="972">
+<title>Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases.</title>
+<authorList>
+<person name="Couttas T.A."/>
+<person name="Raftery M.J."/>
+<person name="Padula M.P."/>
+<person name="Herbert B.R."/>
+<person name="Wilkins M.R."/>
+</authorList>
+<dbReference type="PubMed" id="22522802"/>
+<dbReference type="DOI" id="10.1002/pmic.201100570"/>
+</citation>
+<scope>METHYLATION AT LYS-30 BY EFM1</scope>
+<scope>METHYLATION AT LYS-316 BY SEE1</scope>
+<scope>METHYLATION AT LYS-79 AND LYS-390</scope>
+</reference>
+<reference key="38">
+<citation type="journal article" date="2014" name="Biochem. Biophys. Res. Commun." volume="455" first="382" last="389">
+<title>A new type of protein lysine methyltransferase trimethylates Lys-79 of elongation factor 1A.</title>
+<authorList>
+<person name="Dzialo M.C."/>
+<person name="Travaglini K.J."/>
+<person name="Shen S."/>
+<person name="Loo J.A."/>
+<person name="Clarke S.G."/>
+</authorList>
+<dbReference type="PubMed" id="25446118"/>
+<dbReference type="DOI" id="10.1016/j.bbrc.2014.11.022"/>
+</citation>
+<scope>METHYLATION AT LYS-79 BY EFM5</scope>
+</reference>
+<reference key="39">
+<citation type="journal article" date="2014" name="J. Proteome Res." volume="13" first="1744" last="1756">
+<title>Stoichiometry of Saccharomyces cerevisiae lysine methylation: insights into non-histone protein lysine methyltransferase activity.</title>
+<authorList>
+<person name="Hart-Smith G."/>
+<person name="Chia S.Z."/>
+<person name="Low J.K."/>
+<person name="McKay M.J."/>
+<person name="Molloy M.P."/>
+<person name="Wilkins M.R."/>
+</authorList>
+<dbReference type="PubMed" id="24517342"/>
+<dbReference type="DOI" id="10.1021/pr401251k"/>
+</citation>
+<scope>METHYLATION AT LYS-30; LYS-79 AND LYS-390</scope>
+<scope>METHYLATION AT LYS-316 BY SEE1</scope>
+</reference>
+<reference key="40">
+<citation type="journal article" date="2015" name="PLoS ONE" volume="10" first="E0131426" last="E0131426">
+<title>Saccharomyces cerevisiae eukaryotic elongation factor 1A (eEF1A) is methylated at Lys-390 by a METTL21-like methyltransferase.</title>
+<authorList>
+<person name="Jakobsson M.E."/>
+<person name="Davydova E."/>
+<person name="Malecki J."/>
+<person name="Moen A."/>
+<person name="Falnes P.O."/>
+</authorList>
+<dbReference type="PubMed" id="26115316"/>
+<dbReference type="DOI" id="10.1371/journal.pone.0131426"/>
+</citation>
+<scope>METHYLATION AT LYS-390 BY EFM6</scope>
+</reference>
+<reference key="41">
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+<title>Novel N-terminal and lysine methyltransferases that target translation elongation factor 1A in yeast and human.</title>
+<authorList>
+<person name="Hamey J.J."/>
+<person name="Winter D.L."/>
+<person name="Yagoub D."/>
+<person name="Overall C.M."/>
+<person name="Hart-Smith G."/>
+<person name="Wilkins M.R."/>
+</authorList>
+<dbReference type="PubMed" id="26545399"/>
+<dbReference type="DOI" id="10.1074/mcp.m115.052449"/>
+</citation>
+<scope>METHYLATION AT GLY-2 AND LYS-3 BY NNT1</scope>
+</reference>
+<reference key="42">
+<citation type="journal article" date="2000" name="Mol. Cell" volume="6" first="1261" last="1266">
+<title>Structural basis for nucleotide exchange and competition with tRNA in the yeast elongation factor complex eEF1A:eEF1Balpha.</title>
+<authorList>
+<person name="Andersen G.R."/>
+<person name="Pedersen L."/>
+<person name="Valente L."/>
+<person name="Chatterjee I."/>
+<person name="Kinzy T.G."/>
+<person name="Kjeldgaard M."/>
+<person name="Nyborg J."/>
+</authorList>
+<dbReference type="PubMed" id="11106763"/>
+<dbReference type="DOI" id="10.1016/s1097-2765(00)00122-2"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (1.67 ANGSTROMS) IN COMPLEX WITH EFB1</scope>
+</reference>
+<reference key="43">
+<citation type="journal article" date="2001" name="Nat. Struct. Biol." volume="8" first="531" last="534">
+<title>Crystal structures of nucleotide exchange intermediates in the eEF1A-eEF1Balpha complex.</title>
+<authorList>
+<person name="Andersen G.R."/>
+<person name="Valente L."/>
+<person name="Pedersen L."/>
+<person name="Kinzy T.G."/>
+<person name="Nyborg J."/>
+</authorList>
+<dbReference type="PubMed" id="11373622"/>
+<dbReference type="DOI" id="10.1038/88598"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH EFB1</scope>
+</reference>
+<comment type="function">
+<text evidence="3 11 14 20">GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. Plays a role as a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells (PubMed:21849502).</text>
+</comment>
+<comment type="biophysicochemical properties">
+<kinetics>
+<KM evidence="24">0.14 mM for GTP</KM>
+</kinetics>
+</comment>
+<comment type="pathway">
+<text>Protein biosynthesis; polypeptide chain elongation.</text>
+</comment>
+<comment type="subunit">
+<text evidence="5 6 7 11 12 13 14 22 23 25 26">The eukaryotic elongation factor 1 complex (eEF1) is probably a heterohexamer. Two trimeric complexes, each composed of eEF1A (TEF1 or TEF2), eEF1Balpha (EFB1) and eEF1Bgamma (CAM1 or TEF4), are probably dimerized via the eF1Bgamma subunits. eEF1A interacts directly with eEF1Balpha. Interacts with elongation factor 3 (YEF3 or HEF3), BNI1, SRV2 and ZPR1. Binds to actin and forms a ternary complex with BNI1 and profilin. Interacts with the proteasome, probably via RPT1. Interacts with CEX1 and NAP1. Interacts with GCN2 (via C-terminus); this interaction is direct, occurs in amino acid-repleted cells, may be stabilzed in a ribosome-dependent manner, reduces GCN2-mediated eIF-2-alpha phosphorylation and is lost in amino acid-starved cells and by uncharged tRNAs (PubMed:21849502). Associates with ribosomes (PubMed:21849502).</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-6314">
+<id>P02994</id>
+</interactant>
+<interactant intactId="EBI-22787">
+<id>P43573</id>
+<label>BUD27</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-6314">
+<id>P02994</id>
+</interactant>
+<interactant intactId="EBI-6319">
+<id>P32471</id>
+<label>EFB1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-6314">
+<id>P02994</id>
+</interactant>
+<interactant intactId="EBI-28053">
+<id>Q05040</id>
+<label>FAR8</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-6314">
+<id>P02994</id>
+</interactant>
+<interactant intactId="EBI-4024">
+<id>P17555</id>
+<label>SRV2</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-6314">
+<id>P02994</id>
+</interactant>
+<interactant intactId="EBI-11566629">
+<id>Q62384</id>
+<label>Zpr1</label>
+</interactant>
+<organismsDiffer>true</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="9">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="9">Cytoplasm</location>
+<location evidence="9">Cytoskeleton</location>
+</subcellularLocation>
+</comment>
+<comment type="PTM">
+<text evidence="8">S-thiolated in response to oxidative stress, probably inhibiting the protein and causing a reduction in protein synthesis.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="10">Present with 827 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text>There are two genes for eEF1A in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="27">Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.</text>
+</comment>
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+<property type="protein sequence ID" value="CAA25356.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X01638">
+<property type="protein sequence ID" value="CAA25798.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="M10992">
+<property type="protein sequence ID" value="AAA34585.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="M15666">
+<property type="protein sequence ID" value="AAA34584.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="M15667">
+<property type="protein sequence ID" value="AAA34586.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X78993">
+<property type="protein sequence ID" value="CAA55620.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z35987">
+<property type="protein sequence ID" value="CAA85075.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="U51033">
+<property type="protein sequence ID" value="AAB68129.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY692927">
+<property type="protein sequence ID" value="AAT92946.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X73532">
+<property type="protein sequence ID" value="CAA51936.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AF402004">
+<property type="protein sequence ID" value="AAP86465.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY130810">
+<property type="protein sequence ID" value="AAM83111.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY130811">
+<property type="protein sequence ID" value="AAM83112.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY130812">
+<property type="protein sequence ID" value="AAM83113.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY130813">
+<property type="protein sequence ID" value="AAM83114.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006936">
+<property type="protein sequence ID" value="DAA07236.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11498.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="A03522">
+<property type="entry name" value="EFBY1A"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_009676.1">
+<property type="nucleotide sequence ID" value="NM_001178466.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_015405.1">
+<property type="nucleotide sequence ID" value="NM_001184177.1"/>
+</dbReference>
+<dbReference type="PDB" id="1F60">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="1.67"/>
+<property type="chains" value="A=1-458"/>
+</dbReference>
+<dbReference type="PDB" id="1G7C">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.05"/>
+<property type="chains" value="A=1-458"/>
+</dbReference>
+<dbReference type="PDB" id="1IJE">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.40"/>
+<property type="chains" value="A=1-458"/>
+</dbReference>
+<dbReference type="PDB" id="1IJF">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="3.00"/>
+<property type="chains" value="A=1-458"/>
+</dbReference>
+<dbReference type="PDB" id="2B7B">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.60"/>
+<property type="chains" value="A=1-458"/>
+</dbReference>
+<dbReference type="PDB" id="2B7C">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="1.80"/>
+<property type="chains" value="A=1-458"/>
+</dbReference>
+<dbReference type="PDB" id="5O8W">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="1.67"/>
+<property type="chains" value="A=1-458"/>
+</dbReference>
+<dbReference type="PDBsum" id="1F60"/>
+<dbReference type="PDBsum" id="1G7C"/>
+<dbReference type="PDBsum" id="1IJE"/>
+<dbReference type="PDBsum" id="1IJF"/>
+<dbReference type="PDBsum" id="2B7B"/>
+<dbReference type="PDBsum" id="2B7C"/>
+<dbReference type="PDBsum" id="5O8W"/>
+<dbReference type="SMR" id="P02994"/>
+<dbReference type="BioGRID" id="32820">
+<property type="interactions" value="348"/>
+</dbReference>
+<dbReference type="BioGRID" id="36251">
+<property type="interactions" value="233"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-2854">
+<property type="entry name" value="Elongation Factor eEF1 complex, variant CAM1"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-425">
+<property type="entry name" value="Elongation Factor eEF1 complex, variant TEF4"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-2250N"/>
+<dbReference type="IntAct" id="P02994">
+<property type="interactions" value="808"/>
+</dbReference>
+<dbReference type="MINT" id="P02994"/>
+<dbReference type="STRING" id="4932.YPR080W"/>
+<dbReference type="CarbonylDB" id="P02994"/>
+<dbReference type="iPTMnet" id="P02994"/>
+<dbReference type="MaxQB" id="P02994"/>
+<dbReference type="PaxDb" id="P02994"/>
+<dbReference type="PRIDE" id="P02994"/>
+<dbReference type="TopDownProteomics" id="P02994"/>
+<dbReference type="EnsemblFungi" id="YBR118W_mRNA">
+<property type="protein sequence ID" value="YBR118W"/>
+<property type="gene ID" value="YBR118W"/>
+</dbReference>
+<dbReference type="EnsemblFungi" id="YPR080W_mRNA">
+<property type="protein sequence ID" value="YPR080W"/>
+<property type="gene ID" value="YPR080W"/>
+</dbReference>
+<dbReference type="GeneID" id="852415"/>
+<dbReference type="GeneID" id="856195"/>
+<dbReference type="KEGG" id="sce:YBR118W"/>
+<dbReference type="KEGG" id="sce:YPR080W"/>
+<dbReference type="SGD" id="S000006284">
+<property type="gene designation" value="TEF1"/>
+</dbReference>
+<dbReference type="SGD" id="S000000322">
+<property type="gene designation" value="TEF2"/>
+</dbReference>
+<dbReference type="eggNOG" id="KOG0052">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00940000164334"/>
+<dbReference type="HOGENOM" id="CLU_007265_3_5_1"/>
+<dbReference type="InParanoid" id="P02994"/>
+<dbReference type="OMA" id="CKWSEDR"/>
+<dbReference type="BioCyc" id="YEAST:G3O-34224-MONOMER"/>
+<dbReference type="Reactome" id="R-SCE-156842">
+<property type="pathway name" value="Eukaryotic Translation Elongation"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-3371511">
+<property type="pathway name" value="HSF1 activation"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-6798695">
+<property type="pathway name" value="Neutrophil degranulation"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-8876725">
+<property type="pathway name" value="Protein methylation"/>
+</dbReference>
+<dbReference type="UniPathway" id="UPA00345"/>
+<dbReference type="EvolutionaryTrace" id="P02994"/>
+<dbReference type="PRO" id="PR:P02994"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome II"/>
+</dbReference>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XVI"/>
+</dbReference>
+<dbReference type="RNAct" id="P02994">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005856">
+<property type="term" value="C:cytoskeleton"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000329">
+<property type="term" value="C:fungal-type vacuole membrane"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005739">
+<property type="term" value="C:mitochondrion"/>
+<property type="evidence" value="ECO:0000353"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0051015">
+<property type="term" value="F:actin filament binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0019003">
+<property type="term" value="F:GDP binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005525">
+<property type="term" value="F:GTP binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003924">
+<property type="term" value="F:GTPase activity"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:1904408">
+<property type="term" value="F:melatonin binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0019901">
+<property type="term" value="F:protein kinase binding"/>
+<property type="evidence" value="ECO:0000353"/>
+<property type="project" value="UniProtKB"/>
+</dbReference>
+<dbReference type="GO" id="GO:0043022">
+<property type="term" value="F:ribosome binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="UniProtKB"/>
+</dbReference>
+<dbReference type="GO" id="GO:0031267">
+<property type="term" value="F:small GTPase binding"/>
+<property type="evidence" value="ECO:0000353"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003746">
+<property type="term" value="F:translation elongation factor activity"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0051017">
+<property type="term" value="P:actin filament bundle assembly"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0034198">
+<property type="term" value="P:cellular response to amino acid starvation"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="UniProtKB"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006469">
+<property type="term" value="P:negative regulation of protein kinase activity"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="UniProtKB"/>
+</dbReference>
+<dbReference type="GO" id="GO:0001933">
+<property type="term" value="P:negative regulation of protein phosphorylation"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="UniProtKB"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006412">
+<property type="term" value="P:translation"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006414">
+<property type="term" value="P:translational elongation"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006409">
+<property type="term" value="P:tRNA export from nucleus"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="HAMAP" id="MF_00118_A">
+<property type="entry name" value="EF_Tu_A"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR004161">
+<property type="entry name" value="EFTu-like_2"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR031157">
+<property type="entry name" value="G_TR_CS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR027417">
+<property type="entry name" value="P-loop_NTPase"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000795">
+<property type="entry name" value="T_Tr_GTP-bd_dom"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR009000">
+<property type="entry name" value="Transl_B-barrel_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR009001">
+<property type="entry name" value="Transl_elong_EF1A/Init_IF2_C"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR004539">
+<property type="entry name" value="Transl_elong_EF1A_euk/arc"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR004160">
+<property type="entry name" value="Transl_elong_EFTu/EF1A_C"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00009">
+<property type="entry name" value="GTP_EFTU"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF03144">
+<property type="entry name" value="GTP_EFTU_D2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF03143">
+<property type="entry name" value="GTP_EFTU_D3"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PRINTS" id="PR00315">
+<property type="entry name" value="ELONGATNFCT"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF50447">
+<property type="entry name" value="SSF50447"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF50465">
+<property type="entry name" value="SSF50465"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF52540">
+<property type="entry name" value="SSF52540"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="TIGRFAMs" id="TIGR00483">
+<property type="entry name" value="EF-1_alpha"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00301">
+<property type="entry name" value="G_TR_1"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS51722">
+<property type="entry name" value="G_TR_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0009">Actin-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0206">Cytoskeleton</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0251">Elongation factor</keyword>
+<keyword id="KW-0342">GTP-binding</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0488">Methylation</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0648">Protein biosynthesis</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="19">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="Elongation factor 1-alpha" id="PRO_0000090973">
+<location>
+<begin position="2"/>
+<end position="458"/>
+</location>
+</feature>
+<feature type="domain" description="tr-type G">
+<location>
+<begin position="5"/>
+<end position="240"/>
+</location>
+</feature>
+<feature type="nucleotide phosphate-binding region" description="GTP">
+<location>
+<begin position="14"/>
+<end position="21"/>
+</location>
+</feature>
+<feature type="nucleotide phosphate-binding region" description="GTP">
+<location>
+<begin position="91"/>
+<end position="95"/>
+</location>
+</feature>
+<feature type="nucleotide phosphate-binding region" description="GTP">
+<location>
+<begin position="153"/>
+<end position="156"/>
+</location>
+</feature>
+<feature type="region of interest" description="G1" evidence="1">
+<location>
+<begin position="14"/>
+<end position="21"/>
+</location>
+</feature>
+<feature type="region of interest" description="G2" evidence="1">
+<location>
+<begin position="70"/>
+<end position="74"/>
+</location>
+</feature>
+<feature type="region of interest" description="G3" evidence="1">
+<location>
+<begin position="91"/>
+<end position="94"/>
+</location>
+</feature>
+<feature type="region of interest" description="G4" evidence="1">
+<location>
+<begin position="153"/>
+<end position="156"/>
+</location>
+</feature>
+<feature type="region of interest" description="G5" evidence="1">
+<location>
+<begin position="192"/>
+<end position="194"/>
+</location>
+</feature>
+<feature type="site" description="Not modified">
+<location>
+<position position="298"/>
+</location>
+</feature>
+<feature type="site" description="Not modified">
+<location>
+<position position="372"/>
+</location>
+</feature>
+<feature type="modified residue" description="N,N,N-trimethylglycine; by EFM7" evidence="19">
+<location>
+<position position="2"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6,N6-dimethyllysine; by EFM7; alternate" evidence="19">
+<location>
+<position position="3"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-methyllysine; by EFM7; alternate" evidence="19">
+<location>
+<position position="3"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="30">
+<location>
+<position position="18"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-methyllysine; by EFM1" evidence="15 16 21">
+<location>
+<position position="30"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphothreonine" evidence="30">
+<location>
+<position position="72"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6,N6,N6-trimethyllysine; by EFM5" evidence="15 16 17 21">
+<location>
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+<title>Protein synthesis in yeast. Structural and functional analysis of the gene encoding elongation factor 3.</title>
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+<person name="Hillier L.W."/>
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+<person name="Albermann K."/>
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+<person name="Ansorge W."/>
+<person name="Benes V."/>
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+<person name="Dubois E."/>
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+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
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+<person name="Hilger F."/>
+<person name="Kleine K."/>
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+<person name="Pohl T.M."/>
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+<person name="Rechmann S."/>
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+<person name="Rinke M."/>
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+<person name="Schwager C."/>
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+<person name="Underwood A.P."/>
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+<person name="Vandenbol M."/>
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+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1999" name="Biosci. Biotechnol. Biochem." volume="63" first="769" last="772">
+<title>Detection and analysis of translation elongation factor 3 genes from various yeasts.</title>
+<authorList>
+<person name="Uritani M."/>
+<person name="Shoumura Y."/>
+<person name="Yamada S."/>
+</authorList>
+<dbReference type="PubMed" id="10361693"/>
+<dbReference type="DOI" id="10.1271/bbb.63.769"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 446-955</scope>
+<source>
+<strain>ATCC 208279 / BJ926</strain>
+</source>
+</reference>
+<reference key="7">
+<citation type="journal article" date="1994" name="Electrophoresis" volume="15" first="1466" last="1486">
+<title>Protein identifications for a Saccharomyces cerevisiae protein database.</title>
+<authorList>
+<person name="Garrels J.I."/>
+<person name="Futcher B."/>
+<person name="Kobayashi R."/>
+<person name="Latter G.I."/>
+<person name="Schwender B."/>
+<person name="Volpe T."/>
+<person name="Warner J.R."/>
+<person name="McLaughlin C.S."/>
+</authorList>
+<dbReference type="PubMed" id="7895733"/>
+<dbReference type="DOI" id="10.1002/elps.11501501210"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 959-967</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="8">
+<citation type="journal article" date="1981" name="J. Biol. Chem." volume="256" first="9999" last="10004">
+<title>Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Dasmahapatra B."/>
+<person name="Chakraburtty K."/>
+</authorList>
+<dbReference type="PubMed" id="6456269"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>CATALYTIC ACTIVITY</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="1995" name="J. Biol. Chem." volume="270" first="20473" last="20478">
+<title>The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor.</title>
+<authorList>
+<person name="Triana-Alonso F.J."/>
+<person name="Chakraburtty K."/>
+<person name="Nierhaus K.H."/>
+</authorList>
+<dbReference type="PubMed" id="7657623"/>
+<dbReference type="DOI" id="10.1074/jbc.270.35.20473"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>CATALYTIC ACTIVITY</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="1994" name="Eur. J. Biochem." volume="226" first="133" last="140">
+<title>Comparative analysis of ribosome-associated adenosinetriphosphatase (ATPase) from pig liver and the ATPase of elongation factor 3 from Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Kovalchuke O."/>
+<person name="Chakraburtty K."/>
+</authorList>
+<dbReference type="PubMed" id="7957240"/>
+<dbReference type="DOI" id="10.1111/j.1432-1033.1994.tb20034.x"/>
+</citation>
+<scope>CATALYTIC ACTIVITY</scope>
+<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
+<scope>ACTIVITY REGULATION</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="1997" name="Electrophoresis" volume="18" first="1347" last="1360">
+<title>Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins.</title>
+<authorList>
+<person name="Garrels J.I."/>
+<person name="McLaughlin C.S."/>
+<person name="Warner J.R."/>
+<person name="Futcher B."/>
+<person name="Latter G.I."/>
+<person name="Kobayashi R."/>
+<person name="Schwender B."/>
+<person name="Volpe T."/>
+<person name="Anderson D.S."/>
+<person name="Mesquita-Fuentes R."/>
+<person name="Payne W.E."/>
+</authorList>
+<dbReference type="PubMed" id="9298649"/>
+<dbReference type="DOI" id="10.1002/elps.1150180810"/>
+</citation>
+<scope>ACETYLATION AT SER-2</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="1998" name="Eur. J. Biochem." volume="258" first="986" last="993">
+<title>Competition and cooperation amongst yeast elongation factors.</title>
+<authorList>
+<person name="Kovalchuke O."/>
+<person name="Kambampati R."/>
+<person name="Pladies E."/>
+<person name="Chakraburtty K."/>
+</authorList>
+<dbReference type="PubMed" id="9990316"/>
+<dbReference type="DOI" id="10.1046/j.1432-1327.1998.2580986.x"/>
+</citation>
+<scope>INTERACTION WITH EEF1A</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="239" last="253">
+<title>Identification and kinetic analysis of a functional homolog of elongation factor 3, YEF3 in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Sarthy A.V."/>
+<person name="McGonigal T."/>
+<person name="Capobianco J.O."/>
+<person name="Schmidt M."/>
+<person name="Green S.R."/>
+<person name="Moehle C.M."/>
+<person name="Goldman R.C."/>
+</authorList>
+<dbReference type="PubMed" id="9544245"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199802)14:3&lt;239::aid-yea219>3.0.co;2-b"/>
+</citation>
+<scope>CHARACTERIZATION</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="1998" name="J. Biol. Chem." volume="273" first="10249" last="10252">
+<title>The N-terminus of eukaryotic translation elongation factor 3 interacts with 18 S rRNA and 80 S ribosomes.</title>
+<authorList>
+<person name="Gontarek R.R."/>
+<person name="Li H."/>
+<person name="Nurse K."/>
+<person name="Prescott C.D."/>
+</authorList>
+<dbReference type="PubMed" id="9553076"/>
+<dbReference type="DOI" id="10.1074/jbc.273.17.10249"/>
+</citation>
+<scope>INTERACTION WITH 18S RRNA</scope>
+</reference>
+<reference key="15">
+<citation type="journal article" date="1999" name="Mol. Cell. Biol." volume="19" first="7357" last="7368">
+<title>A sampling of the yeast proteome.</title>
+<authorList>
+<person name="Futcher B."/>
+<person name="Latter G.I."/>
+<person name="Monardo P."/>
+<person name="McLaughlin C.S."/>
+<person name="Garrels J.I."/>
+</authorList>
+<dbReference type="PubMed" id="10523624"/>
+<dbReference type="DOI" id="10.1128/mcb.19.11.7357"/>
+</citation>
+<scope>PHOSPHORYLATION</scope>
+</reference>
+<reference key="16">
+<citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="6985" last="6991">
+<title>Functional interactions between yeast translation eukaryotic elongation factor (eEF) 1A and eEF3.</title>
+<authorList>
+<person name="Anand M."/>
+<person name="Chakraburtty K."/>
+<person name="Marton M.J."/>
+<person name="Hinnebusch A.G."/>
+<person name="Kinzy T.G."/>
+</authorList>
+<dbReference type="PubMed" id="12493761"/>
+<dbReference type="DOI" id="10.1074/jbc.m209224200"/>
+</citation>
+<scope>MUTAGENESIS OF PHE-650</scope>
+<scope>INTERACTION WITH EEF1A</scope>
+</reference>
+<reference key="17">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="18">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="19">
+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
+<person name="Haas W."/>
+<person name="Villen J."/>
+<person name="Elias J.E."/>
+<person name="Gygi S.P."/>
+</authorList>
+<dbReference type="PubMed" id="17330950"/>
+<dbReference type="DOI" id="10.1021/pr060559j"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039 AND SER-1040</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ADR376</strain>
+</source>
+</reference>
+<reference key="20">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-972; SER-1039 AND SER-1040</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="21">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-642; THR-972; SER-974; SER-1039 AND SER-1040</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="22">
+<citation type="journal article" date="2012" name="J. Biol. Chem." volume="287" first="37757" last="37768">
+<title>Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation.</title>
+<authorList>
+<person name="Visweswaraiah J."/>
+<person name="Lee S.J."/>
+<person name="Hinnebusch A.G."/>
+<person name="Sattlegger E."/>
+</authorList>
+<dbReference type="PubMed" id="22888004"/>
+<dbReference type="DOI" id="10.1074/jbc.m112.368266"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>ASSOCIATION WITH RIBOSOMES</scope>
+<scope>DOMAIN</scope>
+</reference>
+<reference key="23">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="24">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-350 AND LYS-636</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="25">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="960" last="972">
+<title>Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases.</title>
+<authorList>
+<person name="Couttas T.A."/>
+<person name="Raftery M.J."/>
+<person name="Padula M.P."/>
+<person name="Herbert B.R."/>
+<person name="Wilkins M.R."/>
+</authorList>
+<dbReference type="PubMed" id="22522802"/>
+<dbReference type="DOI" id="10.1002/pmic.201100570"/>
+</citation>
+<scope>METHYLATION AT LYS-187; LYS-196 AND LYS-789</scope>
+</reference>
+<reference key="26">
+<citation type="journal article" date="2018" name="PLoS ONE" volume="13" first="e0190524" last="e0190524">
+<title>Demonstration of translation elongation factor 3 activity from a non-fungal species, Phytophthora infestans.</title>
+<authorList>
+<person name="Mateyak M.K."/>
+<person name="Pupek J.K."/>
+<person name="Garino A.E."/>
+<person name="Knapp M.C."/>
+<person name="Colmer S.F."/>
+<person name="Kinzy T.G."/>
+<person name="Dunaway S."/>
+</authorList>
+<dbReference type="PubMed" id="29300771"/>
+<dbReference type="DOI" id="10.1371/journal.pone.0190524"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>CATALYTIC ACTIVITY</scope>
+</reference>
+<reference key="27">
+<citation type="journal article" date="2020" name="Genes (Basel)" volume="11" first="E1432" last="E1432">
+<title>Eukaryotic Elongation Factor 3 Protects Saccharomyces cerevisiae Yeast from Oxidative Stress.</title>
+<authorList>
+<person name="Goscinska K."/>
+<person name="Shahmoradi Ghahe S."/>
+<person name="Domogala S."/>
+<person name="Topf U."/>
+</authorList>
+<dbReference type="PubMed" id="33260587"/>
+<dbReference type="DOI" id="10.3390/genes11121432"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<comment type="function">
+<text evidence="6 7 9 10">Ribosome-dependent ATPase that functions in cytoplasmic translation elongation (PubMed:7657623, PubMed:6456269, PubMed:29300771). Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (PubMed:7657623). Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied (PubMed:7657623). Plays a role as a negative regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved or repleted cells (PubMed:22888004).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="7 9 10 11">
+<text>ATP + H2O = ADP + H(+) + phosphate</text>
+<dbReference type="Rhea" id="RHEA:13065"/>
+<dbReference type="ChEBI" id="CHEBI:15377"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:30616"/>
+<dbReference type="ChEBI" id="CHEBI:43474"/>
+<dbReference type="ChEBI" id="CHEBI:456216"/>
+</reaction>
+</comment>
+<comment type="activity regulation">
+<text evidence="11">Inhibited by the translational inhibitors neomycin and alpha-sarcin, which suppress the ATPase activity.</text>
+</comment>
+<comment type="biophysicochemical properties">
+<kinetics>
+<KM evidence="11">0.126 mM for ATP</KM>
+<KM evidence="11">0.125 mM for GTP</KM>
+<Vmax evidence="11">15.2 umol/min/mg enzyme with ATP as substrate</Vmax>
+</kinetics>
+</comment>
+<comment type="pathway" evidence="15">
+<text>Protein biosynthesis; polypeptide chain elongation.</text>
+</comment>
+<comment type="subunit">
+<text evidence="2 6 13 14">Monomer. Interacts with elongation factor 1A (eEF1A). Interacts through its N-terminus with 18S rRNA. Associates with ribosomes (PubMed:22888004).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="3">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="induction">
+<text evidence="8">Increases in strong (1 mM) hydrogen peroxide stress, and decreases in milder (0.5 mM) hydrogen peroxide stress.</text>
+</comment>
+<comment type="domain">
+<text evidence="6">The heat repeats and the C-terminal domain are necessary for impairing GCN1 function on ribosomes, and hence preventing GCN2 kinase activity in amino acid-starved or repleted cells (PubMed:22888004).</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 870578 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="15">Belongs to the ABC transporter superfamily. ABCF family. EF3 subfamily.</text>
+</comment>
+<dbReference type="EC" id="3.6.4.-" evidence="7 9 10 11"/>
+<dbReference type="EMBL" id="J05197">
+<property type="protein sequence ID" value="AAA35232.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="protein sequence ID" value="AAA35233.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="U20865">
+<property type="protein sequence ID" value="AAB67391.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="AB018539">
+<property type="protein sequence ID" value="BAA33897.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09563.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S59395">
+<property type="entry name" value="DVBYE3"/>
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+<dbReference type="RefSeq" id="NP_013350.1">
+<property type="nucleotide sequence ID" value="NM_001182136.1"/>
+</dbReference>
+<dbReference type="PDB" id="2IW3">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.40"/>
+<property type="chains" value="A/B=2-981"/>
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+<dbReference type="PDB" id="2IWH">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="3.00"/>
+<property type="chains" value="A/B=2-981"/>
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+<dbReference type="PDB" id="2IX3">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.70"/>
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+<dbReference type="PDB" id="2IX8">
+<property type="method" value="EM"/>
+<property type="resolution" value="6.00"/>
+<property type="chains" value="A=2-977"/>
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+<dbReference type="PDBsum" id="2IW3"/>
+<dbReference type="PDBsum" id="2IWH"/>
+<dbReference type="PDBsum" id="2IX3"/>
+<dbReference type="PDBsum" id="2IX8"/>
+<dbReference type="SMR" id="P16521"/>
+<dbReference type="BioGRID" id="31517">
+<property type="interactions" value="172"/>
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+<dbReference type="DIP" id="DIP-2249N"/>
+<dbReference type="IntAct" id="P16521">
+<property type="interactions" value="83"/>
+</dbReference>
+<dbReference type="MINT" id="P16521"/>
+<dbReference type="STRING" id="4932.YLR249W"/>
+<dbReference type="CarbonylDB" id="P16521"/>
+<dbReference type="iPTMnet" id="P16521"/>
+<dbReference type="MaxQB" id="P16521"/>
+<dbReference type="PaxDb" id="P16521"/>
+<dbReference type="PRIDE" id="P16521"/>
+<dbReference type="EnsemblFungi" id="YLR249W_mRNA">
+<property type="protein sequence ID" value="YLR249W"/>
+<property type="gene ID" value="YLR249W"/>
+</dbReference>
+<dbReference type="GeneID" id="850951"/>
+<dbReference type="KEGG" id="sce:YLR249W"/>
+<dbReference type="SGD" id="S000004239">
+<property type="gene designation" value="YEF3"/>
+</dbReference>
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+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
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+<person name="Binkley G."/>
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+<person name="Wong E.D."/>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="93" last="98">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.</title>
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+<person name="Philippsen P."/>
+<person name="Kleine K."/>
+<person name="Poehlmann R."/>
+<person name="Duesterhoeft A."/>
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+<person name="Hegemann J.H."/>
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+<person name="Urrestarazu L.A."/>
+<person name="Aert R."/>
+<person name="Albermann K."/>
+<person name="Altmann R."/>
+<person name="Andre B."/>
+<person name="Baladron V."/>
+<person name="Ballesta J.P.G."/>
+<person name="Becam A.-M."/>
+<person name="Beinhauer J.D."/>
+<person name="Boskovic J."/>
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+<person name="Dubois E."/>
+<person name="Fiedler T.A."/>
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+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
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+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
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+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
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+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
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+<reference key="6">
+<citation type="journal article" date="2004" name="Proc. Natl. Acad. Sci. U.S.A." volume="101" first="13513" last="13518">
+<title>Regulation of chromosome stability by the histone H2A variant Htz1, the Swr1 chromatin remodeling complex, and the histone acetyltransferase NuA4.</title>
+<authorList>
+<person name="Krogan N.J."/>
+<person name="Baetz K."/>
+<person name="Keogh M.-C."/>
+<person name="Datta N."/>
+<person name="Sawa C."/>
+<person name="Kwok T.C.Y."/>
+<person name="Thompson N.J."/>
+<person name="Davey M.G."/>
+<person name="Pootoolal J."/>
+<person name="Hughes T.R."/>
+<person name="Emili A."/>
+<person name="Buratowski S."/>
+<person name="Hieter P."/>
+<person name="Greenblatt J.F."/>
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+<scope>IDENTIFICATION IN THE NUA4 COMPLEX</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
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+</citation>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<comment type="function">
+<text>Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histone H4 and H2A. The NuA4 complex is also involved in DNA repair.</text>
+</comment>
+<comment type="subunit">
+<text evidence="4">Component of the NuA4 histone acetyltransferase complex composed of at least ACT1, ARP4, YAF9, VID21, SWC4, EAF3, EAF5, EAF6, EAF7, EPL1, ESA1, TRA1 and YNG2.</text>
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+<subcellularLocation>
+<location evidence="2">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 300 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="5">Belongs to the EAF7 family.</text>
+</comment>
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+<title>The primary structure of a glyceraldehyde-3-phosphate dehydrogenase gene from Saccharomyces cerevisiae.</title>
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+<scope>CLEAVAGE OF INITIATOR METHIONINE</scope>
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+<scope>X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS)</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<comment type="catalytic activity">
+<reaction evidence="2">
+<text>D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH</text>
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+</comment>
+<comment type="pathway">
+<text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.</text>
+</comment>
+<comment type="subunit">
+<text evidence="7">Homotetramer.</text>
+</comment>
+<comment type="subcellular location">
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+<location evidence="3">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="6">Mitochondrion</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text>There are three genes for G3PDH in yeast.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="5">Present with 169000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="8">Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.</text>
+</comment>
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+<dbReference type="DOI" id="10.1002/yea.320070814"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1980" name="J. Biol. Chem." volume="255" first="2596" last="2605">
+<title>Structural comparison of two nontandemly repeated yeast glyceraldehyde-3-phosphate dehydrogenase genes.</title>
+<authorList>
+<person name="Holland J.P."/>
+<person name="Holland M.J."/>
+</authorList>
+<dbReference type="PubMed" id="6244283"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1996" name="EMBO J." volume="15" first="2031" last="2049">
+<title>Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.</title>
+<authorList>
+<person name="Galibert F."/>
+<person name="Alexandraki D."/>
+<person name="Baur A."/>
+<person name="Boles E."/>
+<person name="Chalwatzis N."/>
+<person name="Chuat J.-C."/>
+<person name="Coster F."/>
+<person name="Cziepluch C."/>
+<person name="de Haan M."/>
+<person name="Domdey H."/>
+<person name="Durand P."/>
+<person name="Entian K.-D."/>
+<person name="Gatius M."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="Hennemann A."/>
+<person name="Herbert C.J."/>
+<person name="Heumann K."/>
+<person name="Hilger F."/>
+<person name="Hollenberg C.P."/>
+<person name="Huang M.-E."/>
+<person name="Jacq C."/>
+<person name="Jauniaux J.-C."/>
+<person name="Katsoulou C."/>
+<person name="Kirchrath L."/>
+<person name="Kleine K."/>
+<person name="Kordes E."/>
+<person name="Koetter P."/>
+<person name="Liebl S."/>
+<person name="Louis E.J."/>
+<person name="Manus V."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Obermaier B."/>
+<person name="Perea J."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rasmussen S.W."/>
+<person name="Rose M."/>
+<person name="Rossau R."/>
+<person name="Schaaff-Gerstenschlaeger I."/>
+<person name="Smits P.H.M."/>
+<person name="Scarcez T."/>
+<person name="Soriano N."/>
+<person name="To Van D."/>
+<person name="Tzermia M."/>
+<person name="Van Broekhoven A."/>
+<person name="Vandenbol M."/>
+<person name="Wedler H."/>
+<person name="von Wettstein D."/>
+<person name="Wambutt R."/>
+<person name="Zagulski M."/>
+<person name="Zollner A."/>
+<person name="Karpfinger-Hartl L."/>
+</authorList>
+<dbReference type="PubMed" id="8641269"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1996.tb00557.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1995" name="Electrophoresis" volume="16" first="149" last="156">
+<title>Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides.</title>
+<authorList>
+<person name="Norbeck J."/>
+<person name="Blomberg A."/>
+</authorList>
+<dbReference type="PubMed" id="7737086"/>
+<dbReference type="DOI" id="10.1002/elps.1150160124"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 24-37; 72-77; 81-86; 199-213; 226-232 AND 322-331</scope>
+<source>
+<strain>ATCC 38531 / Y41</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="submission" date="1996-02" db="UniProtKB">
+<authorList>
+<person name="Frutiger S."/>
+<person name="Hughes G.J."/>
+<person name="Sanchez J.-C."/>
+<person name="Hochstrasser D.F."/>
+</authorList>
+</citation>
+<scope>PROTEIN SEQUENCE OF 2-13</scope>
+<source>
+<strain>ATCC 26786 / X2180-1A</strain>
+</source>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-63</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="catalytic activity">
+<reaction evidence="3">
+<text>D-glyceraldehyde 3-phosphate + NAD(+) + phosphate = (2R)-3-phospho-glyceroyl phosphate + H(+) + NADH</text>
+<dbReference type="Rhea" id="RHEA:10300"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
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+<dbReference type="ChEBI" id="CHEBI:57604"/>
+<dbReference type="ChEBI" id="CHEBI:57945"/>
+<dbReference type="ChEBI" id="CHEBI:59776"/>
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+</comment>
+<comment type="pathway">
+<text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 1/5.</text>
+</comment>
+<comment type="subunit">
+<text>Homotetramer.</text>
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+<interactant intactId="EBI-7212">
+<id>P00358</id>
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+<interactant intactId="EBI-7000452">
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+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text>There are three genes for G3PDH in yeast.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 121000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the glyceraldehyde-3-phosphate dehydrogenase family.</text>
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+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="5">
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+<feature type="region of interest" description="Glyceraldehyde 3-phosphate binding" evidence="1">
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+</feature>
+<feature type="active site" description="Nucleophile" evidence="3">
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+</feature>
+<feature type="binding site" description="NAD" evidence="1">
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+</feature>
+<feature type="binding site" description="NAD; via carbonyl oxygen" evidence="1">
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+</feature>
+<feature type="binding site" description="NAD" evidence="1">
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+<feature type="site" description="Activates thiol group during catalysis" evidence="1">
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+<feature type="modified residue" description="Phosphoserine" evidence="2">
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+<feature type="sequence conflict" description="In Ref. 5; AA sequence." ref="5" evidence="6">
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+<name>KPC1_YEAST</name>
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+<fullName>Protein kinase C-like 1</fullName>
+<shortName>PKC 1</shortName>
+<ecNumber>2.7.11.13</ecNumber>
+</recommendedName>
+</protein>
+<gene>
+<name type="primary">PKC1</name>
+<name type="synonym">HPO2</name>
+<name type="synonym">STT1</name>
+<name type="ordered locus">YBL105C</name>
+<name type="ORF">YBL0807</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1990" name="Cell" volume="62" first="213" last="224">
+<title>A candidate protein kinase C gene, PKC1, is required for the S. cerevisiae cell cycle.</title>
+<authorList>
+<person name="Levin D.E."/>
+<person name="Fields F.O."/>
+<person name="Kunisawa R."/>
+<person name="Bishop J.M."/>
+<person name="Thorner J."/>
+</authorList>
+<dbReference type="PubMed" id="2196995"/>
+<dbReference type="DOI" id="10.1016/0092-8674(90)90360-q"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [MRNA]</scope>
+<source>
+<strain>ATCC 204278 / EG123 / SM1058</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="1103" last="1112">
+<title>Sequence analysis of a 78.6 kb segment of the left end of Saccharomyces cerevisiae chromosome II.</title>
+<authorList>
+<person name="Obermaier B."/>
+<person name="Gassenhuber J."/>
+<person name="Piravandi E."/>
+<person name="Domdey H."/>
+</authorList>
+<dbReference type="PubMed" id="7502586"/>
+<dbReference type="DOI" id="10.1002/yea.320111112"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1994" name="EMBO J." volume="13" first="5795" last="5809">
+<title>Complete DNA sequence of yeast chromosome II.</title>
+<authorList>
+<person name="Feldmann H."/>
+<person name="Aigle M."/>
+<person name="Aljinovic G."/>
+<person name="Andre B."/>
+<person name="Baclet M.C."/>
+<person name="Barthe C."/>
+<person name="Baur A."/>
+<person name="Becam A.-M."/>
+<person name="Biteau N."/>
+<person name="Boles E."/>
+<person name="Brandt T."/>
+<person name="Brendel M."/>
+<person name="Brueckner M."/>
+<person name="Bussereau F."/>
+<person name="Christiansen C."/>
+<person name="Contreras R."/>
+<person name="Crouzet M."/>
+<person name="Cziepluch C."/>
+<person name="Demolis N."/>
+<person name="Delaveau T."/>
+<person name="Doignon F."/>
+<person name="Domdey H."/>
+<person name="Duesterhus S."/>
+<person name="Dubois E."/>
+<person name="Dujon B."/>
+<person name="El Bakkoury M."/>
+<person name="Entian K.-D."/>
+<person name="Feuermann M."/>
+<person name="Fiers W."/>
+<person name="Fobo G.M."/>
+<person name="Fritz C."/>
+<person name="Gassenhuber J."/>
+<person name="Glansdorff N."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="de Haan M."/>
+<person name="Hein C."/>
+<person name="Herbert C.J."/>
+<person name="Hollenberg C.P."/>
+<person name="Holmstroem K."/>
+<person name="Jacq C."/>
+<person name="Jacquet M."/>
+<person name="Jauniaux J.-C."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kallesoee T."/>
+<person name="Kiesau P."/>
+<person name="Kirchrath L."/>
+<person name="Koetter P."/>
+<person name="Korol S."/>
+<person name="Liebl S."/>
+<person name="Logghe M."/>
+<person name="Lohan A.J.E."/>
+<person name="Louis E.J."/>
+<person name="Li Z.Y."/>
+<person name="Maat M.J."/>
+<person name="Mallet L."/>
+<person name="Mannhaupt G."/>
+<person name="Messenguy F."/>
+<person name="Miosga T."/>
+<person name="Molemans F."/>
+<person name="Mueller S."/>
+<person name="Nasr F."/>
+<person name="Obermaier B."/>
+<person name="Perea J."/>
+<person name="Pierard A."/>
+<person name="Piravandi E."/>
+<person name="Pohl F.M."/>
+<person name="Pohl T.M."/>
+<person name="Potier S."/>
+<person name="Proft M."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rieger M."/>
+<person name="Rose M."/>
+<person name="Schaaff-Gerstenschlaeger I."/>
+<person name="Scherens B."/>
+<person name="Schwarzlose C."/>
+<person name="Skala J."/>
+<person name="Slonimski P.P."/>
+<person name="Smits P.H.M."/>
+<person name="Souciet J.-L."/>
+<person name="Steensma H.Y."/>
+<person name="Stucka R."/>
+<person name="Urrestarazu L.A."/>
+<person name="van der Aart Q.J.M."/>
+<person name="Van Dyck L."/>
+<person name="Vassarotti A."/>
+<person name="Vetter I."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Wagner G."/>
+<person name="de Wergifosse P."/>
+<person name="Wolfe K.H."/>
+<person name="Zagulski M."/>
+<person name="Zimmermann F.K."/>
+<person name="Mewes H.-W."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="7813418"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1994.tb06923.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<scope>SEQUENCE REVISION TO 81; 621 AND 789</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-226 AND SER-761</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="1997" name="Yeast" volume="13" first="305" last="312">
+<title>Saccharomyces cerevisiae cell lysis mutations cly5 and cly7 define temperature-sensitive alleles of PKC1, the gene encoding yeast protein kinase C.</title>
+<authorList>
+<person name="Baymiller J."/>
+<person name="McCullough J.E."/>
+</authorList>
+<dbReference type="PubMed" id="9133734"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19970330)13:4&lt;305::aid-yea91>3.0.co;2-f"/>
+</citation>
+<scope>VARIANTS CLY5 AND CLY7</scope>
+</reference>
+<comment type="function">
+<text>Required for cell growth and for the G2->M transition of the cell division cycle. Mediates a protein kinase cascade; it activates BCK1 which itself activates MKK1/MKK2.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]</text>
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+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-threonyl-[protein]</text>
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+<id>P06786</id>
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+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="similarity">
+<text evidence="7">Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. PKC subfamily.</text>
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+</entry>
+<entry dataset="Swiss-Prot" created="1997-11-01" modified="2021-04-07" version="180">
+<accession>Q12460</accession>
+<accession>D6VYK0</accession>
+<name>NOP56_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Nucleolar protein 56</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Ribosome biosynthesis protein SIK1</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Suppressor of I kappa b protein 1</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">NOP56</name>
+<name type="synonym">SIK1</name>
+<name type="ordered locus">YLR197W</name>
+<name type="ORF">L8167.9</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="Cell Growth Differ." volume="6" first="789" last="798">
+<title>Genetic analysis of growth inhibition by GAL4-L kappa B-alpha in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Morin P.J."/>
+<person name="Downs J.A."/>
+<person name="Snodgrass A.M."/>
+<person name="Gilmore T.D."/>
+</authorList>
+<dbReference type="PubMed" id="7547500"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>S288c / YPH1</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Louis E.J."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Scholler P."/>
+<person name="Schwager C."/>
+<person name="Schwarz S."/>
+<person name="Underwood A.P."/>
+<person name="Urrestarazu L.A."/>
+<person name="Vandenbol M."/>
+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
+<person name="Zollner A."/>
+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1997" name="Mol. Cell. Biol." volume="17" first="7088" last="7098">
+<title>Nucleolar KKE/D repeat proteins Nop56p and Nop58p interact with Nop1p and are required for ribosome biogenesis.</title>
+<authorList>
+<person name="Gautier T."/>
+<person name="Berges T."/>
+<person name="Tollervey D."/>
+<person name="Hurt E."/>
+</authorList>
+<dbReference type="PubMed" id="9372940"/>
+<dbReference type="DOI" id="10.1128/mcb.17.12.7088"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH NOP1 AND NOP58</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+<scope>MUTAGENESIS OF VAL-333; TYR-355 AND MET-385</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2002" name="Nature" volume="417" first="967" last="970">
+<title>A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis.</title>
+<authorList>
+<person name="Dragon F."/>
+<person name="Gallagher J.E.G."/>
+<person name="Compagnone-Post P.A."/>
+<person name="Mitchell B.M."/>
+<person name="Porwancher K.A."/>
+<person name="Wehner K.A."/>
+<person name="Wormsley S."/>
+<person name="Settlage R.E."/>
+<person name="Shabanowitz J."/>
+<person name="Osheim Y."/>
+<person name="Beyer A.L."/>
+<person name="Hunt D.F."/>
+<person name="Baserga S.J."/>
+</authorList>
+<dbReference type="PubMed" id="12068309"/>
+<dbReference type="DOI" id="10.1038/nature00769"/>
+</citation>
+<scope>IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="4">Required for 60S ribosomal subunit synthesis.</text>
+</comment>
+<comment type="subunit">
+<text evidence="2 4">Interacts with NOP1 and NOP58. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-17148">
+<id>Q12460</id>
+</interactant>
+<interactant intactId="EBI-6838">
+<id>P15646</id>
+<label>NOP1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>5</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-17148">
+<id>Q12460</id>
+</interactant>
+<interactant intactId="EBI-12032">
+<id>P39990</id>
+<label>SNU13</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>4</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="4">Nucleus</location>
+<location evidence="4">Nucleolus</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 13500 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="5">Belongs to the NOP5/NOP56 family.</text>
+</comment>
+<dbReference type="EMBL" id="U20237">
+<property type="protein sequence ID" value="AAC49066.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="U14913">
+<property type="protein sequence ID" value="AAB67431.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09516.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S48550">
+<property type="entry name" value="S48550"/>
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+<dbReference type="RefSeq" id="NP_013298.1">
+<property type="nucleotide sequence ID" value="NM_001182084.1"/>
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+<dbReference type="ComplexPortal" id="CPX-1604">
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+<dbReference type="GeneID" id="850894"/>
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+<dbReference type="GO" id="GO:0030686">
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+<dbReference type="GO" id="GO:0005730">
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+<dbReference type="GO" id="GO:0005654">
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+<dbReference type="GO" id="GO:0006364">
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+<dbReference type="Gene3D" id="1.10.246.90">
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+<dbReference type="Gene3D" id="1.10.287.660">
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+<dbReference type="InterPro" id="IPR029012">
+<property type="entry name" value="Helix_hairpin_bin_sf"/>
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+<dbReference type="InterPro" id="IPR012974">
+<property type="entry name" value="NOP5_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR042239">
+<property type="entry name" value="Nop_C"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR002687">
+<property type="entry name" value="Nop_dom"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036070">
+<property type="entry name" value="Nop_dom_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012976">
+<property type="entry name" value="NOSIC"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01798">
+<property type="entry name" value="Nop"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF08156">
+<property type="entry name" value="NOP5NT"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM00931">
+<property type="entry name" value="NOSIC"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF89124">
+<property type="entry name" value="SSF89124"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS51358">
+<property type="entry name" value="NOP"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0690">Ribosome biogenesis</keyword>
+<feature type="chain" description="Nucleolar protein 56" id="PRO_0000219030">
+<location>
+<begin position="1"/>
+<end position="504"/>
+</location>
+</feature>
+<feature type="domain" description="Nop" evidence="1">
+<location>
+<begin position="299"/>
+<end position="417"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Asp/Glu/Lys-rich">
+<location>
+<begin position="443"/>
+<end position="504"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="6">
+<location>
+<position position="321"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Reduced growth rate at all temperatures; when associated with R-385." evidence="4">
+<original>V</original>
+<variation>A</variation>
+<location>
+<position position="333"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="At 37 degrees, growth slows after 6 to 8 hours and cell division stops after 20 hours." evidence="4">
+<original>Y</original>
+<variation>C</variation>
+<location>
+<position position="355"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Reduced growth rate at all temperatures; when associated with A-333." evidence="4">
+<original>M</original>
+<variation>R</variation>
+<location>
+<position position="385"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00690"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="12068309"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="9372940"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000305"/>
+<evidence key="6" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="18407956"/>
+</source>
+</evidence>
+<sequence length="504" mass="56864" checksum="F8522A5870EF4842" modified="1996-11-01" version="1">MAPIEYLLFEEPTGYAVFKVKLQQDDIGSRLKEVQEQINDFGAFTKLIELVSFAPFKGAAEALENANDISEGLVSESLKAILDLNLPKASSKKKNITLAISDKNLGPSIKEEFPYVDCISNELAQDLIRGVRLHGEKLFKGLQSGDLERAQLGLGHAYSRAKVKFSVQKNDNHIIQAIALLDQLDKDINTFAMRVKEWYGWHFPELAKLVPDNYTFAKLVLFIKDKASLNDDSLHDLAALLNEDSGIAQRVIDNARISMGQDISETDMENVCVFAQRVASLADYRRQLYDYLCEKMHTVAPNLSELIGEVIGARLISHAGSLTNLSKQAASTVQILGAEKALFRALKTKGNTPKYGLIYHSGFISKASAKNKGRISRYLANKCSMASRIDNYSEEPSNVFGSVLKKQVEQRLEFYNTGKPTLKNELAIQEAMELYNKDKPAAEVEETKEKESSKKRKLEDDDEEKKEKKEKKSKKEKKEKKEKKDKKEKKDKKEKKDKKKKSKD</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2004-12-07" modified="2021-04-07" version="152">
+<accession>Q99207</accession>
+<accession>D6VRK0</accession>
+<name>NOP14_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Nucleolar complex protein 14</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>U three protein 2</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>U3 small nucleolar RNA-associated protein 2</fullName>
+<shortName>U3 snoRNA-associated protein 2</shortName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">NOP14</name>
+<name type="synonym">UTP2</name>
+<name type="ordered locus">YDL148C</name>
+<name type="ORF">D1566</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1996" name="Yeast" volume="12" first="1587" last="1592">
+<title>Analysis of a 23 kb region on the left arm of yeast chromosome IV.</title>
+<authorList>
+<person name="Delaveau T.T.D."/>
+<person name="Blugeon C."/>
+<person name="Jacq C."/>
+<person name="Perea J."/>
+</authorList>
+<dbReference type="PubMed" id="8972581"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199612)12:15&lt;1587::aid-yea46>3.0.co;2-6"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 96604 / S288c / FY1679</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="75" last="78">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
+<person name="Jacq C."/>
+<person name="Alt-Moerbe J."/>
+<person name="Andre B."/>
+<person name="Arnold W."/>
+<person name="Bahr A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Bargues M."/>
+<person name="Baron L."/>
+<person name="Becker A."/>
+<person name="Biteau N."/>
+<person name="Bloecker H."/>
+<person name="Blugeon C."/>
+<person name="Boskovic J."/>
+<person name="Brandt P."/>
+<person name="Brueckner M."/>
+<person name="Buitrago M.J."/>
+<person name="Coster F."/>
+<person name="Delaveau T."/>
+<person name="del Rey F."/>
+<person name="Dujon B."/>
+<person name="Eide L.G."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Goffeau A."/>
+<person name="Gomez-Peris A."/>
+<person name="Granotier C."/>
+<person name="Hanemann V."/>
+<person name="Hankeln T."/>
+<person name="Hoheisel J.D."/>
+<person name="Jaeger W."/>
+<person name="Jimenez A."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kraemer C."/>
+<person name="Kuester H."/>
+<person name="Laamanen P."/>
+<person name="Legros Y."/>
+<person name="Louis E.J."/>
+<person name="Moeller-Rieker S."/>
+<person name="Monnet A."/>
+<person name="Moro M."/>
+<person name="Mueller-Auer S."/>
+<person name="Nussbaumer B."/>
+<person name="Paricio N."/>
+<person name="Paulin L."/>
+<person name="Perea J."/>
+<person name="Perez-Alonso M."/>
+<person name="Perez-Ortin J.E."/>
+<person name="Pohl T.M."/>
+<person name="Prydz H."/>
+<person name="Purnelle B."/>
+<person name="Rasmussen S.W."/>
+<person name="Remacha M.A."/>
+<person name="Revuelta J.L."/>
+<person name="Rieger M."/>
+<person name="Salom D."/>
+<person name="Saluz H.P."/>
+<person name="Saiz J.E."/>
+<person name="Saren A.-M."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Schmidt E.R."/>
+<person name="Schneider C."/>
+<person name="Scholler P."/>
+<person name="Schwarz S."/>
+<person name="Soler-Mira A."/>
+<person name="Urrestarazu L.A."/>
+<person name="Verhasselt P."/>
+<person name="Vissers S."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Wagner G."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Woelfl S."/>
+<person name="Harris D.E."/>
+<person name="Bowman S."/>
+<person name="Brown D."/>
+<person name="Churcher C.M."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jones L."/>
+<person name="McDonald S."/>
+<person name="Murphy L.D."/>
+<person name="Niblett D."/>
+<person name="Odell C."/>
+<person name="Oliver K."/>
+<person name="Rajandream M.A."/>
+<person name="Richards C."/>
+<person name="Shore L."/>
+<person name="Walsh S.V."/>
+<person name="Barrell B.G."/>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin D."/>
+<person name="Mosedale D."/>
+<person name="Nakahara K."/>
+<person name="Namath A."/>
+<person name="Oefner P."/>
+<person name="Oh C."/>
+<person name="Petel F.X."/>
+<person name="Roberts D."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Shogren T."/>
+<person name="Shroff N."/>
+<person name="Winant A."/>
+<person name="Yelton M.A."/>
+<person name="Botstein D."/>
+<person name="Davis R.W."/>
+<person name="Johnston M."/>
+<person name="Andrews S."/>
+<person name="Brinkman R."/>
+<person name="Cooper J."/>
+<person name="Ding H."/>
+<person name="Du Z."/>
+<person name="Favello A."/>
+<person name="Fulton L."/>
+<person name="Gattung S."/>
+<person name="Greco T."/>
+<person name="Hallsworth K."/>
+<person name="Hawkins J."/>
+<person name="Hillier L.W."/>
+<person name="Jier M."/>
+<person name="Johnson D."/>
+<person name="Johnston L."/>
+<person name="Kirsten J."/>
+<person name="Kucaba T."/>
+<person name="Langston Y."/>
+<person name="Latreille P."/>
+<person name="Le T."/>
+<person name="Mardis E."/>
+<person name="Menezes S."/>
+<person name="Miller N."/>
+<person name="Nhan M."/>
+<person name="Pauley A."/>
+<person name="Peluso D."/>
+<person name="Rifkin L."/>
+<person name="Riles L."/>
+<person name="Taich A."/>
+<person name="Trevaskis E."/>
+<person name="Vignati D."/>
+<person name="Wilcox L."/>
+<person name="Wohldman P."/>
+<person name="Vaudin M."/>
+<person name="Wilson R."/>
+<person name="Waterston R."/>
+<person name="Albermann K."/>
+<person name="Hani J."/>
+<person name="Heumann K."/>
+<person name="Kleine K."/>
+<person name="Mewes H.-W."/>
+<person name="Zollner A."/>
+<person name="Zaccaria P."/>
+</authorList>
+<dbReference type="PubMed" id="9169867"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2001" name="Mol. Biol. Cell" volume="12" first="3644" last="3657">
+<title>Novel stress-responsive genes EMG1 and NOP14 encode conserved, interacting proteins required for 40S ribosome biogenesis.</title>
+<authorList>
+<person name="Liu P.C."/>
+<person name="Thiele D.J."/>
+</authorList>
+<dbReference type="PubMed" id="11694595"/>
+<dbReference type="DOI" id="10.1091/mbc.12.11.3644"/>
+</citation>
+<scope>INTERACTION WITH EMG1</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2002" name="Nature" volume="417" first="967" last="970">
+<title>A large nucleolar U3 ribonucleoprotein required for 18S ribosomal RNA biogenesis.</title>
+<authorList>
+<person name="Dragon F."/>
+<person name="Gallagher J.E.G."/>
+<person name="Compagnone-Post P.A."/>
+<person name="Mitchell B.M."/>
+<person name="Porwancher K.A."/>
+<person name="Wehner K.A."/>
+<person name="Wormsley S."/>
+<person name="Settlage R.E."/>
+<person name="Shabanowitz J."/>
+<person name="Osheim Y."/>
+<person name="Beyer A.L."/>
+<person name="Hunt D.F."/>
+<person name="Baserga S.J."/>
+</authorList>
+<dbReference type="PubMed" id="12068309"/>
+<dbReference type="DOI" id="10.1038/nature00769"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH MPP10 AND SNORNA U3</scope>
+<scope>IDENTIFICATION IN SSU PROCESSOME BY MASS SPECTROMETRY</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="4072" last="4081">
+<title>A Noc complex specifically involved in the formation and nuclear export of ribosomal 40 S subunits.</title>
+<authorList>
+<person name="Milkereit P."/>
+<person name="Strauss D."/>
+<person name="Bassler J."/>
+<person name="Gadal O."/>
+<person name="Kuhn H."/>
+<person name="Schutz S."/>
+<person name="Gas N."/>
+<person name="Lechner J."/>
+<person name="Hurt E."/>
+<person name="Tschochner H."/>
+</authorList>
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+<dbReference type="DOI" id="10.1074/jbc.m208898200"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH NOC4</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
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+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="2 3">Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm.</text>
+</comment>
+<comment type="subunit">
+<text evidence="1 2 3">Interacts with snoRNA U3. Interacts with EMG1, MPP10 and NOC4. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3.</text>
+</comment>
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+<interactant intactId="EBI-11979">
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+</entry>
+<entry dataset="Swiss-Prot" created="1996-10-01" modified="2021-04-07" version="196">
+<accession>P54784</accession>
+<accession>D6VZA8</accession>
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+<recommendedName>
+<fullName>Origin recognition complex subunit 1</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Origin recognition complex 120 kDa subunit</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">ORC1</name>
+<name type="ordered locus">YML065W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
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+<citation type="journal article" date="1995" name="Cell" volume="83" first="563" last="568">
+<title>The multidomain structure of Orc1p reveals similarity to regulators of DNA replication and transcriptional silencing.</title>
+<authorList>
+<person name="Bell S.P."/>
+<person name="Mitchell J."/>
+<person name="Leber J."/>
+<person name="Kobayashi R."/>
+<person name="Stillman B."/>
+</authorList>
+<dbReference type="PubMed" id="7585959"/>
+<dbReference type="DOI" id="10.1016/0092-8674(95)90096-9"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<scope>PROTEIN SEQUENCE OF 381-408; 532-550; 642-653 AND 726-732</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1995" name="Mol. Biol. Cell" volume="6" first="741" last="756">
+<title>The origin recognition complex in silencing, cell cycle progression, and DNA replication.</title>
+<authorList>
+<person name="Loo S."/>
+<person name="Fox C.A."/>
+<person name="Rine J."/>
+<person name="Kobayashi R."/>
+<person name="Stillman B."/>
+<person name="Bell S.P."/>
+</authorList>
+<dbReference type="PubMed" id="7579692"/>
+<dbReference type="DOI" id="10.1091/mbc.6.6.741"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="90" last="93">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.</title>
+<authorList>
+<person name="Bowman S."/>
+<person name="Churcher C.M."/>
+<person name="Badcock K."/>
+<person name="Brown D."/>
+<person name="Chillingworth T."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Devlin K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jagels K."/>
+<person name="Lye G."/>
+<person name="Moule S."/>
+<person name="Odell C."/>
+<person name="Pearson D."/>
+<person name="Rajandream M.A."/>
+<person name="Rice P."/>
+<person name="Skelton J."/>
+<person name="Walsh S.V."/>
+<person name="Whitehead S."/>
+<person name="Barrell B.G."/>
+</authorList>
+<dbReference type="PubMed" id="9169872"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2000" name="Genes Cells" volume="5" first="975" last="989">
+<title>Interactions between Mcm10p and other replication factors are required for proper initiation and elongation of chromosomal DNA replication in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Kawasaki Y."/>
+<person name="Hiraga S."/>
+<person name="Sugino A."/>
+</authorList>
+<dbReference type="PubMed" id="11168584"/>
+<dbReference type="DOI" id="10.1046/j.1365-2443.2000.00387.x"/>
+</citation>
+<scope>INTERACTION MCM10</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2007" name="FEMS Yeast Res." volume="7" first="1256" last="1262">
+<title>Interaction between ORC and Cdt1p of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Asano T."/>
+<person name="Makise M."/>
+<person name="Takehara M."/>
+<person name="Mizushima T."/>
+</authorList>
+<dbReference type="PubMed" id="17825064"/>
+<dbReference type="DOI" id="10.1111/j.1567-1364.2007.00299.x"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH TAH11</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
+<person name="Haas W."/>
+<person name="Villen J."/>
+<person name="Elias J.E."/>
+<person name="Gygi S.P."/>
+</authorList>
+<dbReference type="PubMed" id="17330950"/>
+<dbReference type="DOI" id="10.1021/pr060559j"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ADR376</strain>
+</source>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-237</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="6">Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.</text>
+</comment>
+<comment type="subunit">
+<text evidence="4 6">Component of the origin recognition complex (ORC) composed of at least ORC1, ORC2, ORC3, ORC4, ORC5 and ORC6. Interacts with MCM10 and TAH11.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-12568">
+<id>P54784</id>
+</interactant>
+<interactant intactId="EBI-12580">
+<id>P54791</id>
+<label>ORC4</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>6</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-12568">
+<id>P54784</id>
+</interactant>
+<interactant intactId="EBI-12588">
+<id>P38826</id>
+<label>ORC6</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>4</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-12568">
+<id>P54784</id>
+</interactant>
+<interactant intactId="EBI-17211">
+<id>P21691</id>
+<label>SIR1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="domain">
+<text>The N-terminus is dedicated to mating-type repression.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="5">Present with 3930 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="7">Belongs to the ORC1 family.</text>
+</comment>
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+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="protein sequence ID" value="CAA86256.1"/>
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+<title>Autoregulation may control the expression of yeast pyruvate decarboxylase structural genes PDC1 and PDC5.</title>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
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+<person name="Hillier L.W."/>
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+<person name="Albermann K."/>
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+<person name="Delius H."/>
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+<person name="Entian K.-D."/>
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+<person name="Koetter P."/>
+<person name="Louis E.J."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
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+<person name="Rose M."/>
+<person name="Scharfe M."/>
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+<person name="Schwager C."/>
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+<scope>PROTEIN SEQUENCE OF 47-57; 260-269; 344-355; 486-497 AND 507-512</scope>
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+<strain>ATCC 38531 / Y41</strain>
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+<scope>ENZYME ACTIVITY</scope>
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+<authorList>
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+<person name="Takakura H."/>
+<person name="Blomberg A."/>
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+<scope>GENERATION OF ACYLOINS</scope>
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+<scope>AROMATIC AMINO ACIDS AS NITROGEN SOURCE</scope>
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+<scope>BIOTECHNOLOGICAL RELEVANCE</scope>
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+<dbReference type="DOI" id="10.1016/s0167-4838(98)00069-7"/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+</reference>
+<comment type="function">
+<text evidence="1 2 5 6 7 8 11 13 17 19 21">Major of three pyruvate decarboxylases (PDC1, PDC5, PDC6) implicated in the nonoxidative conversion of pyruvate to acetaldehyde and carbon dioxide during alcoholic fermentation. Most of the produced acetaldehyde is subsequently reduced to ethanol, but some is required for cytosolic acetyl-CoA production for biosynthetic pathways. The enzyme is also one of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) able to decarboxylate more complex 2-oxo acids (alpha-ketoacids) than pyruvate, which seem mainly involved in amino acid catabolism. Here the enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids. In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from threonine (2-oxobutanoate), norvaline (2-oxopentanoate), valine (3-methyl-2-oxobutanoate, also alpha-keto-isovalerate), isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate), phenylalanine (phenylpyruvate), and tryptophan (3-(indol-3-yl)pyruvate), whereas transaminated leucine is no substrate. In a side-reaction the carbanionic intermediate (or active aldehyde) generated by decarboxylation or by activation of an aldehyde can react with an aldehyde via condensation (or carboligation) yielding a 2-hydroxy ketone, collectively called acyloins.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="13">
+<text>H(+) + pyruvate = acetaldehyde + CO2</text>
+<dbReference type="Rhea" id="RHEA:45484"/>
+<dbReference type="ChEBI" id="CHEBI:15343"/>
+<dbReference type="ChEBI" id="CHEBI:15361"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:16526"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="21">
+<text>3-methyl-2-oxobutanoate + H(+) = 2-methylpropanal + CO2</text>
+<dbReference type="Rhea" id="RHEA:54356"/>
+<dbReference type="ChEBI" id="CHEBI:11851"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:16526"/>
+<dbReference type="ChEBI" id="CHEBI:48943"/>
+<dbReference type="EC" id="4.1.1.72"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="5">
+<text>(S)-3-methyl-2-oxopentanoate + H(+) = 2-methylbutanal + CO2</text>
+<dbReference type="Rhea" id="RHEA:21108"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:16182"/>
+<dbReference type="ChEBI" id="CHEBI:16526"/>
+<dbReference type="ChEBI" id="CHEBI:35146"/>
+<dbReference type="EC" id="4.1.1.72"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="7">
+<text>H(+) + indole-3-pyruvate = CO2 + indole-3-acetaldehyde</text>
+<dbReference type="Rhea" id="RHEA:18017"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:16526"/>
+<dbReference type="ChEBI" id="CHEBI:17640"/>
+<dbReference type="ChEBI" id="CHEBI:18086"/>
+<dbReference type="EC" id="4.1.1.74"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="7">
+<text>3-phenylpyruvate + H(+) = 2-phenylacetaldehyde + CO2</text>
+<dbReference type="Rhea" id="RHEA:14185"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:16424"/>
+<dbReference type="ChEBI" id="CHEBI:16526"/>
+<dbReference type="ChEBI" id="CHEBI:18005"/>
+<dbReference type="EC" id="4.1.1.43"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="11">
+<text>2-oxobutanoate + H(+) = CO2 + propanal</text>
+<dbReference type="Rhea" id="RHEA:55072"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:16526"/>
+<dbReference type="ChEBI" id="CHEBI:16763"/>
+<dbReference type="ChEBI" id="CHEBI:17153"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="11 12">
+<text>2-oxopentanoate + H(+) = butanal + CO2</text>
+<dbReference type="Rhea" id="RHEA:50312"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:15743"/>
+<dbReference type="ChEBI" id="CHEBI:16526"/>
+<dbReference type="ChEBI" id="CHEBI:28644"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="6 23">
+<text>2 acetaldehyde = acetoin</text>
+<dbReference type="Rhea" id="RHEA:54364"/>
+<dbReference type="ChEBI" id="CHEBI:15343"/>
+<dbReference type="ChEBI" id="CHEBI:15688"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="6 23">
+<text>acetaldehyde + H(+) + pyruvate = acetoin + CO2</text>
+<dbReference type="Rhea" id="RHEA:54368"/>
+<dbReference type="ChEBI" id="CHEBI:15343"/>
+<dbReference type="ChEBI" id="CHEBI:15361"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:15688"/>
+<dbReference type="ChEBI" id="CHEBI:16526"/>
+</reaction>
+</comment>
+<comment type="cofactor">
+<cofactor>
+<name>Mg(2+)</name>
+<dbReference type="ChEBI" id="CHEBI:18420"/>
+</cofactor>
+<text>Binds 1 Mg(2+) per subunit.</text>
+</comment>
+<comment type="cofactor">
+<cofactor>
+<name>thiamine diphosphate</name>
+<dbReference type="ChEBI" id="CHEBI:58937"/>
+</cofactor>
+<text>Binds 1 thiamine pyrophosphate per subunit.</text>
+</comment>
+<comment type="activity regulation">
+<text>Allosterically activated by substrate.</text>
+</comment>
+<comment type="biophysicochemical properties">
+<kinetics>
+<KM evidence="11">2.8 mM for pyruvate</KM>
+<KM evidence="11">1.0 mM for 2-oxobutanoate</KM>
+<KM evidence="11">1.5 mM for 2-oxopentanoate</KM>
+<Vmax evidence="11">1.5 umol/min/mg enzyme for pyruvate</Vmax>
+<Vmax evidence="11">0.5 umol/min/mg enzyme for 2-oxobutanoate</Vmax>
+<Vmax evidence="11">0.4 umol/min/mg enzyme for 2-oxopentanoate</Vmax>
+<Vmax evidence="11">38 umol/min/mg enzyme for 3-methyl-2-oxobutanoate</Vmax>
+<Vmax evidence="11">15 umol/min/mg enzyme for 4-methyl-2-oxopentanoate</Vmax>
+<Vmax evidence="11">9 umol/min/mg enzyme for 3-methyl-2-oxopentanoate</Vmax>
+<Vmax evidence="11">41 umol/min/mg enzyme for 4-methylthio-2-oxobutanoate</Vmax>
+</kinetics>
+</comment>
+<comment type="pathway">
+<text>Fermentation; ethanol fermentation.</text>
+</comment>
+<comment type="pathway">
+<text>Amino-acid degradation; Ehrlich pathway.</text>
+</comment>
+<comment type="subunit">
+<text evidence="4 15 16">Homotetramer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="9">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="9">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="induction">
+<text>Protein expression is strongly induced by high concentrations of fermentable carbon sources and under anaerobic growth conditions and is repressed by ethanol. Protein expression level is also autoregulated through an unknown mechanism.</text>
+</comment>
+<comment type="PTM">
+<text evidence="3 18">Cleavage of N-terminal methionine and N-terminal acetylation by NAT1/ARD1.</text>
+</comment>
+<comment type="biotechnology">
+<text evidence="20">Fusel oils and acyloins are important flavor and aroma compounds in yeast-fermented products contributing to the quality of beverages and food, e.g. fusel oils in whiskey, contrary to common believe, seem to alleviate hangover. In general they are desirable at low concentrations, whereas high concentrations may spoil the product. By adjusting growth conditions and substrate their production is sought to be influenced. Due to their broad substrate tolerance pyruvate decarboxylases are important biocatalysts for chemoenzymatic syntheses, both by fermentation and in vitro, e.g. in the production of ephedrine, vitamin E, or phenylethanol (rose flavor).</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="10">Present with 8966 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="22">Belongs to the TPP enzyme family.</text>
+</comment>
+<dbReference type="EC" id="4.1.1.-" evidence="12 13"/>
+<dbReference type="EC" id="4.1.1.43" evidence="7"/>
+<dbReference type="EC" id="4.1.1.72" evidence="5 21"/>
+<dbReference type="EC" id="4.1.1.74" evidence="7"/>
+<dbReference type="EMBL" id="X04675">
+<property type="protein sequence ID" value="CAA28380.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X77316">
+<property type="protein sequence ID" value="CAA54522.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X94607">
+<property type="protein sequence ID" value="CAA64291.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z73216">
+<property type="protein sequence ID" value="CAA97573.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z73217">
+<property type="protein sequence ID" value="CAA97575.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X77312">
+<property type="protein sequence ID" value="CAA54518.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X77315">
+<property type="protein sequence ID" value="CAA54521.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09362.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S64871">
+<property type="entry name" value="DCBYP"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013145.1">
+<property type="nucleotide sequence ID" value="NM_001181931.1"/>
+</dbReference>
+<dbReference type="PDB" id="1PVD">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.30"/>
+<property type="chains" value="A/B=2-556"/>
+</dbReference>
+<dbReference type="PDB" id="1PYD">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.40"/>
+<property type="chains" value="A/B=1-556"/>
+</dbReference>
+<dbReference type="PDB" id="1QPB">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.40"/>
+<property type="chains" value="A/B=1-563"/>
+</dbReference>
+<dbReference type="PDB" id="2VK1">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="1.71"/>
+<property type="chains" value="A/B/C/D=1-563"/>
+</dbReference>
+<dbReference type="PDB" id="2VK8">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="1.42"/>
+<property type="chains" value="A/B/C/D=1-563"/>
+</dbReference>
+<dbReference type="PDB" id="2W93">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="1.60"/>
+<property type="chains" value="A/B/C/D=1-563"/>
+</dbReference>
+<dbReference type="PDBsum" id="1PVD"/>
+<dbReference type="PDBsum" id="1PYD"/>
+<dbReference type="PDBsum" id="1QPB"/>
+<dbReference type="PDBsum" id="2VK1"/>
+<dbReference type="PDBsum" id="2VK8"/>
+<dbReference type="PDBsum" id="2W93"/>
+<dbReference type="SMR" id="P06169"/>
+<dbReference type="BioGRID" id="31319">
+<property type="interactions" value="190"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-6773N"/>
+<dbReference type="IntAct" id="P06169">
+<property type="interactions" value="134"/>
+</dbReference>
+<dbReference type="MINT" id="P06169"/>
+<dbReference type="STRING" id="4932.YLR044C"/>
+<dbReference type="CarbonylDB" id="P06169"/>
+<dbReference type="iPTMnet" id="P06169"/>
+<dbReference type="COMPLUYEAST-2DPAGE" id="P06169"/>
+<dbReference type="SWISS-2DPAGE" id="P06169"/>
+<dbReference type="MaxQB" id="P06169"/>
+<dbReference type="PaxDb" id="P06169"/>
+<dbReference type="PRIDE" id="P06169"/>
+<dbReference type="TopDownProteomics" id="P06169"/>
+<dbReference type="EnsemblFungi" id="YLR044C_mRNA">
+<property type="protein sequence ID" value="YLR044C"/>
+<property type="gene ID" value="YLR044C"/>
+</dbReference>
+<dbReference type="GeneID" id="850733"/>
+<dbReference type="KEGG" id="sce:YLR044C"/>
+<dbReference type="SGD" id="S000004034">
+<property type="gene designation" value="PDC1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YLR044C"/>
+<dbReference type="eggNOG" id="KOG1184">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00940000176336"/>
+<dbReference type="HOGENOM" id="CLU_013748_0_2_1"/>
+<dbReference type="InParanoid" id="P06169"/>
+<dbReference type="OMA" id="VGCPSTI"/>
+<dbReference type="BioCyc" id="MetaCyc:MONOMER3O-117"/>
+<dbReference type="BRENDA" id="4.1.1.1">
+<property type="organism ID" value="984"/>
+</dbReference>
+<dbReference type="SABIO-RK" id="P06169"/>
+<dbReference type="UniPathway" id="UPA00206"/>
+<dbReference type="UniPathway" id="UPA00866"/>
+<dbReference type="EvolutionaryTrace" id="P06169"/>
+<dbReference type="PRO" id="PR:P06169"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XII"/>
+</dbReference>
+<dbReference type="RNAct" id="P06169">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046809">
+<property type="term" value="C:replication compartment"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0047433">
+<property type="term" value="F:branched-chain-2-oxoacid decarboxylase activity"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0016831">
+<property type="term" value="F:carboxy-lyase activity"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0047434">
+<property type="term" value="F:indolepyruvate decarboxylase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000287">
+<property type="term" value="F:magnesium ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="InterPro"/>
+</dbReference>
+<dbReference type="GO" id="GO:0050177">
+<property type="term" value="F:phenylpyruvate decarboxylase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004737">
+<property type="term" value="F:pyruvate decarboxylase activity"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0030976">
+<property type="term" value="F:thiamine pyrophosphate binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="InterPro"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000949">
+<property type="term" value="P:aromatic amino acid family catabolic process to alcohol via Ehrlich pathway"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0009083">
+<property type="term" value="P:branched-chain amino acid catabolic process"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0019655">
+<property type="term" value="P:glycolytic fermentation to ethanol"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006559">
+<property type="term" value="P:L-phenylalanine catabolic process"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006090">
+<property type="term" value="P:pyruvate metabolic process"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0045069">
+<property type="term" value="P:regulation of viral genome replication"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006569">
+<property type="term" value="P:tryptophan catabolic process"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR029035">
+<property type="entry name" value="DHS-like_NAD/FAD-binding_dom"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR029061">
+<property type="entry name" value="THDP-binding"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012000">
+<property type="entry name" value="Thiamin_PyroP_enz_cen_dom"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012001">
+<property type="entry name" value="Thiamin_PyroP_enz_TPP-bd_dom"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000399">
+<property type="entry name" value="TPP-bd_CS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012110">
+<property type="entry name" value="TPP_enzyme"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR011766">
+<property type="entry name" value="TPP_enzyme-bd_C"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR43452">
+<property type="entry name" value="PTHR43452"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF02775">
+<property type="entry name" value="TPP_enzyme_C"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00205">
+<property type="entry name" value="TPP_enzyme_M"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF02776">
+<property type="entry name" value="TPP_enzyme_N"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PIRSF" id="PIRSF036565">
+<property type="entry name" value="Pyruvt_ip_decrb"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF52467">
+<property type="entry name" value="SSF52467"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF52518">
+<property type="entry name" value="SSF52518"/>
+<property type="match status" value="2"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00187">
+<property type="entry name" value="TPP_ENZYMES"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0021">Allosteric enzyme</keyword>
+<keyword id="KW-0101">Branched-chain amino acid catabolism</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0210">Decarboxylase</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0456">Lyase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0585">Phenylalanine catabolism</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0786">Thiamine pyrophosphate</keyword>
+<keyword id="KW-0823">Tryptophan catabolism</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="3 18">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="Pyruvate decarboxylase isozyme 1" id="PRO_0000090770">
+<location>
+<begin position="2"/>
+<end position="563"/>
+</location>
+</feature>
+<feature type="region of interest" description="Thiamine pyrophosphate binding">
+<location>
+<begin position="390"/>
+<end position="476"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium">
+<location>
+<position position="444"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium">
+<location>
+<position position="471"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; via carbonyl oxygen">
+<location>
+<position position="473"/>
+</location>
+</feature>
+<feature type="binding site" description="Substrate">
+<location>
+<position position="28"/>
+</location>
+</feature>
+<feature type="binding site" description="Substrate">
+<location>
+<position position="115"/>
+</location>
+</feature>
+<feature type="binding site" description="Substrate; allosteric site">
+<location>
+<position position="157"/>
+</location>
+</feature>
+<feature type="binding site" description="Substrate">
+<location>
+<position position="477"/>
+</location>
+</feature>
+<feature type="modified residue" description="N-acetylserine" evidence="3 18">
+<location>
+<position position="2"/>
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+<title>Insertion site specificity of the transposon Tn3.</title>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="75" last="78">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
+<person name="Jacq C."/>
+<person name="Alt-Moerbe J."/>
+<person name="Andre B."/>
+<person name="Arnold W."/>
+<person name="Bahr A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Bargues M."/>
+<person name="Baron L."/>
+<person name="Becker A."/>
+<person name="Biteau N."/>
+<person name="Bloecker H."/>
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+<person name="Boskovic J."/>
+<person name="Brandt P."/>
+<person name="Brueckner M."/>
+<person name="Buitrago M.J."/>
+<person name="Coster F."/>
+<person name="Delaveau T."/>
+<person name="del Rey F."/>
+<person name="Dujon B."/>
+<person name="Eide L.G."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Goffeau A."/>
+<person name="Gomez-Peris A."/>
+<person name="Granotier C."/>
+<person name="Hanemann V."/>
+<person name="Hankeln T."/>
+<person name="Hoheisel J.D."/>
+<person name="Jaeger W."/>
+<person name="Jimenez A."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kraemer C."/>
+<person name="Kuester H."/>
+<person name="Laamanen P."/>
+<person name="Legros Y."/>
+<person name="Louis E.J."/>
+<person name="Moeller-Rieker S."/>
+<person name="Monnet A."/>
+<person name="Moro M."/>
+<person name="Mueller-Auer S."/>
+<person name="Nussbaumer B."/>
+<person name="Paricio N."/>
+<person name="Paulin L."/>
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+<scope>MUTAGENESIS OF 7-LYS-LYS-8 AND 17-LYS-LYS-18</scope>
+<scope>FUNCTION</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="28">
+<citation type="journal article" date="2006" name="Mol. Cell. Proteomics" volume="5" first="737" last="748">
+<title>A tandem affinity tag for two-step purification under fully denaturing conditions: application in ubiquitin profiling and protein complex identification combined with in vivocross-linking.</title>
+<authorList>
+<person name="Tagwerker C."/>
+<person name="Flick K."/>
+<person name="Cui M."/>
+<person name="Guerrero C."/>
+<person name="Dou Y."/>
+<person name="Auer B."/>
+<person name="Baldi P."/>
+<person name="Huang L."/>
+<person name="Kaiser P."/>
+</authorList>
+<dbReference type="PubMed" id="16432255"/>
+<dbReference type="DOI" id="10.1074/mcp.m500368-mcp200"/>
+</citation>
+<scope>UBIQUITINATION AT LYS-124</scope>
+</reference>
+<reference key="29">
+<citation type="journal article" date="2009" name="J. Proteome Res." volume="8" first="900" last="906">
+<title>Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software.</title>
+<authorList>
+<person name="Zhang K."/>
+<person name="Chen Y."/>
+<person name="Zhang Z."/>
+<person name="Zhao Y."/>
+</authorList>
+<dbReference type="PubMed" id="19113941"/>
+<dbReference type="DOI" id="10.1021/pr8005155"/>
+</citation>
+<scope>ACETYLATION AT LYS-17; LYS-18; LYS-22 AND LYS-23</scope>
+<scope>BUTYRYLATION AT LYS-22</scope>
+<scope>METHYLATION AT LYS-23 AND LYS-38</scope>
+</reference>
+<reference key="30">
+<citation type="journal article" date="2012" name="Mol. Cell. Proteomics" volume="11" first="100" last="107">
+<title>Lysine succinylation and lysine malonylation in histones.</title>
+<authorList>
+<person name="Xie Z."/>
+<person name="Dai J."/>
+<person name="Dai L."/>
+<person name="Tan M."/>
+<person name="Cheng Z."/>
+<person name="Wu Y."/>
+<person name="Boeke J.D."/>
+<person name="Zhao Y."/>
+</authorList>
+<dbReference type="PubMed" id="22389435"/>
+<dbReference type="DOI" id="10.1074/mcp.m111.015875"/>
+</citation>
+<scope>SUCCINYLATION AT LYS-35 AND LYS-47</scope>
+</reference>
+<reference key="31">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="32">
+<citation type="journal article" date="2008" name="Nat. Struct. Mol. Biol." volume="15" first="868" last="869">
+<title>NMR structure of chaperone Chz1 complexed with histones H2A.Z-H2B.</title>
+<authorList>
+<person name="Zhou Z."/>
+<person name="Feng H."/>
+<person name="Hansen D.F."/>
+<person name="Kato H."/>
+<person name="Luk E."/>
+<person name="Freedberg D.I."/>
+<person name="Kay L.E."/>
+<person name="Wu C."/>
+<person name="Bai Y."/>
+</authorList>
+<dbReference type="PubMed" id="18641662"/>
+<dbReference type="DOI" id="10.1038/nsmb.1465"/>
+</citation>
+<scope>STRUCTURE BY NMR OF 37-131</scope>
+</reference>
+<comment type="function">
+<text evidence="4 5 9 12 13 14 15 16 18">Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.</text>
+</comment>
+<comment type="subunit">
+<text>The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8088">
+<id>P02293</id>
+</interactant>
+<interactant intactId="EBI-18410">
+<id>P32597</id>
+<label>STH1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Nucleus</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Chromosome</location>
+</subcellularLocation>
+</comment>
+<comment type="PTM">
+<text>Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. Deubiquitination is performed by UBP8 in presence of SGF11.</text>
+</comment>
+<comment type="PTM">
+<text evidence="15 16">Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis.</text>
+</comment>
+<comment type="PTM">
+<text evidence="2 3 11 18">Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription.</text>
+</comment>
+<comment type="PTM">
+<text evidence="10 18">Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription.</text>
+</comment>
+<comment type="similarity">
+<text evidence="21">Belongs to the histone H2B family.</text>
+</comment>
+<comment type="caution">
+<text evidence="21">To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2BK6ac = acetylated Lys-7; H2BK6su = sumoylated Lys-7; H2BK7ac = acetylated Lys-8; H2BK7su = sumoylated Lys-8; H2BS10ph = phosphorylated Ser-11; H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17; H2BK16su = sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1 = monoubiquitinated Lys-124.</text>
+</comment>
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+<property type="protein sequence ID" value="AAA88719.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
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+<property type="protein sequence ID" value="AAC33141.1"/>
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+<property type="nucleotide sequence ID" value="NM_001180532.3"/>
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+</dbReference>
+<dbReference type="PDB" id="5BT1">
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+<dbReference type="PDB" id="6GEN">
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+<property type="resolution" value="3.60"/>
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+</dbReference>
+<dbReference type="PDB" id="6QLD">
+<property type="method" value="EM"/>
+<property type="resolution" value="4.15"/>
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+<dbReference type="PDBsum" id="2JSS"/>
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+<dbReference type="ComplexPortal" id="CPX-1611">
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+<dbReference type="ComplexPortal" id="CPX-1612">
+<property type="entry name" value="Nucleosome, variant HTA1-HTB1"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1613">
+<property type="entry name" value="Nucleosome, variant HTZ1-HTB1"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-416N"/>
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+<dbReference type="MINT" id="P02293"/>
+<dbReference type="STRING" id="4932.YDR224C"/>
+<dbReference type="iPTMnet" id="P02293"/>
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+<dbReference type="PRIDE" id="P02293"/>
+<dbReference type="EnsemblFungi" id="YDR224C_mRNA">
+<property type="protein sequence ID" value="YDR224C"/>
+<property type="gene ID" value="YDR224C"/>
+</dbReference>
+<dbReference type="GeneID" id="851810"/>
+<dbReference type="KEGG" id="sce:YDR224C"/>
+<dbReference type="SGD" id="S000002632">
+<property type="gene designation" value="HTB1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YDR224C"/>
+<dbReference type="eggNOG" id="KOG1744">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT01020000230503"/>
+<dbReference type="HOGENOM" id="CLU_075666_1_3_1"/>
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+<dbReference type="OMA" id="DIFDRMA"/>
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+<property type="pathway name" value="Condensation of Prophase Chromosomes"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-2559580">
+<property type="pathway name" value="Oxidative Stress Induced Senescence"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-3214815">
+<property type="pathway name" value="HDACs deacetylate histones"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-3214847">
+<property type="pathway name" value="HATs acetylate histones"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-427359">
+<property type="pathway name" value="SIRT1 negatively regulates rRNA expression"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-5625886">
+<property type="pathway name" value="Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3"/>
+</dbReference>
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+<property type="pathway name" value="Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks"/>
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+<dbReference type="Reactome" id="R-SCE-73772">
+<property type="pathway name" value="RNA Polymerase I Promoter Escape"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-9018519">
+<property type="pathway name" value="Estrogen-dependent gene expression"/>
+</dbReference>
+<dbReference type="EvolutionaryTrace" id="P02293"/>
+<dbReference type="PRO" id="PR:P02293"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome IV"/>
+</dbReference>
+<dbReference type="RNAct" id="P02293">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000786">
+<property type="term" value="C:nucleosome"/>
+<property type="evidence" value="ECO:0000314"/>
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+<dbReference type="GO" id="GO:0031298">
+<property type="term" value="C:replication fork protection complex"/>
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+<dbReference type="GO" id="GO:0003677">
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+<dbReference type="GO" id="GO:0046982">
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+<property type="term" value="P:nucleosome assembly"/>
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+</dbReference>
+<dbReference type="GO" id="GO:0006301">
+<property type="term" value="P:postreplication repair"/>
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+<property type="entry name" value="Histone-fold"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR007125">
+<property type="entry name" value="Histone_H2A/H2B/H3"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000558">
+<property type="entry name" value="Histone_H2B"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR23428">
+<property type="entry name" value="PTHR23428"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00125">
+<property type="entry name" value="Histone"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PRINTS" id="PR00621">
+<property type="entry name" value="HISTONEH2B"/>
+</dbReference>
+<dbReference type="SMART" id="SM00427">
+<property type="entry name" value="H2B"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF47113">
+<property type="entry name" value="SSF47113"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00357">
+<property type="entry name" value="HISTONE_H2B"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0158">Chromosome</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0488">Methylation</keyword>
+<keyword id="KW-0544">Nucleosome core</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="21">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="Histone H2B.1" id="PRO_0000071938">
+<location>
+<begin position="2"/>
+<end position="131"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="18">
+<location>
+<position position="7"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="18">
+<location>
+<position position="8"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="15 16">
+<location>
+<position position="11"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine" evidence="3 11">
+<location>
+<position position="12"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="3 11 18 19">
+<location>
+<position position="17"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="19">
+<location>
+<position position="18"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="19">
+<location>
+<position position="22"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-butyryllysine; alternate" evidence="19">
+<location>
+<position position="22"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="19">
+<location>
+<position position="23"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-methyllysine; alternate" evidence="19">
+<location>
+<position position="23"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-succinyllysine" evidence="20">
+<location>
+<position position="35"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6,N6-dimethyllysine" evidence="19">
+<location>
+<position position="38"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-succinyllysine" evidence="20">
+<location>
+<position position="47"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate">
+<location>
+<position position="7"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate">
+<location>
+<position position="8"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate" evidence="21">
+<location>
+<position position="17"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate" evidence="21">
+<location>
+<position position="18"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="1 6 7 8 12 17">
+<location>
+<position position="124"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Reduces sumoylation." evidence="18">
+<original>KK</original>
+<variation>AA</variation>
+<location>
+<begin position="7"/>
+<end position="8"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Desensitizes cells to H(2)O(2) treatment." evidence="15">
+<original>S</original>
+<variation>A</variation>
+<location>
+<position position="11"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Induces apoptotic-like features including chromatin condensation." evidence="15">
+<original>S</original>
+<variation>E</variation>
+<location>
+<position position="11"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Reduces sumoylation." evidence="18">
+<original>KK</original>
+<variation>AA</variation>
+<location>
+<begin position="17"/>
+<end position="18"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Confers UV-radiation sensitivity; when associated with F-87 and S-88." evidence="4">
+<original>V</original>
+<variation>F</variation>
+<location>
+<position position="48"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Confers UV-radiation sensitivity; when associated with F-48 and S-88." evidence="4">
+<original>Y</original>
+<variation>F</variation>
+<location>
+<position position="87"/>
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+</reference>
+<reference key="19">
+<citation type="journal article" date="2005" name="Cell" volume="120" first="25" last="36">
+<title>Sterile 20 kinase phosphorylates histone H2B at serine 10 during hydrogen peroxide-induced apoptosis in S. cerevisiae.</title>
+<authorList>
+<person name="Ahn S.-H."/>
+<person name="Cheung W.L."/>
+<person name="Hsu J.-Y."/>
+<person name="Diaz R.L."/>
+<person name="Smith M.M."/>
+<person name="Allis C.D."/>
+</authorList>
+<dbReference type="PubMed" id="15652479"/>
+<dbReference type="DOI" id="10.1016/j.cell.2004.11.016"/>
+</citation>
+<scope>PHOSPHORYLATION AT SER-11</scope>
+<scope>MUTAGENESIS OF SER-11</scope>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="20">
+<citation type="journal article" date="2005" name="Cell Cycle" volume="4" first="780" last="783">
+<title>H2B (Ser10) phosphorylation is induced during apoptosis and meiosis in S. cerevisiae.</title>
+<authorList>
+<person name="Ahn S.-H."/>
+<person name="Henderson K.A."/>
+<person name="Keeney S."/>
+<person name="Allis C.D."/>
+</authorList>
+<dbReference type="PubMed" id="15970663"/>
+<dbReference type="DOI" id="10.4161/cc.4.6.1745"/>
+</citation>
+<scope>PHOSPHORYLATION AT SER-11</scope>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="21">
+<citation type="journal article" date="2005" name="Mol. Cell. Biol." volume="25" first="637" last="651">
+<title>Histone H2B ubiquitylation is associated with elongating RNA polymerase II.</title>
+<authorList>
+<person name="Xiao T."/>
+<person name="Kao C.-F."/>
+<person name="Krogan N.J."/>
+<person name="Sun Z.-W."/>
+<person name="Greenblatt J.F."/>
+<person name="Osley M.A."/>
+<person name="Strahl B.D."/>
+</authorList>
+<dbReference type="PubMed" id="15632065"/>
+<dbReference type="DOI" id="10.1128/mcb.25.2.637-651.2005"/>
+</citation>
+<scope>UBIQUITINATION BY THE UBC2-BRE1 COMPLEX</scope>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="22">
+<citation type="journal article" date="2005" name="Mol. Cell. Biol." volume="25" first="1162" last="1172">
+<title>H2B ubiquitin protease Ubp8 and Sgf11 constitute a discrete functional module within the Saccharomyces cerevisiae SAGA complex.</title>
+<authorList>
+<person name="Ingvarsdottir K."/>
+<person name="Krogan N.J."/>
+<person name="Emre N.C.T."/>
+<person name="Wyce A."/>
+<person name="Thompson N.J."/>
+<person name="Emili A."/>
+<person name="Hughes T.R."/>
+<person name="Greenblatt J.F."/>
+<person name="Berger S.L."/>
+</authorList>
+<dbReference type="PubMed" id="15657441"/>
+<dbReference type="DOI" id="10.1128/mcb.25.3.1162-1172.2005"/>
+</citation>
+<scope>DEUBIQUITINATION BY THE UBP8-SGF11 COMPLEX</scope>
+</reference>
+<reference key="23">
+<citation type="journal article" date="2005" name="Mol. Cell. Biol." volume="25" first="1173" last="1182">
+<title>The deubiquitylation activity of Ubp8 is dependent upon Sgf11 and its association with the SAGA complex.</title>
+<authorList>
+<person name="Lee K.K."/>
+<person name="Florens L."/>
+<person name="Swanson S.K."/>
+<person name="Washburn M.P."/>
+<person name="Workman J.L."/>
+</authorList>
+<dbReference type="PubMed" id="15657442"/>
+<dbReference type="DOI" id="10.1128/mcb.25.3.1173-1182.2005"/>
+</citation>
+<scope>DEUBIQUITINATION BY THE UBP8-SGF11 COMPLEX</scope>
+</reference>
+<reference key="24">
+<citation type="journal article" date="2006" name="Genes Dev." volume="20" first="966" last="976">
+<title>Histone sumoylation is a negative regulator in Saccharomyces cerevisiae and shows dynamic interplay with positive-acting histone modifications.</title>
+<authorList>
+<person name="Nathan D."/>
+<person name="Ingvarsdottir K."/>
+<person name="Sterner D.E."/>
+<person name="Bylebyl G.R."/>
+<person name="Dokmanovic M."/>
+<person name="Dorsey J.A."/>
+<person name="Whelan K.A."/>
+<person name="Krsmanovic M."/>
+<person name="Lane W.S."/>
+<person name="Meluh P.B."/>
+<person name="Johnson E.S."/>
+<person name="Berger S.L."/>
+</authorList>
+<dbReference type="PubMed" id="16598039"/>
+<dbReference type="DOI" id="10.1101/gad.1404206"/>
+</citation>
+<scope>SUMOYLATION AT LYS-7; LYS-8; LYS-17 AND LYS-18</scope>
+<scope>ACETYLATION AT LYS-7; LYS-8 AND LYS-17</scope>
+<scope>MUTAGENESIS OF 7-LYS-LYS-8 AND 17-LYS-LYS-18</scope>
+<scope>FUNCTION</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="25">
+<citation type="journal article" date="2008" name="Mol. Cell. Biol." volume="28" first="1313" last="1325">
+<title>Phosphorylation by casein kinase 2 regulates Nap1 localization and function.</title>
+<authorList>
+<person name="Calvert M.E.K."/>
+<person name="Keck K.M."/>
+<person name="Ptak C."/>
+<person name="Shabanowitz J."/>
+<person name="Hunt D.F."/>
+<person name="Pemberton L.F."/>
+</authorList>
+<dbReference type="PubMed" id="18086883"/>
+<dbReference type="DOI" id="10.1128/mcb.01035-07"/>
+</citation>
+<scope>INTERACTION WITH NAP1</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="26">
+<citation type="journal article" date="2009" name="J. Proteome Res." volume="8" first="900" last="906">
+<title>Identification and verification of lysine propionylation and butyrylation in yeast core histones using PTMap software.</title>
+<authorList>
+<person name="Zhang K."/>
+<person name="Chen Y."/>
+<person name="Zhang Z."/>
+<person name="Zhao Y."/>
+</authorList>
+<dbReference type="PubMed" id="19113941"/>
+<dbReference type="DOI" id="10.1021/pr8005155"/>
+</citation>
+<scope>ACETYLATION AT LYS-17; LYS-18; LYS-22 AND LYS-23</scope>
+<scope>BUTYRYLATION AT LYS-22</scope>
+<scope>METHYLATION AT LYS-23 AND LYS-38</scope>
+</reference>
+<reference key="27">
+<citation type="journal article" date="2012" name="Mol. Cell. Proteomics" volume="11" first="100" last="107">
+<title>Lysine succinylation and lysine malonylation in histones.</title>
+<authorList>
+<person name="Xie Z."/>
+<person name="Dai J."/>
+<person name="Dai L."/>
+<person name="Tan M."/>
+<person name="Cheng Z."/>
+<person name="Wu Y."/>
+<person name="Boeke J.D."/>
+<person name="Zhao Y."/>
+</authorList>
+<dbReference type="PubMed" id="22389435"/>
+<dbReference type="DOI" id="10.1074/mcp.m111.015875"/>
+</citation>
+<scope>SUCCINYLATION AT LYS-35 AND LYS-47</scope>
+</reference>
+<reference key="28">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="29">
+<citation type="journal article" date="2001" name="EMBO J." volume="20" first="5207" last="5218">
+<title>Structure of the yeast nucleosome core particle reveals fundamental changes in internucleosome interactions.</title>
+<authorList>
+<person name="White C.L."/>
+<person name="Suto R.K."/>
+<person name="Luger K."/>
+</authorList>
+<dbReference type="PubMed" id="11566884"/>
+<dbReference type="DOI" id="10.1093/emboj/20.18.5207"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS) OF NUCLEOSOME CORE COMPLEX</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="30">
+<citation type="journal article" date="2006" name="Curr. Biol." volume="16" first="R276" last="R278">
+<title>The path of DNA in the kinetochore.</title>
+<authorList>
+<person name="Bloom K.S."/>
+<person name="Sharma S."/>
+<person name="Dokholyan N.V."/>
+</authorList>
+<dbReference type="PubMed" id="16631569"/>
+<dbReference type="DOI" id="10.1016/j.cub.2006.03.054"/>
+</citation>
+<scope>3D-STRUCTURE MODELING</scope>
+</reference>
+<comment type="function">
+<text evidence="4 9 12 13 14 15 16">Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 17">The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA. Interacts with NAP1.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Nucleus</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Chromosome</location>
+</subcellularLocation>
+</comment>
+<comment type="PTM">
+<text>Monoubiquitinated by the RAD6/UBC2-BRE1 complex to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation. Deubiquitination is performed by UBP8 in presence of SGF11.</text>
+</comment>
+<comment type="PTM">
+<text evidence="14 15">Phosphorylated by STE20 to form H2BS10ph during progression through meiotic prophase. May be correlated with chromosome condensation. H2BS10ph is also formed after H(2)O(2) treatment, and is a step leading to apoptosis.</text>
+</comment>
+<comment type="PTM">
+<text evidence="1 2 11 16">Acetylated by GCN5, a component of the SAGA complex, to form H2BK11ac and H2BK16ac. H2BK16ac can also be formed by ESA1, a component of the NuA4 histone acetyltransferase (HAT) complex. Acetylation of N-terminal lysines and particularly formation of H2BK11acK16ac has a positive effect on transcription.</text>
+</comment>
+<comment type="PTM">
+<text evidence="10 16">Sumoylation to form H2BK6su or H2BK7su, and probably also H2BK16su or H2BK17su, occurs preferentially near the telomeres and represses gene transcription.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="7">Present with 443000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="20">Belongs to the histone H2B family.</text>
+</comment>
+<comment type="caution">
+<text evidence="20">To ensure consistency between histone entries, we follow the 'Brno' nomenclature for histone modifications, with positions referring to those used in the literature for the 'closest' model organism. Due to slight variations in histone sequences between organisms and to the presence of initiator methionine in UniProtKB/Swiss-Prot sequences, the actual positions of modified amino acids in the sequence generally differ. In this entry the following conventions are used: H2BK6ac = acetylated Lys-7; H2BK6su = sumoylated Lys-7; H2BK7ac = acetylated Lys-8; H2BK7su = sumoylated Lys-8; H2BS10ph = phosphorylated Ser-11; H2BK11ac = acetylated Lys-12; H2BK16ac = acetylated Lys-17; H2BK16su = sumoylated Lys-17; H2BK17su = sumoylated Lys-18; H2BK123ub1 = monoubiquitinated Lys-124.</text>
+</comment>
+<dbReference type="EMBL" id="V01308">
+<property type="protein sequence ID" value="CAA24615.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z26494">
+<property type="protein sequence ID" value="CAA81268.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z35763">
+<property type="protein sequence ID" value="CAA84817.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY693063">
+<property type="protein sequence ID" value="AAT93082.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006936">
+<property type="protein sequence ID" value="DAA07120.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S44558">
+<property type="entry name" value="HSBYB2"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_009553.1">
+<property type="nucleotide sequence ID" value="NM_001178242.1"/>
+</dbReference>
+<dbReference type="PDB" id="1ID3">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="3.10"/>
+<property type="chains" value="D/H=2-131"/>
+</dbReference>
+<dbReference type="PDB" id="2FSB">
+<property type="method" value="Model"/>
+<property type="chains" value="D/H=1-131"/>
+</dbReference>
+<dbReference type="PDB" id="4JJN">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="3.09"/>
+<property type="chains" value="D/H=2-131"/>
+</dbReference>
+<dbReference type="PDB" id="6QLD">
+<property type="method" value="EM"/>
+<property type="resolution" value="4.15"/>
+<property type="chains" value="d=37-129"/>
+</dbReference>
+<dbReference type="PDBsum" id="1ID3"/>
+<dbReference type="PDBsum" id="2FSB"/>
+<dbReference type="PDBsum" id="4JJN"/>
+<dbReference type="PDBsum" id="6QLD"/>
+<dbReference type="SMR" id="P02294"/>
+<dbReference type="BioGRID" id="32700">
+<property type="interactions" value="277"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1610">
+<property type="entry name" value="Nucleosome, variant HTA2-HTB2"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1614">
+<property type="entry name" value="Nucleosome, variant HTZ1-HTB2"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-2566">
+<property type="entry name" value="Nucleosome, variant HTA1-HTB2"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-3897N"/>
+<dbReference type="IntAct" id="P02294">
+<property type="interactions" value="101"/>
+</dbReference>
+<dbReference type="MINT" id="P02294"/>
+<dbReference type="STRING" id="4932.YBL002W"/>
+<dbReference type="iPTMnet" id="P02294"/>
+<dbReference type="MaxQB" id="P02294"/>
+<dbReference type="PaxDb" id="P02294"/>
+<dbReference type="PRIDE" id="P02294"/>
+<dbReference type="EnsemblFungi" id="YBL002W_mRNA">
+<property type="protein sequence ID" value="YBL002W"/>
+<property type="gene ID" value="YBL002W"/>
+</dbReference>
+<dbReference type="GeneID" id="852284"/>
+<dbReference type="KEGG" id="sce:YBL002W"/>
+<dbReference type="SGD" id="S000000098">
+<property type="gene designation" value="HTB2"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YBL002W"/>
+<dbReference type="eggNOG" id="KOG1744">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT01020000230503"/>
+<dbReference type="HOGENOM" id="CLU_075666_1_3_1"/>
+<dbReference type="InParanoid" id="P02294"/>
+<dbReference type="OMA" id="MIMNSYI"/>
+<dbReference type="Reactome" id="R-SCE-2299718">
+<property type="pathway name" value="Condensation of Prophase Chromosomes"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-2559580">
+<property type="pathway name" value="Oxidative Stress Induced Senescence"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-3214815">
+<property type="pathway name" value="HDACs deacetylate histones"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-3214847">
+<property type="pathway name" value="HATs acetylate histones"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-427359">
+<property type="pathway name" value="SIRT1 negatively regulates rRNA expression"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-5625886">
+<property type="pathway name" value="Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-5693565">
+<property type="pathway name" value="Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-73772">
+<property type="pathway name" value="RNA Polymerase I Promoter Escape"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-9018519">
+<property type="pathway name" value="Estrogen-dependent gene expression"/>
+</dbReference>
+<dbReference type="EvolutionaryTrace" id="P02294"/>
+<dbReference type="PRO" id="PR:P02294"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome II"/>
+</dbReference>
+<dbReference type="RNAct" id="P02294">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000786">
+<property type="term" value="C:nucleosome"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0031298">
+<property type="term" value="C:replication fork protection complex"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046982">
+<property type="term" value="F:protein heterodimerization activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="InterPro"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006333">
+<property type="term" value="P:chromatin assembly or disassembly"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006334">
+<property type="term" value="P:nucleosome assembly"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="Gene3D" id="1.10.20.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="IDEAL" id="IID50136"/>
+<dbReference type="InterPro" id="IPR009072">
+<property type="entry name" value="Histone-fold"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR007125">
+<property type="entry name" value="Histone_H2A/H2B/H3"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000558">
+<property type="entry name" value="Histone_H2B"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR23428">
+<property type="entry name" value="PTHR23428"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00125">
+<property type="entry name" value="Histone"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PRINTS" id="PR00621">
+<property type="entry name" value="HISTONEH2B"/>
+</dbReference>
+<dbReference type="SMART" id="SM00427">
+<property type="entry name" value="H2B"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF47113">
+<property type="entry name" value="SSF47113"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00357">
+<property type="entry name" value="HISTONE_H2B"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0158">Chromosome</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0488">Methylation</keyword>
+<keyword id="KW-0544">Nucleosome core</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="20">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="Histone H2B.2" id="PRO_0000071939">
+<location>
+<begin position="2"/>
+<end position="131"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="16">
+<location>
+<position position="7"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="16">
+<location>
+<position position="8"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="14 15">
+<location>
+<position position="11"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine" evidence="2 11">
+<location>
+<position position="12"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="2 11 16 18">
+<location>
+<position position="17"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="18">
+<location>
+<position position="18"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="18">
+<location>
+<position position="22"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-butyryllysine; alternate" evidence="18">
+<location>
+<position position="22"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-acetyllysine; alternate" evidence="18">
+<location>
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+<feature type="modified residue" description="N6-methyllysine; alternate" evidence="18">
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+<feature type="modified residue" description="N6-succinyllysine" evidence="19">
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+<feature type="modified residue" description="N6,N6-dimethyllysine" evidence="18">
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+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate">
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+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate">
+<location>
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+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate" evidence="20">
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+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate" evidence="20">
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+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="5 6 8 12">
+<location>
+<position position="124"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Reduces sumoylation." evidence="16">
+<original>KK</original>
+<variation>AA</variation>
+<location>
+<begin position="7"/>
+<end position="8"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Desensitizes cells to H(2)O(2) treatment." evidence="14">
+<original>S</original>
+<variation>A</variation>
+<location>
+<position position="11"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Induces apoptotic-like features including chromatin condensation." evidence="14">
+<original>S</original>
+<variation>E</variation>
+<location>
+<position position="11"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Reduces sumoylation." evidence="16">
+<original>KK</original>
+<variation>AA</variation>
+<location>
+<begin position="17"/>
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+</feature>
+<feature type="mutagenesis site" description="Impairs ubiquitin conjugation, DNA double-strand breaks formation during meiosis and histone H3-K79 methylation." evidence="4 8 12">
+<original>K</original>
+<variation>R</variation>
+<location>
+<position position="124"/>
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+</feature>
+<feature type="helix" evidence="21">
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+<begin position="42"/>
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+</entry>
+<entry dataset="Swiss-Prot" created="1990-04-01" modified="2021-04-07" version="212">
+<accession>P15108</accession>
+<accession>D6W010</accession>
+<name>HSC82_YEAST</name>
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+<recommendedName>
+<fullName>ATP-dependent molecular chaperone HSC82</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>82 kDa heat shock cognate protein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Heat shock protein Hsp90 constitutive isoform</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">HSC82</name>
+<name type="ordered locus">YMR186W</name>
+<name type="ORF">YM8010.16</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1989" name="Mol. Cell. Biol." volume="9" first="3919" last="3930">
+<title>hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.</title>
+<authorList>
+<person name="Borkovich K.A."/>
+<person name="Farrelly F.W."/>
+<person name="Finkelstein D.B."/>
+<person name="Taulien J."/>
+<person name="Lindquist S."/>
+</authorList>
+<dbReference type="PubMed" id="2674684"/>
+<dbReference type="DOI" id="10.1128/mcb.9.9.3919"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE</scope>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="90" last="93">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.</title>
+<authorList>
+<person name="Bowman S."/>
+<person name="Churcher C.M."/>
+<person name="Badcock K."/>
+<person name="Brown D."/>
+<person name="Chillingworth T."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Devlin K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jagels K."/>
+<person name="Lye G."/>
+<person name="Moule S."/>
+<person name="Odell C."/>
+<person name="Pearson D."/>
+<person name="Rajandream M.A."/>
+<person name="Rice P."/>
+<person name="Skelton J."/>
+<person name="Walsh S.V."/>
+<person name="Whitehead S."/>
+<person name="Barrell B.G."/>
+</authorList>
+<dbReference type="PubMed" id="9169872"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="601" last="613">
+<title>Two-dimensional protein map of Saccharomyces cerevisiae: construction of a gene-protein index.</title>
+<authorList>
+<person name="Boucherie H."/>
+<person name="Dujardin G."/>
+<person name="Kermorgant M."/>
+<person name="Monribot C."/>
+<person name="Slonimski P.P."/>
+<person name="Perrot M."/>
+</authorList>
+<dbReference type="PubMed" id="7483834"/>
+<dbReference type="DOI" id="10.1002/yea.320110702"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 2-8</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1997" name="J. Cell Sci." volume="110" first="1879" last="1891">
+<title>A yeast heat shock transcription factor (Hsf1) mutant is defective in both Hsc82/Hsp82 synthesis and spindle pole body duplication.</title>
+<authorList>
+<person name="Zarzov P."/>
+<person name="Boucherie H."/>
+<person name="Mann C."/>
+</authorList>
+<dbReference type="PubMed" id="9296388"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2000" name="Mol. Cell. Biol." volume="20" first="9262" last="9270">
+<title>Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin.</title>
+<authorList>
+<person name="Imai J."/>
+<person name="Yahara I."/>
+</authorList>
+<dbReference type="PubMed" id="11094077"/>
+<dbReference type="DOI" id="10.1128/mcb.20.24.9262-9270.2000"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH CNA2</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2002" name="J. Biol. Chem." volume="277" first="34959" last="34966">
+<title>Interaction between the N-terminal and middle regions is essential for the in vivo function of HSP90 molecular chaperone.</title>
+<authorList>
+<person name="Matsumoto S."/>
+<person name="Tanaka E."/>
+<person name="Nemoto T.K."/>
+<person name="Ono T."/>
+<person name="Takagi T."/>
+<person name="Imai J."/>
+<person name="Kimura Y."/>
+<person name="Yahara I."/>
+<person name="Kobayakawa T."/>
+<person name="Ayuse T."/>
+<person name="Oi K."/>
+<person name="Mizuno A."/>
+</authorList>
+<dbReference type="PubMed" id="12121981"/>
+<dbReference type="DOI" id="10.1074/jbc.m203038200"/>
+</citation>
+<scope>MUTAGENESIS OF LEU-453 AND GLU-493</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2004" name="Mol. Cell. Biol." volume="24" first="8069" last="8079">
+<title>Sgt1 associates with Hsp90: an initial step of assembly of the core kinetochore complex.</title>
+<authorList>
+<person name="Bansal P.K."/>
+<person name="Abdulle R."/>
+<person name="Kitagawa K."/>
+</authorList>
+<dbReference type="PubMed" id="15340069"/>
+<dbReference type="DOI" id="10.1128/mcb.24.18.8069-8079.2004"/>
+</citation>
+<scope>INTERACTION WITH SGT1</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="13207" last="13212">
+<title>The proteome of Saccharomyces cerevisiae mitochondria.</title>
+<authorList>
+<person name="Sickmann A."/>
+<person name="Reinders J."/>
+<person name="Wagner Y."/>
+<person name="Joppich C."/>
+<person name="Zahedi R.P."/>
+<person name="Meyer H.E."/>
+<person name="Schoenfisch B."/>
+<person name="Perschil I."/>
+<person name="Chacinska A."/>
+<person name="Guiard B."/>
+<person name="Rehling P."/>
+<person name="Pfanner N."/>
+<person name="Meisinger C."/>
+</authorList>
+<dbReference type="PubMed" id="14576278"/>
+<dbReference type="DOI" id="10.1073/pnas.2135385100"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ATCC 76625 / YPH499</strain>
+</source>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2008" name="Mol. Cell. Biol." volume="28" first="1313" last="1325">
+<title>Phosphorylation by casein kinase 2 regulates Nap1 localization and function.</title>
+<authorList>
+<person name="Calvert M.E.K."/>
+<person name="Keck K.M."/>
+<person name="Ptak C."/>
+<person name="Shabanowitz J."/>
+<person name="Hunt D.F."/>
+<person name="Pemberton L.F."/>
+</authorList>
+<dbReference type="PubMed" id="18086883"/>
+<dbReference type="DOI" id="10.1128/mcb.01035-07"/>
+</citation>
+<scope>INTERACTION WITH NAP1</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="1 2">Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins involved in cell cycle control and signal transduction such as CNA2. Undergoes a functional cycle that is linked to its ATPase activity (By similarity). Interacts dynamically with various co-chaperones that modulate its substrate recognition, ATPase cycle and chaperone function. Required for growth at high temperatures.</text>
+</comment>
+<comment type="subunit">
+<text evidence="2 5 6">Interacts with the co-chaperone SGT1. Interacts directly with the substrate CNA2. Interacts with NAP1.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-37072">
+<id>Q12449</id>
+<label>AHA1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-2883">
+<id>P08566</id>
+<label>ARO1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-4806">
+<id>P33313</id>
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+<organismsDiffer>false</organismsDiffer>
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+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-5436">
+<id>P47103</id>
+<label>CPR7</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-13796">
+<id>P53043</id>
+<label>PPT1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-21365">
+<id>P38164</id>
+<label>SEA4</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-1797">
+<id>Q02821</id>
+<label>SRP1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-8591">
+<id>P10591</id>
+<label>SSA1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8666">
+<id>P15108</id>
+</interactant>
+<interactant intactId="EBI-18418">
+<id>P15705</id>
+<label>STI1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Mitochondrion</location>
+</subcellularLocation>
+</comment>
+<comment type="induction">
+<text evidence="7 9">Expressed constitutively at a high level and is moderately induced by high temperatures dependent on transcription factor HSF1.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 132053 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="10">Belongs to the heat shock protein 90 family.</text>
+</comment>
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+<property type="protein sequence ID" value="AAA02813.1"/>
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+<property type="protein sequence ID" value="CAA89919.1"/>
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+<dbReference type="Reactome" id="R-SCE-5218920">
+<property type="pathway name" value="VEGFR2 mediated vascular permeability"/>
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+<dbReference type="Reactome" id="R-SCE-6798695">
+<property type="pathway name" value="Neutrophil degranulation"/>
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+<dbReference type="Reactome" id="R-SCE-844456">
+<property type="pathway name" value="The NLRP3 inflammasome"/>
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+<keyword id="KW-0677">Repeat</keyword>
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+</entry>
+<entry dataset="Swiss-Prot" created="1989-07-01" modified="2021-04-07" version="225">
+<accession>P10591</accession>
+<accession>D6VPL2</accession>
+<name>HSP71_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Heat shock protein SSA1</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Heat shock protein YG100</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">SSA1</name>
+<name type="ordered locus">YAL005C</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1989" name="Nucleic Acids Res." volume="17" first="805" last="806">
+<title>The SSA1 and SSA2 genes of the yeast Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Slater M.R."/>
+<person name="Craig E.A."/>
+</authorList>
+<dbReference type="PubMed" id="2644626"/>
+<dbReference type="DOI" id="10.1093/nar/17.2.805"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="submission" date="1993-06" db="EMBL/GenBank/DDBJ databases">
+<authorList>
+<person name="Slater M.R."/>
+</authorList>
+</citation>
+<scope>SEQUENCE REVISION TO 208; 418 AND 422</scope>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1994" name="Yeast" volume="10" first="535" last="541">
+<title>Sequencing of chromosome I of Saccharomyces cerevisiae: analysis of the 42 kbp SPO7-CENI-CDC15 region.</title>
+<authorList>
+<person name="Clark M.W."/>
+<person name="Keng T."/>
+<person name="Storms R.K."/>
+<person name="Zhong W.-W."/>
+<person name="Fortin N."/>
+<person name="Zeng B."/>
+<person name="Delaney S."/>
+<person name="Ouellette B.F.F."/>
+<person name="Barton A.B."/>
+<person name="Kaback D.B."/>
+<person name="Bussey H."/>
+</authorList>
+<dbReference type="PubMed" id="7941740"/>
+<dbReference type="DOI" id="10.1002/yea.320100413"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204511 / S288c / AB972</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1995" name="Proc. Natl. Acad. Sci. U.S.A." volume="92" first="3809" last="3813">
+<title>The nucleotide sequence of chromosome I from Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Kaback D.B."/>
+<person name="Zhong W.-W."/>
+<person name="Vo D.H."/>
+<person name="Clark M.W."/>
+<person name="Fortin N."/>
+<person name="Hall J."/>
+<person name="Ouellette B.F.F."/>
+<person name="Keng T."/>
+<person name="Barton A.B."/>
+<person name="Su Y."/>
+<person name="Davies C.J."/>
+<person name="Storms R.K."/>
+</authorList>
+<dbReference type="PubMed" id="7731988"/>
+<dbReference type="DOI" id="10.1073/pnas.92.9.3809"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1994" name="Electrophoresis" volume="15" first="1466" last="1486">
+<title>Protein identifications for a Saccharomyces cerevisiae protein database.</title>
+<authorList>
+<person name="Garrels J.I."/>
+<person name="Futcher B."/>
+<person name="Kobayashi R."/>
+<person name="Latter G.I."/>
+<person name="Schwender B."/>
+<person name="Volpe T."/>
+<person name="Warner J.R."/>
+<person name="McLaughlin C.S."/>
+</authorList>
+<dbReference type="PubMed" id="7895733"/>
+<dbReference type="DOI" id="10.1002/elps.11501501210"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 92-98 AND 326-342</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="7">
+<citation type="journal article" date="1996" name="FEMS Microbiol. Lett." volume="137" first="1" last="8">
+<title>Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Norbeck J."/>
+<person name="Blomberg A."/>
+</authorList>
+<dbReference type="PubMed" id="8935650"/>
+<dbReference type="DOI" id="10.1111/j.1574-6968.1996.tb08073.x"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 187-196</scope>
+<source>
+<strain>ATCC 38531 / Y41</strain>
+</source>
+</reference>
+<reference key="8">
+<citation type="journal article" date="1984" name="Nucleic Acids Res." volume="12" first="9367" last="9382">
+<title>Transfer RNA splicing in Saccharomyces cerevisiae: defining the substrates.</title>
+<authorList>
+<person name="Ogden R.C."/>
+<person name="Lee M.-C."/>
+<person name="Knapp G."/>
+</authorList>
+<dbReference type="PubMed" id="6096826"/>
+<dbReference type="DOI" id="10.1093/nar/12.24.9367"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 591-642</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="1997" name="Electrophoresis" volume="18" first="1347" last="1360">
+<title>Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins.</title>
+<authorList>
+<person name="Garrels J.I."/>
+<person name="McLaughlin C.S."/>
+<person name="Warner J.R."/>
+<person name="Futcher B."/>
+<person name="Latter G.I."/>
+<person name="Kobayashi R."/>
+<person name="Schwender B."/>
+<person name="Volpe T."/>
+<person name="Anderson D.S."/>
+<person name="Mesquita-Fuentes R."/>
+<person name="Payne W.E."/>
+</authorList>
+<dbReference type="PubMed" id="9298649"/>
+<dbReference type="DOI" id="10.1002/elps.1150180810"/>
+</citation>
+<scope>ACETYLATION AT SER-2</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2001" name="J. Biol. Chem." volume="276" first="14426" last="14433">
+<title>The yeast hsp70 homologue Ssa is required for translation and interacts with Sis1 and Pab1 on translating ribosomes.</title>
+<authorList>
+<person name="Horton L.E."/>
+<person name="James P."/>
+<person name="Craig E.A."/>
+<person name="Hensold J.O."/>
+</authorList>
+<dbReference type="PubMed" id="11279042"/>
+<dbReference type="DOI" id="10.1074/jbc.m100266200"/>
+</citation>
+<scope>INTERACTION WITH PAB1 AND SIS1</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2003" name="J. Biol. Chem." volume="278" first="28553" last="28561">
+<title>Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5.</title>
+<authorList>
+<person name="Li X.S."/>
+<person name="Reddy M.S."/>
+<person name="Baev D."/>
+<person name="Edgerton M."/>
+</authorList>
+<dbReference type="PubMed" id="12761219"/>
+<dbReference type="DOI" id="10.1074/jbc.m300680200"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH HUMAN HTN3</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="15">
+<citation type="journal article" date="2008" name="Mol. Cell. Biol." volume="28" first="1313" last="1325">
+<title>Phosphorylation by casein kinase 2 regulates Nap1 localization and function.</title>
+<authorList>
+<person name="Calvert M.E.K."/>
+<person name="Keck K.M."/>
+<person name="Ptak C."/>
+<person name="Shabanowitz J."/>
+<person name="Hunt D.F."/>
+<person name="Pemberton L.F."/>
+</authorList>
+<dbReference type="PubMed" id="18086883"/>
+<dbReference type="DOI" id="10.1128/mcb.01035-07"/>
+</citation>
+<scope>INTERACTION WITH NAP1</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="16">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-62 AND SER-603</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="17">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-551</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="18">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="2">May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA1 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.</text>
+</comment>
+<comment type="subunit">
+<text evidence="1 2 5">Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity. Interacts with polyadenylate-binding protein PAB1 and Hsp70 chaperone SSA1 on translating ribosomes. Interacts with NAP1.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8591">
+<id>P10591</id>
+</interactant>
+<interactant intactId="EBI-2612341">
+<id>P53940</id>
+<label>APJ1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8591">
+<id>P10591</id>
+</interactant>
+<interactant intactId="EBI-4762">
+<id>P35190</id>
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+<interactant intactId="EBI-8666">
+<id>P15108</id>
+<label>HSC82</label>
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+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8591">
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+</interactant>
+<interactant intactId="EBI-8680">
+<id>P33416</id>
+<label>HSP78</label>
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+<organismsDiffer>false</organismsDiffer>
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+<comment type="interaction">
+<interactant intactId="EBI-8591">
+<id>P10591</id>
+</interactant>
+<interactant intactId="EBI-8659">
+<id>P02829</id>
+<label>HSP82</label>
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+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
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+<comment type="interaction">
+<interactant intactId="EBI-8591">
+<id>P10591</id>
+</interactant>
+<interactant intactId="EBI-4499">
+<id>P25693</id>
+<label>PCL2</label>
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+<organismsDiffer>false</organismsDiffer>
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+<comment type="interaction">
+<interactant intactId="EBI-8591">
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+<interactant intactId="EBI-13327">
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+<organismsDiffer>false</organismsDiffer>
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+<interactant intactId="EBI-8591">
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+<interactant intactId="EBI-13914">
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+<organismsDiffer>false</organismsDiffer>
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+<comment type="interaction">
+<interactant intactId="EBI-8591">
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+<interactant intactId="EBI-17244">
+<id>P25294</id>
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+<organismsDiffer>false</organismsDiffer>
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+<interactant intactId="EBI-8648">
+<id>P32589</id>
+<label>SSE1</label>
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+<organismsDiffer>false</organismsDiffer>
+<experiments>8</experiments>
+</comment>
+<comment type="subcellular location">
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+</subcellularLocation>
+<subcellularLocation>
+<location evidence="3">Secreted</location>
+<location evidence="3">Cell wall</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 269000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="7">Belongs to the heat shock protein 70 family.</text>
+</comment>
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+<property type="protein sequence ID" value="CAA31393.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="pathway name" value="Protein methylation"/>
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+<dbReference type="EvolutionaryTrace" id="P10591"/>
+<dbReference type="PRO" id="PR:P10591"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome I"/>
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+<property type="project" value="UniProtKB-KW"/>
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+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
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+<dbReference type="GO" id="GO:0016887">
+<property type="term" value="F:ATPase activity"/>
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+<dbReference type="GO" id="GO:0031072">
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+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
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+<dbReference type="GO" id="GO:0051787">
+<property type="term" value="F:misfolded protein binding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
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+<dbReference type="GO" id="GO:0044183">
+<property type="term" value="F:protein folding chaperone"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000049">
+<property type="term" value="F:tRNA binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
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+<dbReference type="GO" id="GO:0051082">
+<property type="term" value="F:unfolded protein binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0034620">
+<property type="term" value="P:cellular response to unfolded protein"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0051085">
+<property type="term" value="P:chaperone cofactor-dependent protein refolding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
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+<dbReference type="GO" id="GO:0072318">
+<property type="term" value="P:clathrin coat disassembly"/>
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+<dbReference type="GO" id="GO:0002181">
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+<property type="project" value="SGD"/>
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+<dbReference type="GO" id="GO:0072671">
+<property type="term" value="P:mitochondria-associated ubiquitin-dependent protein catabolic process"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
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+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
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+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
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+<person name="Pohl T.M."/>
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+<person name="Rinke M."/>
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+<person name="Scharfe M."/>
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+<person name="Scholler P."/>
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+<person name="Vandenbol M."/>
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+<person name="Latter G.I."/>
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+<title>Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.</title>
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+<person name="Blomberg A."/>
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+<title>Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins.</title>
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+<person name="McLaughlin C.S."/>
+<person name="Warner J.R."/>
+<person name="Futcher B."/>
+<person name="Latter G.I."/>
+<person name="Kobayashi R."/>
+<person name="Schwender B."/>
+<person name="Volpe T."/>
+<person name="Anderson D.S."/>
+<person name="Mesquita-Fuentes R."/>
+<person name="Payne W.E."/>
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+<title>Candida albicans Ssa1/2p is the cell envelope binding protein for human salivary histatin 5.</title>
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+<person name="Li X.S."/>
+<person name="Reddy M.S."/>
+<person name="Baev D."/>
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+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
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+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
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+<title>A proteomics approach to understanding protein ubiquitination.</title>
+<authorList>
+<person name="Peng J."/>
+<person name="Schwartz D."/>
+<person name="Elias J.E."/>
+<person name="Thoreen C.C."/>
+<person name="Cheng D."/>
+<person name="Marsischky G."/>
+<person name="Roelofs J."/>
+<person name="Finley D."/>
+<person name="Gygi S.P."/>
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+<strain>SUB592</strain>
+</source>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2008" name="Mol. Cell. Biol." volume="28" first="1313" last="1325">
+<title>Phosphorylation by casein kinase 2 regulates Nap1 localization and function.</title>
+<authorList>
+<person name="Calvert M.E.K."/>
+<person name="Keck K.M."/>
+<person name="Ptak C."/>
+<person name="Shabanowitz J."/>
+<person name="Hunt D.F."/>
+<person name="Pemberton L.F."/>
+</authorList>
+<dbReference type="PubMed" id="18086883"/>
+<dbReference type="DOI" id="10.1128/mcb.01035-07"/>
+</citation>
+<scope>INTERACTION WITH NAP1</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="15">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="16">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-556</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="2">May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A functional difference between SSA1 and SSA2 proteins is expected. SSA2 can participate in the ATP-dependent disassembly of clathrin-coated vesicles.</text>
+</comment>
+<comment type="subunit">
+<text evidence="2 4">Binds human HTN3/histatin-5, a peptide from saliva, and mediates its fungicidal activity. Interacts with NAP1.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8603">
+<id>P10592</id>
+</interactant>
+<interactant intactId="EBI-2612341">
+<id>P53940</id>
+<label>APJ1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8603">
+<id>P10592</id>
+</interactant>
+<interactant intactId="EBI-4912">
+<id>P18900</id>
+<label>COQ1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8603">
+<id>P10592</id>
+</interactant>
+<interactant intactId="EBI-6679">
+<id>P22696</id>
+<label>ESS1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8603">
+<id>P10592</id>
+</interactant>
+<interactant intactId="EBI-8659">
+<id>P02829</id>
+<label>HSP82</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8603">
+<id>P10592</id>
+</interactant>
+<interactant intactId="EBI-10594">
+<id>P17505</id>
+<label>MDH1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8603">
+<id>P10592</id>
+</interactant>
+<interactant intactId="EBI-17244">
+<id>P25294</id>
+<label>SIS1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Secreted</location>
+<location>Cell wall</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 364000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the heat shock protein 70 family.</text>
+</comment>
+<dbReference type="EMBL" id="X12927">
+<property type="protein sequence ID" value="CAA31394.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z73129">
+<property type="protein sequence ID" value="CAA97472.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X97560">
+<property type="protein sequence ID" value="CAA66167.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09296.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S20139">
+<property type="entry name" value="S20139"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013076.1">
+<property type="nucleotide sequence ID" value="NM_001181844.1"/>
+</dbReference>
+<dbReference type="SMR" id="P10592"/>
+<dbReference type="BioGRID" id="31229">
+<property type="interactions" value="465"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1276">
+<property type="entry name" value="HMC complex"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1883">
+<property type="entry name" value="HAP1 transcriptional repressor complex, SSA2 variant"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-2265N"/>
+<dbReference type="IntAct" id="P10592">
+<property type="interactions" value="972"/>
+</dbReference>
+<dbReference type="MINT" id="P10592"/>
+<dbReference type="STRING" id="4932.YLL024C"/>
+<dbReference type="CarbonylDB" id="P10592"/>
+<dbReference type="iPTMnet" id="P10592"/>
+<dbReference type="COMPLUYEAST-2DPAGE" id="P10592"/>
+<dbReference type="SWISS-2DPAGE" id="P10592"/>
+<dbReference type="MaxQB" id="P10592"/>
+<dbReference type="PaxDb" id="P10592"/>
+<dbReference type="PRIDE" id="P10592"/>
+<dbReference type="EnsemblFungi" id="YLL024C_mRNA">
+<property type="protein sequence ID" value="YLL024C"/>
+<property type="gene ID" value="YLL024C"/>
+</dbReference>
+<dbReference type="GeneID" id="850636"/>
+<dbReference type="KEGG" id="sce:YLL024C"/>
+<dbReference type="SGD" id="S000003947">
+<property type="gene designation" value="SSA2"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YLL024C"/>
+<dbReference type="eggNOG" id="KOG0101">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00940000176322"/>
+<dbReference type="HOGENOM" id="CLU_005965_7_0_1"/>
+<dbReference type="InParanoid" id="P10592"/>
+<dbReference type="OMA" id="HIEVEYK"/>
+<dbReference type="Reactome" id="R-SCE-3371453">
+<property type="pathway name" value="Regulation of HSF1-mediated heat shock response"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-3371497">
+<property type="pathway name" value="HSP90 chaperone cycle for steroid hormone receptors (SHR)"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-3371571">
+<property type="pathway name" value="HSF1-dependent transactivation"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-6798695">
+<property type="pathway name" value="Neutrophil degranulation"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-8856828">
+<property type="pathway name" value="Clathrin-mediated endocytosis"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-8876725">
+<property type="pathway name" value="Protein methylation"/>
+</dbReference>
+<dbReference type="PRO" id="PR:P10592"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XII"/>
+</dbReference>
+<dbReference type="RNAct" id="P10592">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005576">
+<property type="term" value="C:extracellular region"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0009277">
+<property type="term" value="C:fungal-type cell wall"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000329">
+<property type="term" value="C:fungal-type vacuole membrane"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005739">
+<property type="term" value="C:mitochondrion"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005886">
+<property type="term" value="C:plasma membrane"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005844">
+<property type="term" value="C:polysome"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0016887">
+<property type="term" value="F:ATPase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0031072">
+<property type="term" value="F:heat shock protein binding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0051787">
+<property type="term" value="F:misfolded protein binding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0044183">
+<property type="term" value="F:protein folding chaperone"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000049">
+<property type="term" value="F:tRNA binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0051082">
+<property type="term" value="F:unfolded protein binding"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0034620">
+<property type="term" value="P:cellular response to unfolded protein"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0051085">
+<property type="term" value="P:chaperone cofactor-dependent protein refolding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0090344">
+<property type="term" value="P:negative regulation of cell aging"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0043161">
+<property type="term" value="P:proteasome-mediated ubiquitin-dependent protein catabolic process"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006457">
+<property type="term" value="P:protein folding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0042026">
+<property type="term" value="P:protein refolding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006616">
+<property type="term" value="P:SRP-dependent cotranslational protein targeting to membrane, translocation"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0035719">
+<property type="term" value="P:tRNA import into nucleus"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0016192">
+<property type="term" value="P:vesicle-mediated transport"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="Gene3D" id="1.20.1270.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="2.60.34.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043129">
+<property type="entry name" value="ATPase_NBD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR018181">
+<property type="entry name" value="Heat_shock_70_CS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR029048">
+<property type="entry name" value="HSP70_C_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR029047">
+<property type="entry name" value="HSP70_peptide-bd_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013126">
+<property type="entry name" value="Hsp_70_fam"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR19375">
+<property type="entry name" value="PTHR19375"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00012">
+<property type="entry name" value="HSP70"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF100920">
+<property type="entry name" value="SSF100920"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF100934">
+<property type="entry name" value="SSF100934"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53067">
+<property type="entry name" value="SSF53067"/>
+<property type="match status" value="2"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00297">
+<property type="entry name" value="HSP70_1"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00329">
+<property type="entry name" value="HSP70_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS01036">
+<property type="entry name" value="HSP70_3"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0134">Cell wall</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0964">Secreted</keyword>
+<keyword id="KW-0346">Stress response</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="5 9">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="Heat shock protein SSA2" id="PRO_0000078386">
+<location>
+<begin position="2"/>
+<end position="639"/>
+</location>
+</feature>
+<feature type="modified residue" description="N-acetylserine" evidence="5 9">
+<location>
+<position position="2"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="7">
+<location>
+<position position="20"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="1">
+<location>
+<position position="551"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="1">
+<location>
+<position position="603"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="8">
+<location>
+<position position="556"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="P10591"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="12761219"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="18086883"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="9298649"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000305"/>
+<evidence key="7" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="18407956"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22106047"/>
+</source>
+</evidence>
+<evidence key="9" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22814378"/>
+</source>
+</evidence>
+<sequence length="639" mass="69470" checksum="129049E21C9DD1F3" modified="2007-01-23" version="3">MSKAVGIDLGTTYSCVAHFSNDRVDIIANDQGNRTTPSFVGFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRNFNDPEVQGDMKHFPFKLIDVDGKPQIQVEFKGETKNFTPEQISSMVLGKMKETAESYLGAKVNDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGKEEHVLIFDLGGGTFDVSLLSIEDGIFEVKATAGDTHLGGEDFDNRLVNHFIQEFKRKNKKDLSTNQRALRRLRTACERAKRTLSSSAQTSVEIDSLFEGIDFYTSITRARFEELCADLFRSTLDPVEKVLRDAKLDKSQVDEIVLVGGSTRIPKVQKLVTDYFNGKEPNRSINPDEAVAYGAAVQAAILTGDESSKTQDLLLLDVAPLSLGIETAGGVMTKLIPRNSTIPTKKSEVFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDVDSNGILNVSAVEKGTGKSNKITITNDKGRLSKEDIEKMVAEAEKFKEEDEKESQRIASKNQLESIAYSLKNTISEAGDKLEQADKDAVTKKAEETIAWLDSNTTATKEEFDDQLKELQEVANPIMSKLYQAGGAPEGAAPGGFPGGAPPAPEAEGPTVEEVD</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2012-06-13" modified="2021-04-07" version="77">
+<accession>P0CS90</accession>
+<accession>D6VWL6</accession>
+<accession>P12398</accession>
+<name>HSP77_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="10">Import motor subunit, mitochondrial</fullName>
+<ecNumber evidence="1">3.6.4.10</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName evidence="10">Endonuclease SceI 75 kDa subunit</fullName>
+<shortName evidence="10">Endo.SceI 75 kDa subunit</shortName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="10">mtHSP70</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="9 11">SSC1</name>
+<name type="synonym" evidence="11">ENS1</name>
+<name type="ordered locus">YJR045C</name>
+<name type="ORF">J1639</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
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+<citation type="journal article" date="1989" name="Mol. Cell. Biol." volume="9" first="3000" last="3008">
+<title>SSC1, an essential member of the yeast HSP70 multigene family, encodes a mitochondrial protein.</title>
+<authorList>
+<person name="Craig E.A."/>
+<person name="Kramer J."/>
+<person name="Shilling J."/>
+<person name="Werner-Washburne M."/>
+<person name="Holmes S."/>
+<person name="Kosic-Smithers J."/>
+<person name="Nicolet C.M."/>
+</authorList>
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+<dbReference type="DOI" id="10.1128/mcb.9.7.3000"/>
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+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 24657 / D273-10B</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="775" last="781">
+<title>Analysis of a 42.5 kb DNA sequence of chromosome X reveals three tRNA genes and 14 new open reading frames including a gene most probably belonging to the family of ubiquitin-protein ligases.</title>
+<authorList>
+<person name="Huang M.-E."/>
+<person name="Chuat J.-C."/>
+<person name="Galibert F."/>
+</authorList>
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+<dbReference type="DOI" id="10.1002/yea.320110809"/>
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+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
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+<authorList>
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+<person name="Chuat J.-C."/>
+<person name="Coster F."/>
+<person name="Cziepluch C."/>
+<person name="de Haan M."/>
+<person name="Domdey H."/>
+<person name="Durand P."/>
+<person name="Entian K.-D."/>
+<person name="Gatius M."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="Hennemann A."/>
+<person name="Herbert C.J."/>
+<person name="Heumann K."/>
+<person name="Hilger F."/>
+<person name="Hollenberg C.P."/>
+<person name="Huang M.-E."/>
+<person name="Jacq C."/>
+<person name="Jauniaux J.-C."/>
+<person name="Katsoulou C."/>
+<person name="Kirchrath L."/>
+<person name="Kleine K."/>
+<person name="Kordes E."/>
+<person name="Koetter P."/>
+<person name="Liebl S."/>
+<person name="Louis E.J."/>
+<person name="Manus V."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Obermaier B."/>
+<person name="Perea J."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rasmussen S.W."/>
+<person name="Rose M."/>
+<person name="Rossau R."/>
+<person name="Schaaff-Gerstenschlaeger I."/>
+<person name="Smits P.H.M."/>
+<person name="Scarcez T."/>
+<person name="Soriano N."/>
+<person name="To Van D."/>
+<person name="Tzermia M."/>
+<person name="Van Broekhoven A."/>
+<person name="Vandenbol M."/>
+<person name="Wedler H."/>
+<person name="von Wettstein D."/>
+<person name="Wambutt R."/>
+<person name="Zagulski M."/>
+<person name="Zollner A."/>
+<person name="Karpfinger-Hartl L."/>
+</authorList>
+<dbReference type="PubMed" id="8641269"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1996.tb00557.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1990" name="EMBO J." volume="9" first="4315" last="4322">
+<title>A precursor protein partly translocated into yeast mitochondria is bound to a 70 kd mitochondrial stress protein.</title>
+<authorList>
+<person name="Scherer P.E."/>
+<person name="Krieg U.C."/>
+<person name="Hwang S.T."/>
+<person name="Vestweber D."/>
+<person name="Schatz G."/>
+</authorList>
+<dbReference type="PubMed" id="2265609"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1990.tb07880.x"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 24-38</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+<source>
+<strain>ATCC 24657 / D273-10B</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1995" name="Adv. Biophys." volume="31" first="77" last="91">
+<title>Multi-site-specific endonucleases and the initiation of homologous genetic recombination in yeast.</title>
+<authorList>
+<person name="Shibata T."/>
+<person name="Nakagawa K."/>
+<person name="Morishima N."/>
+</authorList>
+<dbReference type="PubMed" id="7625280"/>
+<dbReference type="DOI" id="10.1016/0065-227x(95)99384-2"/>
+</citation>
+<scope>FUNCTION OF ENDONUCLEASE SCEI</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2000" name="Mol. Cell. Biol." volume="20" first="3677" last="3684">
+<title>Role of the mitochondrial Hsp70s, Ssc1 and Ssq1, in the maturation of Yfh1.</title>
+<authorList>
+<person name="Voisine C."/>
+<person name="Schilke B."/>
+<person name="Ohlson M."/>
+<person name="Beinert H."/>
+<person name="Marszalek J."/>
+<person name="Craig E.A."/>
+</authorList>
+<dbReference type="PubMed" id="10779357"/>
+<dbReference type="DOI" id="10.1128/mcb.20.10.3677-3684.2000"/>
+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2002" name="EMBO J." volume="21" first="2626" last="2635">
+<title>The Hsp70 peptide-binding domain determines the interaction of the ATPase domain with Tim44 in mitochondria.</title>
+<authorList>
+<person name="Strub A."/>
+<person name="Roettgers K."/>
+<person name="Voos W."/>
+</authorList>
+<dbReference type="PubMed" id="12032075"/>
+<dbReference type="DOI" id="10.1093/emboj/21.11.2626"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH TIM44</scope>
+<scope>MUTAGENESIS OF PRO-442</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2003" name="EMBO J." volume="22" first="4945" last="4956">
+<title>Tim14, a novel key component of the import motor of the TIM23 protein translocase of mitochondria.</title>
+<authorList>
+<person name="Mokranjac D."/>
+<person name="Sichting M."/>
+<person name="Neupert W."/>
+<person name="Hell K."/>
+</authorList>
+<dbReference type="PubMed" id="14517234"/>
+<dbReference type="DOI" id="10.1093/emboj/cdg485"/>
+</citation>
+<scope>INTERACTION WITH PAM18</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2005" name="Mol. Cell. Biol." volume="25" first="7449" last="7458">
+<title>Pam17 is required for architecture and translocation activity of the mitochondrial protein import motor.</title>
+<authorList>
+<person name="van der Laan M."/>
+<person name="Chacinska A."/>
+<person name="Lind M."/>
+<person name="Perschil I."/>
+<person name="Sickmann A."/>
+<person name="Meyer H.E."/>
+<person name="Guiard B."/>
+<person name="Meisinger C."/>
+<person name="Pfanner N."/>
+<person name="Rehling P."/>
+</authorList>
+<dbReference type="PubMed" id="16107694"/>
+<dbReference type="DOI" id="10.1128/mcb.25.17.7449-7458.2005"/>
+</citation>
+<scope>IDENTIFICATION IN THE PAM COMPLEX WITH PAM16; PAM17; PAM18; TIM44 AND MGE1</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2007" name="Mol. Cell. Proteomics" volume="6" first="1896" last="1906">
+<title>Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.</title>
+<authorList>
+<person name="Reinders J."/>
+<person name="Wagner K."/>
+<person name="Zahedi R.P."/>
+<person name="Stojanovski D."/>
+<person name="Eyrich B."/>
+<person name="van der Laan M."/>
+<person name="Rehling P."/>
+<person name="Sickmann A."/>
+<person name="Pfanner N."/>
+<person name="Meisinger C."/>
+</authorList>
+<dbReference type="PubMed" id="17761666"/>
+<dbReference type="DOI" id="10.1074/mcp.m700098-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-330</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ATCC 76625 / YPH499</strain>
+</source>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2008" name="Mol. Cell. Biol." volume="28" first="1313" last="1325">
+<title>Phosphorylation by casein kinase 2 regulates Nap1 localization and function.</title>
+<authorList>
+<person name="Calvert M.E.K."/>
+<person name="Keck K.M."/>
+<person name="Ptak C."/>
+<person name="Shabanowitz J."/>
+<person name="Hunt D.F."/>
+<person name="Pemberton L.F."/>
+</authorList>
+<dbReference type="PubMed" id="18086883"/>
+<dbReference type="DOI" id="10.1128/mcb.01035-07"/>
+</citation>
+<scope>INTERACTION WITH NAP1</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="15">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="2 3 8">Essential component of the PAM complex, a complex required for the translocation of transit peptide-containing proteins from the inner membrane into the mitochondrial matrix in an ATP-dependent manner. Constitutes the ATP-driven core of the motor and binds the precursor preprotein. Required for the import of the processed frataxin homolog YFH1 into the mitochondrion.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="1">
+<text>ATP + H2O = ADP + H(+) + phosphate</text>
+<dbReference type="Rhea" id="RHEA:13065"/>
+<dbReference type="ChEBI" id="CHEBI:15377"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:30616"/>
+<dbReference type="ChEBI" id="CHEBI:43474"/>
+<dbReference type="ChEBI" id="CHEBI:456216"/>
+<dbReference type="EC" id="3.6.4.10"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="3 4 5 6">Component of the PAM complex, at least composed of SSC1 (mtHsp70), MGE1, TIM44, PAM16/TIM16, PAM17 and PAM18/TIM14. In the complex, SSC1 interacts directly with PAM18 and TIM44. Interacts with NAP1.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8637">
+<id>P0CS90</id>
+</interactant>
+<interactant intactId="EBI-21547">
+<id>P38257</id>
+<label>MMS4</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8637">
+<id>P0CS90</id>
+</interactant>
+<interactant intactId="EBI-19517">
+<id>P53632</id>
+<label>PAP2</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8637">
+<id>P0CS90</id>
+</interactant>
+<interactant intactId="EBI-14780">
+<id>P06779</id>
+<label>RAD7</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8637">
+<id>P0CS90</id>
+</interactant>
+<interactant intactId="EBI-16977">
+<id>P38827</id>
+<label>SET1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8637">
+<id>P0CS90</id>
+</interactant>
+<interactant intactId="EBI-9141">
+<id>Q01852</id>
+<label>TIM44</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8637">
+<id>P0CS90</id>
+</interactant>
+<interactant intactId="EBI-6490">
+<id>P12294</id>
+<label>ENS2</label>
+</interactant>
+<organismsDiffer>true</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="7">Mitochondrion matrix</location>
+</subcellularLocation>
+</comment>
+<comment type="similarity">
+<text evidence="10">Belongs to the heat shock protein 70 family.</text>
+</comment>
+<comment type="caution">
+<text evidence="10">S.cerevisiae displays strain polymorphism with regard to Endo.SceI endouclease activity. This is due to the mitochondrion-encoded, catalytic subunit ENS2, which exhibits strain polymorphism. It can be either present as continuous ORF in the mitochondrial genome (e.g. strain IAM 4274), present but disrupted by the insertion of GC clusters (e.g. strain D273-10B/A), or completely absent in the mitochondrial genome (e.g. strain S288c). Sequences for the 2 subunits ENS2 (AC P12294) and SSC1 (AC P0CS91) for an active Endo.SceI endonuclease can be found in strain IAM 4274.</text>
+</comment>
+<dbReference type="EC" id="3.6.4.10" evidence="1"/>
+<dbReference type="EMBL" id="M27229">
+<property type="protein sequence ID" value="AAA63792.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="L36344">
+<property type="protein sequence ID" value="AAA88747.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z49545">
+<property type="protein sequence ID" value="CAA89573.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006943">
+<property type="protein sequence ID" value="DAA08832.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="A32493">
+<property type="entry name" value="HHBYS1"/>
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+<dbReference type="RefSeq" id="NP_012579.1">
+<property type="nucleotide sequence ID" value="NM_001181703.1"/>
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+<dbReference type="SMR" id="P0CS90"/>
+<dbReference type="BioGRID" id="33797">
+<property type="interactions" value="960"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1423">
+<property type="entry name" value="COX1 pre-assembly complex"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1741">
+<property type="entry name" value="Endonuclease SceI"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-539">
+<property type="entry name" value="TIM23 mitochondrial inner membrane pre-sequence translocase complex, motor variant"/>
+</dbReference>
+<dbReference type="IntAct" id="P0CS90">
+<property type="interactions" value="216"/>
+</dbReference>
+<dbReference type="MINT" id="P0CS90"/>
+<dbReference type="STRING" id="4932.YJR045C"/>
+<dbReference type="iPTMnet" id="P0CS90"/>
+<dbReference type="MaxQB" id="P0CS90"/>
+<dbReference type="PaxDb" id="P0CS90"/>
+<dbReference type="PRIDE" id="P0CS90"/>
+<dbReference type="EnsemblFungi" id="YJR045C_mRNA">
+<property type="protein sequence ID" value="YJR045C"/>
+<property type="gene ID" value="YJR045C"/>
+</dbReference>
+<dbReference type="GeneID" id="853503"/>
+<dbReference type="KEGG" id="sce:YJR045C"/>
+<dbReference type="SGD" id="S000003806">
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+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.</title>
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+<person name="Churcher C.M."/>
+<person name="Bowman S."/>
+<person name="Badcock K."/>
+<person name="Bankier A.T."/>
+<person name="Brown D."/>
+<person name="Chillingworth T."/>
+<person name="Connor R."/>
+<person name="Devlin K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Harris D.E."/>
+<person name="Horsnell T."/>
+<person name="Hunt S."/>
+<person name="Jagels K."/>
+<person name="Jones M."/>
+<person name="Lye G."/>
+<person name="Moule S."/>
+<person name="Odell C."/>
+<person name="Pearson D."/>
+<person name="Rajandream M.A."/>
+<person name="Rice P."/>
+<person name="Rowley N."/>
+<person name="Skelton J."/>
+<person name="Smith V."/>
+<person name="Walsh S.V."/>
+<person name="Whitehead S."/>
+<person name="Barrell B.G."/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
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+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
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+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
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+<dbReference type="DOI" id="10.1038/nature02026"/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
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+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
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+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="13207" last="13212">
+<title>The proteome of Saccharomyces cerevisiae mitochondria.</title>
+<authorList>
+<person name="Sickmann A."/>
+<person name="Reinders J."/>
+<person name="Wagner Y."/>
+<person name="Joppich C."/>
+<person name="Zahedi R.P."/>
+<person name="Meyer H.E."/>
+<person name="Schoenfisch B."/>
+<person name="Perschil I."/>
+<person name="Chacinska A."/>
+<person name="Guiard B."/>
+<person name="Rehling P."/>
+<person name="Pfanner N."/>
+<person name="Meisinger C."/>
+</authorList>
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+<dbReference type="DOI" id="10.1073/pnas.2135385100"/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2014" name="EMBO J." volume="33" first="1624" last="1638">
+<title>The INA complex facilitates assembly of the peripheral stalk of the mitochondrial F1Fo-ATP synthase.</title>
+<authorList>
+<person name="Lytovchenko O."/>
+<person name="Naumenko N."/>
+<person name="Oeljeklaus S."/>
+<person name="Schmidt B."/>
+<person name="von der Malsburg K."/>
+<person name="Deckers M."/>
+<person name="Warscheid B."/>
+<person name="van der Laan M."/>
+<person name="Rehling P."/>
+</authorList>
+<dbReference type="PubMed" id="24942160"/>
+<dbReference type="DOI" id="10.15252/embj.201488076"/>
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+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH INA17</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+<scope>TOPOLOGY</scope>
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+</comment>
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+<text evidence="3">Component of the inner membrane assembly (INA) complex, composed of INA17 and INA22. Interacts with a subset of F(1)F(0)-ATP synthase subunits of the F(1)-domain and the peripheral stalk.</text>
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+<topology evidence="1">Single-pass membrane protein</topology>
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+<text evidence="2">Present with 589 molecules/cell in log phase SD medium.</text>
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+<title>Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae.</title>
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+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="9">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="induction">
+<text evidence="19 25">Expressed constitutively and induced by high temperatures dependent on transcription factor HSF1. According to PubMed:2674684, it is constitutively expressed at low levels, however, due to the specificity of the antibody, this result is unsure.</text>
+</comment>
+<comment type="domain">
+<text>The TPR repeat-binding motif mediates interaction with TPR repeat-containing proteins like the co-chaperones AHA1, CDC37, CNS1, CPR6, CPR7, HCH1, SBA1, SSE1 and STI1. CNS1, CPR6, CPR7 and STI1.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="10">Present with 444943 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="31">Belongs to the heat shock protein 90 family.</text>
+</comment>
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+</entry>
+<entry dataset="Swiss-Prot" created="1993-10-01" modified="2021-04-07" version="204">
+<accession>P32589</accession>
+<accession>D6W3R1</accession>
+<name>HSP7F_YEAST</name>
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+<fullName>Heat shock protein homolog SSE1</fullName>
+</recommendedName>
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+<fullName>Chaperone protein MSI3</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">SSE1</name>
+<name type="synonym">MSI3</name>
+<name type="ordered locus">YPL106C</name>
+<name type="ORF">LPG3C</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
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+<citation type="journal article" date="1993" name="Gene" volume="132" first="57" last="66">
+<title>Isolation and characterization of SSE1 and SSE2, new members of the yeast HSP70 multigene family.</title>
+<authorList>
+<person name="Mukai H."/>
+<person name="Kuno T."/>
+<person name="Tanaka H."/>
+<person name="Hirata D."/>
+<person name="Miyakawa T."/>
+<person name="Tanaka C."/>
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+<dbReference type="DOI" id="10.1016/0378-1119(93)90514-4"/>
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+<strain>ATCC 204626 / S288c / A364A</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1993" name="Mol. Gen. Genet." volume="240" first="323" last="332">
+<title>MSI3, a multicopy suppressor of mutants hyperactivated in the RAS-cAMP pathway, encodes a novel HSP70 protein of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Shirayama M."/>
+<person name="Kawakami K."/>
+<person name="Matsui Y."/>
+<person name="Tanaka K."/>
+<person name="Toh-e A."/>
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+<dbReference type="DOI" id="10.1007/bf00280382"/>
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+<reference key="3">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
+<person name="Albermann K."/>
+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
+<person name="Brueckner M."/>
+<person name="Carpenter J."/>
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+<person name="Fritz C."/>
+<person name="Goffeau A."/>
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+<person name="Heumann K."/>
+<person name="Hilbert H."/>
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+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
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+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Roberts D."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
+<person name="Ushinsky S."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Voss H."/>
+<person name="Walsh S.V."/>
+<person name="Wambutt R."/>
+<person name="Wang Y."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Winnett E."/>
+<person name="Zhong W.-W."/>
+<person name="Zollner A."/>
+<person name="Vo D.H."/>
+<person name="Hani J."/>
+</authorList>
+<dbReference type="PubMed" id="9169875"/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
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+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1994" name="Electrophoresis" volume="15" first="1466" last="1486">
+<title>Protein identifications for a Saccharomyces cerevisiae protein database.</title>
+<authorList>
+<person name="Garrels J.I."/>
+<person name="Futcher B."/>
+<person name="Kobayashi R."/>
+<person name="Latter G.I."/>
+<person name="Schwender B."/>
+<person name="Volpe T."/>
+<person name="Warner J.R."/>
+<person name="McLaughlin C.S."/>
+</authorList>
+<dbReference type="PubMed" id="7895733"/>
+<dbReference type="DOI" id="10.1002/elps.11501501210"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 100-110</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1996" name="FEMS Microbiol. Lett." volume="137" first="1" last="8">
+<title>Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Norbeck J."/>
+<person name="Blomberg A."/>
+</authorList>
+<dbReference type="PubMed" id="8935650"/>
+<dbReference type="DOI" id="10.1111/j.1574-6968.1996.tb08073.x"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 330-339</scope>
+<source>
+<strain>ATCC 38531 / Y41</strain>
+</source>
+</reference>
+<reference key="7">
+<citation type="journal article" date="1997" name="Electrophoresis" volume="18" first="1347" last="1360">
+<title>Proteome studies of Saccharomyces cerevisiae: identification and characterization of abundant proteins.</title>
+<authorList>
+<person name="Garrels J.I."/>
+<person name="McLaughlin C.S."/>
+<person name="Warner J.R."/>
+<person name="Futcher B."/>
+<person name="Latter G.I."/>
+<person name="Kobayashi R."/>
+<person name="Schwender B."/>
+<person name="Volpe T."/>
+<person name="Anderson D.S."/>
+<person name="Mesquita-Fuentes R."/>
+<person name="Payne W.E."/>
+</authorList>
+<dbReference type="PubMed" id="9298649"/>
+<dbReference type="DOI" id="10.1002/elps.1150180810"/>
+</citation>
+<scope>ACETYLATION AT SER-2</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
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+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
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+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-242</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-660</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-195</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text>Has a calcium-dependent calmodulin-binding activity. Required for normal growth at various temperatures.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8648">
+<id>P32589</id>
+</interactant>
+<interactant intactId="EBI-8659">
+<id>P02829</id>
+<label>HSP82</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8648">
+<id>P32589</id>
+</interactant>
+<interactant intactId="EBI-17244">
+<id>P25294</id>
+<label>SIS1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
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+</comment>
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+</interactant>
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+<id>P10591</id>
+<label>SSA1</label>
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+</comment>
+<comment type="interaction">
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+<id>P11484</id>
+<label>SSB1</label>
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+</comment>
+<comment type="interaction">
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+<interactant intactId="EBI-629985">
+<id>P08107</id>
+<label>HSPA1B</label>
+</interactant>
+<organismsDiffer>true</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="induction">
+<text>Increases a few-fold upon upshift to 37 degrees Celsius.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 71700 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="4">Belongs to the heat shock protein 70 family.</text>
+</comment>
+<dbReference type="EMBL" id="D13319">
+<property type="protein sequence ID" value="BAA02576.1"/>
+<property type="molecule type" value="mRNA"/>
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+<dbReference type="EMBL" id="D38368">
+<property type="protein sequence ID" value="BAA07449.1"/>
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+<property type="protein sequence ID" value="BAA02888.1"/>
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+<property type="protein sequence ID" value="AAB68194.1"/>
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+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11327.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S46417">
+<property type="entry name" value="S46417"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_015219.1">
+<property type="nucleotide sequence ID" value="NM_001183920.1"/>
+</dbReference>
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+<title>Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.</title>
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+<person name="Baur A."/>
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+<authorList>
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+<person name="Patterson N."/>
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+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
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+<person name="Huh W.-K."/>
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+<authorList>
+<person name="Walsh P."/>
+<person name="Bursac D."/>
+<person name="Law Y.C."/>
+<person name="Cyr D."/>
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+<reference key="7">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
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+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<reference key="8">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
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+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
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+<person name="Vo D.H."/>
+<person name="Hani J."/>
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+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
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+</reference>
+<reference key="3">
+<citation type="submission" date="2005-06" db="UniProtKB">
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+<person name="Bienvenut W.V."/>
+<person name="Peters C."/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
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+<reference key="4">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
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+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
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+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
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+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
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+</reference>
+<reference key="6">
+<citation type="journal article" date="2004" name="J. Biol. Chem." volume="279" first="22030" last="22038">
+<title>Pil1p and Lsp1p negatively regulate the 3-phosphoinositide-dependent protein kinase-like kinase Pkh1p and downstream signaling pathways Pkc1p and Ypk1p.</title>
+<authorList>
+<person name="Zhang X."/>
+<person name="Lester R.L."/>
+<person name="Dickson R.C."/>
+</authorList>
+<dbReference type="PubMed" id="15016821"/>
+<dbReference type="DOI" id="10.1074/jbc.m400299200"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>PHOSPHORYLATION BY PKH1 AND PHK2</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2005" name="Mol. Cell. Proteomics" volume="4" first="310" last="327">
+<title>Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.</title>
+<authorList>
+<person name="Gruhler A."/>
+<person name="Olsen J.V."/>
+<person name="Mohammed S."/>
+<person name="Mortensen P."/>
+<person name="Faergeman N.J."/>
+<person name="Mann M."/>
+<person name="Jensen O.N."/>
+</authorList>
+<dbReference type="PubMed" id="15665377"/>
+<dbReference type="DOI" id="10.1074/mcp.m400219-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>YAL6B</strain>
+</source>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2006" name="Nature" volume="439" first="998" last="1003">
+<title>Eisosomes mark static sites of endocytosis.</title>
+<authorList>
+<person name="Walther T.C."/>
+<person name="Brickner J.H."/>
+<person name="Aguilar P.S."/>
+<person name="Bernales S."/>
+<person name="Pantoja C."/>
+<person name="Walter P."/>
+</authorList>
+<dbReference type="PubMed" id="16496001"/>
+<dbReference type="DOI" id="10.1038/nature04472"/>
+</citation>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
+<person name="Haas W."/>
+<person name="Villen J."/>
+<person name="Elias J.E."/>
+<person name="Gygi S.P."/>
+</authorList>
+<dbReference type="PubMed" id="17330950"/>
+<dbReference type="DOI" id="10.1021/pr060559j"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ADR376</strain>
+</source>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2009" name="Mol. Syst. Biol." volume="5" first="308" last="308">
+<title>Global analysis of the glycoproteome in Saccharomyces cerevisiae reveals new roles for protein glycosylation in eukaryotes.</title>
+<authorList>
+<person name="Kung L.A."/>
+<person name="Tao S.-C."/>
+<person name="Qian J."/>
+<person name="Smith M.G."/>
+<person name="Snyder M."/>
+<person name="Zhu H."/>
+</authorList>
+<dbReference type="PubMed" id="19756047"/>
+<dbReference type="DOI" id="10.1038/msb.2009.64"/>
+</citation>
+<scope>GLYCOSYLATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-233</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="3">Together with PIL1, main component of eisosomes, structures at the cell periphery underneath the plasma membrane that mark the site of endocytosis. Negative regulator of cell wall integrity (CWI) in unstressed cells, probably by inhibiting protein kinase PKH1/PHK2 activity and regulating their downstream CWI pathways PKC1-MAP kinase pathway and protein kinase YPK1 pathway. Activity may be regulated by the transient increase of sphingolipid long chain bases (LCBs) during heat stress.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-34978">
+<id>Q12230</id>
+</interactant>
+<interactant intactId="EBI-23225">
+<id>P53252</id>
+<label>PIL1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>6</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1 4">Cytoplasm</location>
+<location evidence="1 4">Cell cortex</location>
+</subcellularLocation>
+<text>Localizes at eisosomes, structures which colocalize with sites of protein and lipid endocytosis.</text>
+</comment>
+<comment type="PTM">
+<text evidence="3">Phosphorylated by PKH1 and PKH2. Phosphorylation is stimulated by sphingolipid long chain bases (LCBs).</text>
+</comment>
+<comment type="PTM">
+<text evidence="5">N-glycosylated.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 104485 molecules/cell in log phase SD medium.</text>
+</comment>
+<dbReference type="EMBL" id="U33335">
+<property type="protein sequence ID" value="AAB68101.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z48483">
+<property type="protein sequence ID" value="CAA88382.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z71255">
+<property type="protein sequence ID" value="CAA95037.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11424.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S52527">
+<property type="entry name" value="S52527"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_015321.1">
+<property type="nucleotide sequence ID" value="NM_001183818.1"/>
+</dbReference>
+<dbReference type="PDB" id="3PLT">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.90"/>
+<property type="chains" value="A/B/C=36-267"/>
+</dbReference>
+<dbReference type="PDBsum" id="3PLT"/>
+<dbReference type="SMR" id="Q12230"/>
+<dbReference type="BioGRID" id="36173">
+<property type="interactions" value="160"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-3993N"/>
+<dbReference type="IntAct" id="Q12230">
+<property type="interactions" value="56"/>
+</dbReference>
+<dbReference type="MINT" id="Q12230"/>
+<dbReference type="STRING" id="4932.YPL004C"/>
+<dbReference type="TCDB" id="8.A.148.1.1">
+<property type="family name" value="the plasma membrane organizing center, eisosome (eisosome) family"/>
+</dbReference>
+<dbReference type="iPTMnet" id="Q12230"/>
+<dbReference type="MaxQB" id="Q12230"/>
+<dbReference type="PaxDb" id="Q12230"/>
+<dbReference type="PRIDE" id="Q12230"/>
+<dbReference type="TopDownProteomics" id="Q12230"/>
+<dbReference type="EnsemblFungi" id="YPL004C_mRNA">
+<property type="protein sequence ID" value="YPL004C"/>
+<property type="gene ID" value="YPL004C"/>
+</dbReference>
+<dbReference type="GeneID" id="856103"/>
+<dbReference type="KEGG" id="sce:YPL004C"/>
+<dbReference type="SGD" id="S000005925">
+<property type="gene designation" value="LSP1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YPL004C"/>
+<dbReference type="eggNOG" id="ENOG502QQ1T">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00940000176685"/>
+<dbReference type="HOGENOM" id="CLU_046464_0_0_1"/>
+<dbReference type="InParanoid" id="Q12230"/>
+<dbReference type="OMA" id="NWVEQNA"/>
+<dbReference type="EvolutionaryTrace" id="Q12230"/>
+<dbReference type="PRO" id="PR:Q12230"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XVI"/>
+</dbReference>
+<dbReference type="RNAct" id="Q12230">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0071944">
+<property type="term" value="C:cell periphery"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032126">
+<property type="term" value="C:eisosome"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0036286">
+<property type="term" value="C:eisosome filament"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005741">
+<property type="term" value="C:mitochondrial outer membrane"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005739">
+<property type="term" value="C:mitochondrion"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005886">
+<property type="term" value="C:plasma membrane"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008289">
+<property type="term" value="F:lipid binding"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0070941">
+<property type="term" value="P:eisosome assembly"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006897">
+<property type="term" value="P:endocytosis"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006469">
+<property type="term" value="P:negative regulation of protein kinase activity"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0009408">
+<property type="term" value="P:response to heat"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="1.20.1270.60">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR027267">
+<property type="entry name" value="AH/BAR_dom_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR028245">
+<property type="entry name" value="PIL1/LSP1"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR31962">
+<property type="entry name" value="PTHR31962"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF13805">
+<property type="entry name" value="Pil1"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0325">Glycoprotein</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<feature type="chain" description="Sphingolipid long chain base-responsive protein LSP1" id="PRO_0000084505">
+<location>
+<begin position="1"/>
+<end position="341"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Poly-Pro">
+<location>
+<begin position="21"/>
+<end position="25"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Glu-rich">
+<location>
+<begin position="283"/>
+<end position="324"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphothreonine" evidence="7 8 9 10">
+<location>
+<position position="233"/>
+</location>
+</feature>
+<feature type="turn" evidence="6">
+<location>
+<begin position="53"/>
+<end position="55"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="56"/>
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+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="95"/>
+<end position="159"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="165"/>
+<end position="224"/>
+</location>
+</feature>
+<feature type="strand" evidence="6">
+<location>
+<begin position="234"/>
+<end position="236"/>
+</location>
+</feature>
+<feature type="helix" evidence="6">
+<location>
+<begin position="244"/>
+<end position="260"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000269">
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+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
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+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="15016821"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
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+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
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+</source>
+</evidence>
+<evidence key="6" type="ECO:0007744">
+<source>
+<dbReference type="PDB" id="3PLT"/>
+</source>
+</evidence>
+<evidence key="7" type="ECO:0007744">
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+<dbReference type="PubMed" id="15665377"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0007744">
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+</source>
+</evidence>
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+</source>
+</evidence>
+<evidence key="10" type="ECO:0007744">
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+<dbReference type="PubMed" id="19779198"/>
+</source>
+</evidence>
+<sequence length="341" mass="38071" checksum="6FCEE022ECC9778C" modified="1996-11-01" version="1">MHRTYSLRNQRAPTAAELQAPPPPPSSTKSKFFGKASIASSFRKNAAGNFGPELARKLSQLVKTEKGVLRAMEVVASERREAAKQLSLWGADNDDDVSDVTDKLGVLIYELGELQDQFIDKYDQYRVTLKSIRNIEASVQPSRDRKEKITDEIAHLKYKDPQSTKIPVLEQELVRAEAESLVAEAQLSNITREKLKAAYSYMFDSLRELSEKFALIAGYGKALLELLDDSPVTPGEARPAYDGYEASRQIIMDAESALESWTLDMAAVKPTLSFHQTVDDVYEDEDGEEEEEPEIQNGDIPGQVVEEEEVEWTTEVPVDDEAHEADHHVSQNGHTSGSENI</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2000-05-30" modified="2021-04-07" version="166">
+<accession>Q12117</accession>
+<accession>D6VS17</accession>
+<name>MRH1_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Protein MRH1</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Membrane protein related to HSP30</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">MRH1</name>
+<name type="ordered locus">YDR033W</name>
+<name type="ORF">YD9673.03</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="75" last="78">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
+<person name="Jacq C."/>
+<person name="Alt-Moerbe J."/>
+<person name="Andre B."/>
+<person name="Arnold W."/>
+<person name="Bahr A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Bargues M."/>
+<person name="Baron L."/>
+<person name="Becker A."/>
+<person name="Biteau N."/>
+<person name="Bloecker H."/>
+<person name="Blugeon C."/>
+<person name="Boskovic J."/>
+<person name="Brandt P."/>
+<person name="Brueckner M."/>
+<person name="Buitrago M.J."/>
+<person name="Coster F."/>
+<person name="Delaveau T."/>
+<person name="del Rey F."/>
+<person name="Dujon B."/>
+<person name="Eide L.G."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Goffeau A."/>
+<person name="Gomez-Peris A."/>
+<person name="Granotier C."/>
+<person name="Hanemann V."/>
+<person name="Hankeln T."/>
+<person name="Hoheisel J.D."/>
+<person name="Jaeger W."/>
+<person name="Jimenez A."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kraemer C."/>
+<person name="Kuester H."/>
+<person name="Laamanen P."/>
+<person name="Legros Y."/>
+<person name="Louis E.J."/>
+<person name="Moeller-Rieker S."/>
+<person name="Monnet A."/>
+<person name="Moro M."/>
+<person name="Mueller-Auer S."/>
+<person name="Nussbaumer B."/>
+<person name="Paricio N."/>
+<person name="Paulin L."/>
+<person name="Perea J."/>
+<person name="Perez-Alonso M."/>
+<person name="Perez-Ortin J.E."/>
+<person name="Pohl T.M."/>
+<person name="Prydz H."/>
+<person name="Purnelle B."/>
+<person name="Rasmussen S.W."/>
+<person name="Remacha M.A."/>
+<person name="Revuelta J.L."/>
+<person name="Rieger M."/>
+<person name="Salom D."/>
+<person name="Saluz H.P."/>
+<person name="Saiz J.E."/>
+<person name="Saren A.-M."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Schmidt E.R."/>
+<person name="Schneider C."/>
+<person name="Scholler P."/>
+<person name="Schwarz S."/>
+<person name="Soler-Mira A."/>
+<person name="Urrestarazu L.A."/>
+<person name="Verhasselt P."/>
+<person name="Vissers S."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Wagner G."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Woelfl S."/>
+<person name="Harris D.E."/>
+<person name="Bowman S."/>
+<person name="Brown D."/>
+<person name="Churcher C.M."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jones L."/>
+<person name="McDonald S."/>
+<person name="Murphy L.D."/>
+<person name="Niblett D."/>
+<person name="Odell C."/>
+<person name="Oliver K."/>
+<person name="Rajandream M.A."/>
+<person name="Richards C."/>
+<person name="Shore L."/>
+<person name="Walsh S.V."/>
+<person name="Barrell B.G."/>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin D."/>
+<person name="Mosedale D."/>
+<person name="Nakahara K."/>
+<person name="Namath A."/>
+<person name="Oefner P."/>
+<person name="Oh C."/>
+<person name="Petel F.X."/>
+<person name="Roberts D."/>
+<person name="Schramm S."/>
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+<person name="Kirsten J."/>
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+<person name="Langston Y."/>
+<person name="Latreille P."/>
+<person name="Le T."/>
+<person name="Mardis E."/>
+<person name="Menezes S."/>
+<person name="Miller N."/>
+<person name="Nhan M."/>
+<person name="Pauley A."/>
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+<person name="Rifkin L."/>
+<person name="Riles L."/>
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+<person name="Vaudin M."/>
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+<person name="Kleine K."/>
+<person name="Mewes H.-W."/>
+<person name="Zollner A."/>
+<person name="Zaccaria P."/>
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+<person name="Engel S.R."/>
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+<citation type="journal article" date="2000" name="Biochim. Biophys. Acta" volume="1463" first="477" last="482">
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+<person name="Wu K."/>
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+<authorList>
+<person name="Navarre C."/>
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+</reference>
+<reference key="5">
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+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
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+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
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+<dbReference type="DOI" id="10.1038/nature02026"/>
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+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
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+<authorList>
+<person name="Ghaemmaghami S."/>
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+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
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+<person name="Perschil I."/>
+<person name="Chacinska A."/>
+<person name="Guiard B."/>
+<person name="Rehling P."/>
+<person name="Pfanner N."/>
+<person name="Meisinger C."/>
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+<dbReference type="PubMed" id="14576278"/>
+<dbReference type="DOI" id="10.1073/pnas.2135385100"/>
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+<source>
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+</reference>
+<reference key="8">
+<citation type="journal article" date="2005" name="Mol. Cell. Proteomics" volume="4" first="310" last="327">
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+<authorList>
+<person name="Gruhler A."/>
+<person name="Olsen J.V."/>
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+<person name="Faergeman N.J."/>
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+<person name="Jensen O.N."/>
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+<dbReference type="DOI" id="10.1074/mcp.m400219-mcp200"/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="11142" last="11147">
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+<authorList>
+<person name="Kim H."/>
+<person name="Melen K."/>
+<person name="Oesterberg M."/>
+<person name="von Heijne G."/>
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+<reference key="10">
+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
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+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
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+<person name="Villen J."/>
+<person name="Elias J.E."/>
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+<reference key="11">
+<citation type="journal article" date="2007" name="Mol. Cell. Proteomics" volume="6" first="1896" last="1906">
+<title>Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.</title>
+<authorList>
+<person name="Reinders J."/>
+<person name="Wagner K."/>
+<person name="Zahedi R.P."/>
+<person name="Stojanovski D."/>
+<person name="Eyrich B."/>
+<person name="van der Laan M."/>
+<person name="Rehling P."/>
+<person name="Sickmann A."/>
+<person name="Pfanner N."/>
+<person name="Meisinger C."/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<reference key="12">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; THR-295 AND SER-299</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<reference key="13">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289; THR-295 AND SER-299</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<subcellularLocation>
+<location>Mitochondrion</location>
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+<subcellularLocation>
+<location>Bud</location>
+</subcellularLocation>
+<text>Localized primarily to the plasma membrane. Also found at the buds.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 182000 molecules/cell in log phase SD medium.</text>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
+<person name="Albermann K."/>
+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
+<person name="Brueckner M."/>
+<person name="Carpenter J."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Churcher C.M."/>
+<person name="Coster F."/>
+<person name="Davis K."/>
+<person name="Davis R.W."/>
+<person name="Dietrich F.S."/>
+<person name="Delius H."/>
+<person name="DiPaolo T."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Duncan M."/>
+<person name="Floeth M."/>
+<person name="Fortin N."/>
+<person name="Friesen J.D."/>
+<person name="Fritz C."/>
+<person name="Goffeau A."/>
+<person name="Hall J."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Hilbert H."/>
+<person name="Hillier L.W."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Johnston M."/>
+<person name="Kalman S."/>
+<person name="Kleine K."/>
+<person name="Komp C."/>
+<person name="Kurdi O."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin A."/>
+<person name="Lin D."/>
+<person name="Louis E.J."/>
+<person name="Marathe R."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
+<person name="Nentwich U."/>
+<person name="Oefner P."/>
+<person name="Pearson D."/>
+<person name="Petel F.X."/>
+<person name="Pohl T.M."/>
+<person name="Purnelle B."/>
+<person name="Rajandream M.A."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Roberts D."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
+<person name="Ushinsky S."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Voss H."/>
+<person name="Walsh S.V."/>
+<person name="Wambutt R."/>
+<person name="Wang Y."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Winnett E."/>
+<person name="Zhong W.-W."/>
+<person name="Zollner A."/>
+<person name="Vo D.H."/>
+<person name="Hani J."/>
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+<dbReference type="PubMed" id="9169875"/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2002" name="Mol. Biol. Cell" volume="13" first="847" last="853">
+<title>Genetic basis of mitochondrial function and morphology in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Dimmer K.S."/>
+<person name="Fritz S."/>
+<person name="Fuchs F."/>
+<person name="Messerschmitt M."/>
+<person name="Weinbach N."/>
+<person name="Neupert W."/>
+<person name="Westermann B."/>
+</authorList>
+<dbReference type="PubMed" id="11907266"/>
+<dbReference type="DOI" id="10.1091/mbc.01-12-0588"/>
+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Involved in mitochondrial distribution and morphology.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 414 molecules/cell in log phase SD medium.</text>
+</comment>
+<dbReference type="EMBL" id="U51033">
+<property type="protein sequence ID" value="AAB68132.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11501.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="entry name" value="S69069"/>
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+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<feature type="chain" description="Mitochondrial distribution and morphology protein 36" id="PRO_0000096332">
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+<feature type="modified residue" description="Phosphoserine" evidence="3 4">
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+<evidence key="1" type="ECO:0000269">
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+</entry>
+<entry dataset="Swiss-Prot" created="2005-08-16" modified="2021-04-07" version="161">
+<accession>O14467</accession>
+<accession>D6W2Z8</accession>
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+<accession>Q86ZS7</accession>
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+</recommendedName>
+<alternativeName>
+<fullName>Suppressor of frameshift mutations protein 13</fullName>
+</alternativeName>
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+<name type="ordered locus">YOR298C-A</name>
+</gene>
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+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
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+<taxon>Fungi</taxon>
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+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1998" name="Mol. Cell. Biol." volume="18" first="4971" last="4976">
+<title>Yeast coactivator MBF1 mediates GCN4-dependent transcriptional activation.</title>
+<authorList>
+<person name="Takemaru K."/>
+<person name="Harashima S."/>
+<person name="Ueda H."/>
+<person name="Hirose S."/>
+</authorList>
+<dbReference type="PubMed" id="9710580"/>
+<dbReference type="DOI" id="10.1128/mcb.18.9.4971"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<scope>INTERACTION WITH GCN4 AND TBP</scope>
+<scope>MUTAGENESIS OF ASP-112</scope>
+<scope>FUNCTION</scope>
+<source>
+<strain>KT130</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="98" last="102">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.</title>
+<authorList>
+<person name="Dujon B."/>
+<person name="Albermann K."/>
+<person name="Aldea M."/>
+<person name="Alexandraki D."/>
+<person name="Ansorge W."/>
+<person name="Arino J."/>
+<person name="Benes V."/>
+<person name="Bohn C."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Bordonne R."/>
+<person name="Boyer J."/>
+<person name="Camasses A."/>
+<person name="Casamayor A."/>
+<person name="Casas C."/>
+<person name="Cheret G."/>
+<person name="Cziepluch C."/>
+<person name="Daignan-Fornier B."/>
+<person name="Dang V.-D."/>
+<person name="de Haan M."/>
+<person name="Delius H."/>
+<person name="Durand P."/>
+<person name="Fairhead C."/>
+<person name="Feldmann H."/>
+<person name="Gaillon L."/>
+<person name="Galisson F."/>
+<person name="Gamo F.-J."/>
+<person name="Gancedo C."/>
+<person name="Goffeau A."/>
+<person name="Goulding S.E."/>
+<person name="Grivell L.A."/>
+<person name="Habbig B."/>
+<person name="Hand N.J."/>
+<person name="Hani J."/>
+<person name="Hattenhorst U."/>
+<person name="Hebling U."/>
+<person name="Hernando Y."/>
+<person name="Herrero E."/>
+<person name="Heumann K."/>
+<person name="Hiesel R."/>
+<person name="Hilger F."/>
+<person name="Hofmann B."/>
+<person name="Hollenberg C.P."/>
+<person name="Hughes B."/>
+<person name="Jauniaux J.-C."/>
+<person name="Kalogeropoulos A."/>
+<person name="Katsoulou C."/>
+<person name="Kordes E."/>
+<person name="Lafuente M.J."/>
+<person name="Landt O."/>
+<person name="Louis E.J."/>
+<person name="Maarse A.C."/>
+<person name="Madania A."/>
+<person name="Mannhaupt G."/>
+<person name="Marck C."/>
+<person name="Martin R.P."/>
+<person name="Mewes H.-W."/>
+<person name="Michaux G."/>
+<person name="Paces V."/>
+<person name="Parle-McDermott A.G."/>
+<person name="Pearson B.M."/>
+<person name="Perrin A."/>
+<person name="Pettersson B."/>
+<person name="Poch O."/>
+<person name="Pohl T.M."/>
+<person name="Poirey R."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rechmann S."/>
+<person name="Schwager C."/>
+<person name="Schweizer M."/>
+<person name="Sor F."/>
+<person name="Sterky F."/>
+<person name="Tarassov I.A."/>
+<person name="Teodoru C."/>
+<person name="Tettelin H."/>
+<person name="Thierry A."/>
+<person name="Tobiasch E."/>
+<person name="Tzermia M."/>
+<person name="Uhlen M."/>
+<person name="Unseld M."/>
+<person name="Valens M."/>
+<person name="Vandenbol M."/>
+<person name="Vetter I."/>
+<person name="Vlcek C."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler H."/>
+<person name="Wiemann S."/>
+<person name="Winsor B."/>
+<person name="Wolfe K.H."/>
+<person name="Zollner A."/>
+<person name="Zumstein E."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="9169874"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
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+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
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+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2003" name="Genome Biol." volume="4" first="R45.1" last="R45.13">
+<title>Reinvestigation of the Saccharomyces cerevisiae genome annotation by comparison to the genome of a related fungus: Ashbya gossypii.</title>
+<authorList>
+<person name="Brachat S."/>
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+</authorList>
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+<dbReference type="DOI" id="10.1186/gb-2003-4-7-r45"/>
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+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-58</scope>
+<source>
+<strain>ATCC 204511 / S288c / AB972</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="submission" date="2005-05" db="UniProtKB">
+<authorList>
+<person name="Bienvenut W.V."/>
+<person name="Peters C."/>
+</authorList>
+</citation>
+<scope>PROTEIN SEQUENCE OF 76-83; 103-117 AND 138-149</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
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+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
+<person name="Zhu C."/>
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+<person name="Camargo A.A."/>
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+<person name="McCarron S."/>
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+<person name="Moreira D."/>
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+<person name="Zuo D."/>
+<person name="Mohr S."/>
+<person name="Kane M.F."/>
+<person name="Williamson J."/>
+<person name="Simpson A.J.G."/>
+<person name="Bulyk M.L."/>
+<person name="Harlow E."/>
+<person name="Marsischky G."/>
+<person name="Kolodner R.D."/>
+<person name="LaBaer J."/>
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+<dbReference type="PubMed" id="17322287"/>
+<dbReference type="DOI" id="10.1101/gr.6037607"/>
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+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 94-151</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
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+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
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+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2005" name="Mol. Cell. Proteomics" volume="4" first="310" last="327">
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+<authorList>
+<person name="Gruhler A."/>
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+<person name="Mohammed S."/>
+<person name="Mortensen P."/>
+<person name="Faergeman N.J."/>
+<person name="Mann M."/>
+<person name="Jensen O.N."/>
+</authorList>
+<dbReference type="PubMed" id="15665377"/>
+<dbReference type="DOI" id="10.1074/mcp.m400219-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>YAL6B</strain>
+</source>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
+<person name="Haas W."/>
+<person name="Villen J."/>
+<person name="Elias J.E."/>
+<person name="Gygi S.P."/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ADR376</strain>
+</source>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
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+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
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+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
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+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
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+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<comment type="function">
+<text evidence="4">Transcriptional coactivator that stimulates GCN4-dependent transcriptional activity by bridging the DNA-binding region of GCN4 and TBP (SPT15), thereby recruiting TBP to GCN4-bound promoters.</text>
+</comment>
+<comment type="subunit">
+<text evidence="4">Interacts with TBP and the transcription factor GCN4.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="2">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="2">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 47277 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="5">Belongs to the MBF1 family.</text>
+</comment>
+<comment type="sequence caution" evidence="5">
+<conflict type="frameshift">
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+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0804">Transcription</keyword>
+<keyword id="KW-0805">Transcription regulation</keyword>
+<feature type="chain" description="Multiprotein-bridging factor 1" id="PRO_0000149814">
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+<feature type="modified residue" description="Phosphoserine" evidence="6 7 8 9 10">
+<location>
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+</feature>
+<feature type="mutagenesis site" description="Reduces interaction to TBP." evidence="4">
+<original>D</original>
+<variation>A</variation>
+<location>
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+</feature>
+<evidence key="1" type="ECO:0000255">
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+<entry dataset="Swiss-Prot" created="1986-07-21" modified="2021-04-07" version="209">
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+<accession>D6VR21</accession>
+<name>PGK_YEAST</name>
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+<recommendedName>
+<fullName>Phosphoglycerate kinase</fullName>
+<ecNumber>2.7.2.3</ecNumber>
+</recommendedName>
+</protein>
+<gene>
+<name type="primary">PGK1</name>
+<name type="ordered locus">YCR012W</name>
+<name type="ORF">YCR12W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1982" name="Nucleic Acids Res." volume="10" first="7791" last="7808">
+<title>The primary structure of the Saccharomyces cerevisiae gene for 3-phosphoglycerate kinase.</title>
+<authorList>
+<person name="Hitzeman R.A."/>
+<person name="Hagie F.E."/>
+<person name="Hayflick J.S."/>
+<person name="Chen C.Y."/>
+<person name="Seeburg P.H."/>
+<person name="Derynck R."/>
+</authorList>
+<dbReference type="PubMed" id="6296791"/>
+<dbReference type="DOI" id="10.1093/nar/10.23.7791"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1992" name="Yeast" volume="8" first="409" last="417">
+<title>The complete sequence of a 10.8 kb segment distal of SUF2 on the right arm of chromosome III from Saccharomyces cerevisiae reveals seven open reading frames including the RVS161, ADP1 and PGK genes.</title>
+<authorList>
+<person name="Skala J."/>
+<person name="Purnelle B."/>
+<person name="Goffeau A."/>
+</authorList>
+<dbReference type="PubMed" id="1626432"/>
+<dbReference type="DOI" id="10.1002/yea.320080508"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1992" name="Nature" volume="357" first="38" last="46">
+<title>The complete DNA sequence of yeast chromosome III.</title>
+<authorList>
+<person name="Oliver S.G."/>
+<person name="van der Aart Q.J.M."/>
+<person name="Agostoni-Carbone M.L."/>
+<person name="Aigle M."/>
+<person name="Alberghina L."/>
+<person name="Alexandraki D."/>
+<person name="Antoine G."/>
+<person name="Anwar R."/>
+<person name="Ballesta J.P.G."/>
+<person name="Benit P."/>
+<person name="Berben G."/>
+<person name="Bergantino E."/>
+<person name="Biteau N."/>
+<person name="Bolle P.-A."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Brown A."/>
+<person name="Brown A.J.P."/>
+<person name="Buhler J.-M."/>
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+<person name="Chanet R."/>
+<person name="Contreras R."/>
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+<person name="Chaignepain S."/>
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+<citation type="journal article" date="2005" name="Mol. Cell. Proteomics" volume="4" first="310" last="327">
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+<scope>CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<reference key="13">
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+<title>Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics.</title>
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+<person name="Reinders J."/>
+<person name="Zahedi R.P."/>
+<person name="Pfanner N."/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
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+<dbReference type="DOI" id="10.1021/pr060559j"/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; THR-331 AND THR-392</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
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+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
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+<person name="Eng J."/>
+<person name="Zhou H."/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-93; THR-203; THR-241 AND THR-331</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<reference key="17">
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+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
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+<person name="Morgan D.O."/>
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+<dbReference type="DOI" id="10.1126/science.1172867"/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-172; THR-298; SER-318; THR-331 AND THR-392</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
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+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
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+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
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+<person name="Arnesen T."/>
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+<scope>CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]</scope>
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+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
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+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
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+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
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+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-82; LYS-197; LYS-258; LYS-274 AND LYS-302</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="20">
+<citation type="journal article" date="1982" name="EMBO J." volume="1" first="1635" last="1640">
+<title>Sequence and structure of yeast phosphoglycerate kinase.</title>
+<authorList>
+<person name="Watson H.C."/>
+<person name="Walker N.P.C."/>
+<person name="Shaw P.J."/>
+<person name="Bryant T.N."/>
+<person name="Wendell P.L."/>
+<person name="Fothergill L.A."/>
+<person name="Perkins R.E."/>
+<person name="Conroy S.C."/>
+<person name="Dobson M.J."/>
+<person name="Tuite M.F."/>
+<person name="Kingsman A.J."/>
+<person name="Kingsman S.M."/>
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+<dbReference type="DOI" id="10.1002/j.1460-2075.1982.tb01366.x"/>
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+<scope>X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE AND ATP ANALOG</scope>
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+<reference key="21">
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+<authorList>
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+<person name="Hsu B.T."/>
+<person name="Sherman M.A."/>
+<person name="Mas M.T."/>
+<person name="Rees D.C."/>
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+<dbReference type="DOI" id="10.1021/bi952500o"/>
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+<scope>X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT GLN-66 IN COMPLEX WITH SUBSTRATE AND ATP ANALOG</scope>
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+<comment type="catalytic activity">
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+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 314000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="7">Belongs to the phosphoglycerate kinase family.</text>
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+<sequence length="416" mass="44738" checksum="378AB944DB34EFF0" modified="2007-01-23" version="2">MSLSSKLSVQDLDLKDKRVFIRVDFNVPLDGKKITSNQRIVAALPTIKYVLEHHPRYVVLASHLGRPNGERNEKYSLAPVAKELQSLLGKDVTFLNDCVGPEVEAAVKASAPGSVILLENLRYHIEEEGSRKVDGQKVKASKEDVQKFRHELSSLADVYINDAFGTAHRAHSSMVGFDLPQRAAGFLLEKELKYFGKALENPTRPFLAILGGAKVADKIQLIDNLLDKVDSIIIGGGMAFTFKKVLENTEIGDSIFDKAGAEIVPKLMEKAKAKGVEVVLPVDFIIADAFSADANTKTVTDKEGIPAGWQGLDNGPESRKLFAATVAKAKTIVWNGPPGVFEFEKFAAGTKALLDEVVKSSAAGNTVIIGGGDTATVAKKYGVTDKISHVSTGGGASLELLEGKELPGVAFLSEKK</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1997-11-01" modified="2021-04-07" version="162">
+<accession>Q05568</accession>
+<accession>D6VSP9</accession>
+<accession>E9P8T2</accession>
+<name>PEX10_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Peroxisome biogenesis factor 10</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Peroxin-10</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Peroxisomal biogenesis factor 10</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Peroxisome assembly protein 10</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">PEX10</name>
+<name type="synonym">PAS4</name>
+<name type="ordered locus">YDR265W</name>
+<name type="ORF">D9954.8</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="75" last="78">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
+<person name="Jacq C."/>
+<person name="Alt-Moerbe J."/>
+<person name="Andre B."/>
+<person name="Arnold W."/>
+<person name="Bahr A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Bargues M."/>
+<person name="Baron L."/>
+<person name="Becker A."/>
+<person name="Biteau N."/>
+<person name="Bloecker H."/>
+<person name="Blugeon C."/>
+<person name="Boskovic J."/>
+<person name="Brandt P."/>
+<person name="Brueckner M."/>
+<person name="Buitrago M.J."/>
+<person name="Coster F."/>
+<person name="Delaveau T."/>
+<person name="del Rey F."/>
+<person name="Dujon B."/>
+<person name="Eide L.G."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Goffeau A."/>
+<person name="Gomez-Peris A."/>
+<person name="Granotier C."/>
+<person name="Hanemann V."/>
+<person name="Hankeln T."/>
+<person name="Hoheisel J.D."/>
+<person name="Jaeger W."/>
+<person name="Jimenez A."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kraemer C."/>
+<person name="Kuester H."/>
+<person name="Laamanen P."/>
+<person name="Legros Y."/>
+<person name="Louis E.J."/>
+<person name="Moeller-Rieker S."/>
+<person name="Monnet A."/>
+<person name="Moro M."/>
+<person name="Mueller-Auer S."/>
+<person name="Nussbaumer B."/>
+<person name="Paricio N."/>
+<person name="Paulin L."/>
+<person name="Perea J."/>
+<person name="Perez-Alonso M."/>
+<person name="Perez-Ortin J.E."/>
+<person name="Pohl T.M."/>
+<person name="Prydz H."/>
+<person name="Purnelle B."/>
+<person name="Rasmussen S.W."/>
+<person name="Remacha M.A."/>
+<person name="Revuelta J.L."/>
+<person name="Rieger M."/>
+<person name="Salom D."/>
+<person name="Saluz H.P."/>
+<person name="Saiz J.E."/>
+<person name="Saren A.-M."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Schmidt E.R."/>
+<person name="Schneider C."/>
+<person name="Scholler P."/>
+<person name="Schwarz S."/>
+<person name="Soler-Mira A."/>
+<person name="Urrestarazu L.A."/>
+<person name="Verhasselt P."/>
+<person name="Vissers S."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Wagner G."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Woelfl S."/>
+<person name="Harris D.E."/>
+<person name="Bowman S."/>
+<person name="Brown D."/>
+<person name="Churcher C.M."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jones L."/>
+<person name="McDonald S."/>
+<person name="Murphy L.D."/>
+<person name="Niblett D."/>
+<person name="Odell C."/>
+<person name="Oliver K."/>
+<person name="Rajandream M.A."/>
+<person name="Richards C."/>
+<person name="Shore L."/>
+<person name="Walsh S.V."/>
+<person name="Barrell B.G."/>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin D."/>
+<person name="Mosedale D."/>
+<person name="Nakahara K."/>
+<person name="Namath A."/>
+<person name="Oefner P."/>
+<person name="Oh C."/>
+<person name="Petel F.X."/>
+<person name="Roberts D."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Shogren T."/>
+<person name="Shroff N."/>
+<person name="Winant A."/>
+<person name="Yelton M.A."/>
+<person name="Botstein D."/>
+<person name="Davis R.W."/>
+<person name="Johnston M."/>
+<person name="Andrews S."/>
+<person name="Brinkman R."/>
+<person name="Cooper J."/>
+<person name="Ding H."/>
+<person name="Du Z."/>
+<person name="Favello A."/>
+<person name="Fulton L."/>
+<person name="Gattung S."/>
+<person name="Greco T."/>
+<person name="Hallsworth K."/>
+<person name="Hawkins J."/>
+<person name="Hillier L.W."/>
+<person name="Jier M."/>
+<person name="Johnson D."/>
+<person name="Johnston L."/>
+<person name="Kirsten J."/>
+<person name="Kucaba T."/>
+<person name="Langston Y."/>
+<person name="Latreille P."/>
+<person name="Le T."/>
+<person name="Mardis E."/>
+<person name="Menezes S."/>
+<person name="Miller N."/>
+<person name="Nhan M."/>
+<person name="Pauley A."/>
+<person name="Peluso D."/>
+<person name="Rifkin L."/>
+<person name="Riles L."/>
+<person name="Taich A."/>
+<person name="Trevaskis E."/>
+<person name="Vignati D."/>
+<person name="Wilcox L."/>
+<person name="Wohldman P."/>
+<person name="Vaudin M."/>
+<person name="Wilson R."/>
+<person name="Waterston R."/>
+<person name="Albermann K."/>
+<person name="Hani J."/>
+<person name="Heumann K."/>
+<person name="Kleine K."/>
+<person name="Mewes H.-W."/>
+<person name="Zollner A."/>
+<person name="Zaccaria P."/>
+</authorList>
+<dbReference type="PubMed" id="9169867"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
+<person name="Rolfs A."/>
+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
+<person name="Zhu C."/>
+<person name="Berger M.F."/>
+<person name="Camargo A.A."/>
+<person name="Kelley F."/>
+<person name="McCarron S."/>
+<person name="Jepson D."/>
+<person name="Richardson A."/>
+<person name="Raphael J."/>
+<person name="Moreira D."/>
+<person name="Taycher E."/>
+<person name="Zuo D."/>
+<person name="Mohr S."/>
+<person name="Kane M.F."/>
+<person name="Williamson J."/>
+<person name="Simpson A.J.G."/>
+<person name="Bulyk M.L."/>
+<person name="Harlow E."/>
+<person name="Marsischky G."/>
+<person name="Kolodner R.D."/>
+<person name="LaBaer J."/>
+</authorList>
+<dbReference type="PubMed" id="17322287"/>
+<dbReference type="DOI" id="10.1101/gr.6037607"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Somewhat implicated in the biogenesis of peroxisomes.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-13194">
+<id>Q05568</id>
+</interactant>
+<interactant intactId="EBI-2077297">
+<id>Q04370</id>
+<label>PEX12</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>12</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-13194">
+<id>Q05568</id>
+</interactant>
+<interactant intactId="EBI-13206">
+<id>P80667</id>
+<label>PEX13</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>7</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-13194">
+<id>Q05568</id>
+</interactant>
+<interactant intactId="EBI-13160">
+<id>P32800</id>
+<label>PEX2</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>14</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="3">Peroxisome membrane</location>
+<topology evidence="3">Peripheral membrane protein</topology>
+</subcellularLocation>
+</comment>
+<comment type="similarity">
+<text evidence="3">Belongs to the pex2/pex10/pex12 family.</text>
+</comment>
+<dbReference type="EMBL" id="U51030">
+<property type="protein sequence ID" value="AAB64453.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY557788">
+<property type="protein sequence ID" value="AAS56114.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006938">
+<property type="protein sequence ID" value="DAA12109.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S70125">
+<property type="entry name" value="S70125"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_010551.1">
+<property type="nucleotide sequence ID" value="NM_001180573.1"/>
+</dbReference>
+<dbReference type="SMR" id="Q05568"/>
+<dbReference type="BioGRID" id="32321">
+<property type="interactions" value="182"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1903">
+<property type="entry name" value="Perxosomal PEX2-PEX10-PEX12 ubiquitin ligase complex"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-7566N"/>
+<dbReference type="IntAct" id="Q05568">
+<property type="interactions" value="16"/>
+</dbReference>
+<dbReference type="MINT" id="Q05568"/>
+<dbReference type="STRING" id="4932.YDR265W"/>
+<dbReference type="TCDB" id="3.A.20.1.5">
+<property type="family name" value="the peroxisomal protein importer (ppi) family"/>
+</dbReference>
+<dbReference type="MaxQB" id="Q05568"/>
+<dbReference type="PaxDb" id="Q05568"/>
+<dbReference type="PRIDE" id="Q05568"/>
+<dbReference type="EnsemblFungi" id="YDR265W_mRNA">
+<property type="protein sequence ID" value="YDR265W"/>
+<property type="gene ID" value="YDR265W"/>
+</dbReference>
+<dbReference type="GeneID" id="851858"/>
+<dbReference type="KEGG" id="sce:YDR265W"/>
+<dbReference type="SGD" id="S000002673">
+<property type="gene designation" value="PEX10"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YDR265W"/>
+<dbReference type="eggNOG" id="KOG0317">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00510000048446"/>
+<dbReference type="HOGENOM" id="CLU_041707_2_0_1"/>
+<dbReference type="InParanoid" id="Q05568"/>
+<dbReference type="OMA" id="PRNWIKY"/>
+<dbReference type="Reactome" id="R-SCE-9033241">
+<property type="pathway name" value="Peroxisomal protein import"/>
+</dbReference>
+<dbReference type="PRO" id="PR:Q05568"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome IV"/>
+</dbReference>
+<dbReference type="RNAct" id="Q05568">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005779">
+<property type="term" value="C:integral component of peroxisomal membrane"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:1990429">
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+</dbReference>
+<dbReference type="GO" id="GO:0005778">
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+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0061630">
+<property type="term" value="F:ubiquitin protein ligase activity"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0016558">
+<property type="term" value="P:protein import into peroxisome matrix"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000209">
+<property type="term" value="P:protein polyubiquitination"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0016567">
+<property type="term" value="P:protein ubiquitination"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.40.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR006845">
+<property type="entry name" value="Pex_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001841">
+<property type="entry name" value="Znf_RING"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013083">
+<property type="entry name" value="Znf_RING/FYVE/PHD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR017907">
+<property type="entry name" value="Znf_RING_CS"/>
+</dbReference>
+<dbReference type="Pfam" id="PF04757">
+<property type="entry name" value="Pex2_Pex12"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF13639">
+<property type="entry name" value="zf-RING_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM00184">
+<property type="entry name" value="RING"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00518">
+<property type="entry name" value="ZF_RING_1"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50089">
+<property type="entry name" value="ZF_RING_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0472">Membrane</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0576">Peroxisome</keyword>
+<keyword id="KW-0962">Peroxisome biogenesis</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Peroxisome biogenesis factor 10" id="PRO_0000056381">
+<location>
+<begin position="1"/>
+<end position="337"/>
+</location>
+</feature>
+<feature type="zinc finger region" description="RING-type" evidence="2">
+<location>
+<begin position="286"/>
+<end position="327"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; AAS56114." ref="3" evidence="3">
+<original>V</original>
+<variation>A</variation>
+<location>
+<position position="183"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00175"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000305"/>
+<sequence length="337" mass="39099" checksum="9AF308A8AB2A0E28" modified="1996-11-01" version="1">MKNDNKLQKEALMRLSQLRFPFADAPSIVQAHQKDEQIQGLLIMKVTELCKLIKSQLFVNSYPKELSIFAKLLYLLFTTGRRGRTLGEEYVDLTYTNRKGTRLAGRLKMIVFAFAYPLCPYFITKLYKKIMKNNKESKIEDTESVAAFCKGLLDFILDVHMTLFYFKGAFYSISKRIFGMRYVFKHILSKNEANFREEGSQKYKVLGYILLAQNVMKWYPVLTSTLGSWIYGRKRTNDSITRSSVGLQERSEHESIEGIPKESQLTHINLSDKNQLPFIPEASRKCILCLMNMSDPSCAPCGHLFCWSCLMSWCKERPECPLCRQHCQPQEILVLRQ</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1986-07-21" modified="2021-04-07" version="225">
+<accession>P00950</accession>
+<accession>D6VX45</accession>
+<accession>Q02117</accession>
+<name>PMG1_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Phosphoglycerate mutase 1</fullName>
+<shortName>PGAM 1</shortName>
+<ecNumber evidence="4">5.4.2.11</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>BPG-dependent PGAM 1</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>MPGM 1</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Phosphoglyceromutase 1</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">GPM1</name>
+<name type="synonym">GPM</name>
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+<taxon>Dikarya</taxon>
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+<taxon>Saccharomycetes</taxon>
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+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
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+<source>
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+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
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+</reference>
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+<source>
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+<dbReference type="PubMed" id="1386023"/>
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+<scope>SUBUNIT</scope>
+<scope>MUTAGENESIS OF LYS-169</scope>
+<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
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+</reference>
+<reference key="25">
+<citation type="journal article" date="1999" name="Acta Crystallogr. D" volume="55" first="1822" last="1826">
+<title>Structure of a phosphoglycerate mutase:3-phosphoglyceric acid complex at 1.7 A.</title>
+<authorList>
+<person name="Crowhurst G.S."/>
+<person name="Dalby A.R."/>
+<person name="Isupov M.N."/>
+<person name="Campbell J.W."/>
+<person name="Littlechild J.A."/>
+</authorList>
+<dbReference type="PubMed" id="10531478"/>
+<dbReference type="DOI" id="10.1107/s0907444999009944"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) IN COMPLEX WITH 3-PHOSPHO-D-GLYCERATE</scope>
+<scope>SUBUNIT</scope>
+<scope>ACTIVE SITE</scope>
+</reference>
+<reference key="26">
+<citation type="journal article" date="1999" name="J. Mol. Biol." volume="286" first="1507" last="1517">
+<title>Sulphate ions observed in the 2.12 A structure of a new crystal form of S. cerevisiae phosphoglycerate mutase provide insights into understanding the catalytic mechanism.</title>
+<authorList>
+<person name="Rigden D.J."/>
+<person name="Walter R.A."/>
+<person name="Phillips S.E."/>
+<person name="Fothergill-Gilmore L.A."/>
+</authorList>
+<dbReference type="PubMed" id="10064712"/>
+<dbReference type="DOI" id="10.1006/jmbi.1999.2566"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (2.12 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS</scope>
+<scope>SUBUNIT</scope>
+<scope>ACTIVE SITE</scope>
+</reference>
+<reference key="27" evidence="16 17">
+<citation type="journal article" date="1999" name="J. Mol. Biol." volume="289" first="691" last="699">
+<title>Polyanionic inhibitors of phosphoglycerate mutase: combined structural and biochemical analysis.</title>
+<authorList>
+<person name="Rigden D.J."/>
+<person name="Walter R.A."/>
+<person name="Phillips S.E."/>
+<person name="Fothergill-Gilmore L.A."/>
+</authorList>
+<dbReference type="PubMed" id="10369755"/>
+<dbReference type="DOI" id="10.1006/jmbi.1999.2848"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS</scope>
+<scope>ACTIVITY REGULATION</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<comment type="function">
+<text evidence="4 11">Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also Catalyzes the reaction of EC 5.4.2.4 (synthase), but with a reduced activity.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="4">
+<text>(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate</text>
+<dbReference type="Rhea" id="RHEA:15901"/>
+<dbReference type="ChEBI" id="CHEBI:58272"/>
+<dbReference type="ChEBI" id="CHEBI:58289"/>
+<dbReference type="EC" id="5.4.2.11"/>
+</reaction>
+</comment>
+<comment type="activity regulation">
+<text evidence="2">Inhibited by inositol hexakisphosphate and benzene tri-, tetra- and hexacarboxylates.</text>
+</comment>
+<comment type="biophysicochemical properties">
+<kinetics>
+<KM evidence="4 11">740 uM for 3-phosphoglycerate</KM>
+<KM evidence="4 11">8.1 uM for 2,3-bisphosphoglycerate (for mutase reaction)</KM>
+<KM evidence="4 11">2.4 uM for 2,3-bisphosphoglycerate (for phosphatase reaction)</KM>
+<text evidence="4">kcat is 490 sec(-1) for the mutase reaction, 0.0074 sec(-1) for the synthase reaction and 0.0087 sec(-1) for the phosphatase reaction with 3-phosphoglycerate as substrate.</text>
+</kinetics>
+</comment>
+<comment type="pathway">
+<text>Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5.</text>
+</comment>
+<comment type="subunit">
+<text evidence="1 2 3 10 11 12">Homotetramer: dimer of dimers.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="5">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="7 8">Mitochondrion outer membrane</location>
+<topology evidence="7 8">Peripheral membrane protein</topology>
+<orientation evidence="7 8">Cytoplasmic side</orientation>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="9">Mitochondrion intermembrane space</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="6">Present with 172000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="14">Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily.</text>
+</comment>
+<dbReference type="EC" id="5.4.2.11" evidence="4"/>
+<dbReference type="EMBL" id="X06408">
+<property type="protein sequence ID" value="CAA29698.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X58789">
+<property type="protein sequence ID" value="CAA41595.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z26877">
+<property type="protein sequence ID" value="CAA81501.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z28152">
+<property type="protein sequence ID" value="CAA81994.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="S57976">
+<property type="protein sequence ID" value="AAB26026.1"/>
+<property type="status" value="ALT_TERM"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006944">
+<property type="protein sequence ID" value="DAA09011.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S00358">
+<property type="entry name" value="PMBYY"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_012770.1">
+<property type="nucleotide sequence ID" value="NM_001179718.1"/>
+</dbReference>
+<dbReference type="PDB" id="1BQ3">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.70"/>
+<property type="chains" value="A/B/C/D=2-247"/>
+</dbReference>
+<dbReference type="PDB" id="1BQ4">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.50"/>
+<property type="chains" value="A/B/C/D=2-247"/>
+</dbReference>
+<dbReference type="PDB" id="1QHF">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="1.70"/>
+<property type="chains" value="A/B=2-241"/>
+</dbReference>
+<dbReference type="PDB" id="3PGM">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.80"/>
+<property type="chains" value="A/B=2-247"/>
+</dbReference>
+<dbReference type="PDB" id="4PGM">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.30"/>
+<property type="chains" value="A/B/C/D=2-247"/>
+</dbReference>
+<dbReference type="PDB" id="5PGM">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.12"/>
+<property type="chains" value="A/B/C/D/E/F/G/H=2-247"/>
+</dbReference>
+<dbReference type="PDBsum" id="1BQ3"/>
+<dbReference type="PDBsum" id="1BQ4"/>
+<dbReference type="PDBsum" id="1QHF"/>
+<dbReference type="PDBsum" id="3PGM"/>
+<dbReference type="PDBsum" id="4PGM"/>
+<dbReference type="PDBsum" id="5PGM"/>
+<dbReference type="SMR" id="P00950"/>
+<dbReference type="BioGRID" id="33985">
+<property type="interactions" value="87"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-6260N"/>
+<dbReference type="IntAct" id="P00950">
+<property type="interactions" value="116"/>
+</dbReference>
+<dbReference type="MINT" id="P00950"/>
+<dbReference type="STRING" id="4932.YKL152C"/>
+<dbReference type="iPTMnet" id="P00950"/>
+<dbReference type="COMPLUYEAST-2DPAGE" id="P00950"/>
+<dbReference type="SWISS-2DPAGE" id="P00950"/>
+<dbReference type="MaxQB" id="P00950"/>
+<dbReference type="PaxDb" id="P00950"/>
+<dbReference type="PRIDE" id="P00950"/>
+<dbReference type="TopDownProteomics" id="P00950"/>
+<dbReference type="EnsemblFungi" id="YKL152C_mRNA">
+<property type="protein sequence ID" value="YKL152C"/>
+<property type="gene ID" value="YKL152C"/>
+</dbReference>
+<dbReference type="GeneID" id="853705"/>
+<dbReference type="KEGG" id="sce:YKL152C"/>
+<dbReference type="SGD" id="S000001635">
+<property type="gene designation" value="GPM1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YKL152C"/>
+<dbReference type="eggNOG" id="KOG0235">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00950000182926"/>
+<dbReference type="HOGENOM" id="CLU_033323_1_1_1"/>
+<dbReference type="InParanoid" id="P00950"/>
+<dbReference type="OMA" id="RMLPYWY"/>
+<dbReference type="BioCyc" id="MetaCyc:YKL152C-MONOMER"/>
+<dbReference type="BRENDA" id="5.4.2.11">
+<property type="organism ID" value="984"/>
+</dbReference>
+<dbReference type="SABIO-RK" id="P00950"/>
+<dbReference type="UniPathway" id="UPA00109">
+<property type="reaction ID" value="UER00186"/>
+</dbReference>
+<dbReference type="EvolutionaryTrace" id="P00950"/>
+<dbReference type="PRO" id="PR:P00950"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XI"/>
+</dbReference>
+<dbReference type="RNAct" id="P00950">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005758">
+<property type="term" value="C:mitochondrial intermembrane space"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005741">
+<property type="term" value="C:mitochondrial outer membrane"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005739">
+<property type="term" value="C:mitochondrion"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004619">
+<property type="term" value="F:phosphoglycerate mutase activity"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006094">
+<property type="term" value="P:gluconeogenesis"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006096">
+<property type="term" value="P:glycolytic process"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="CDD" id="cd07067">
+<property type="entry name" value="HP_PGM_like"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.40.50.1240">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="HAMAP" id="MF_01039">
+<property type="entry name" value="PGAM_GpmA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013078">
+<property type="entry name" value="His_Pase_superF_clade-1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR029033">
+<property type="entry name" value="His_PPase_superfam"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001345">
+<property type="entry name" value="PG/BPGM_mutase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR005952">
+<property type="entry name" value="Phosphogly_mut1"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR11931">
+<property type="entry name" value="PTHR11931"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00300">
+<property type="entry name" value="His_Phos_1"/>
+<property type="match status" value="2"/>
+</dbReference>
+<dbReference type="SMART" id="SM00855">
+<property type="entry name" value="PGAM"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53254">
+<property type="entry name" value="SSF53254"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="TIGRFAMs" id="TIGR01258">
+<property type="entry name" value="pgm_1"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00175">
+<property type="entry name" value="PG_MUTASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0324">Glycolysis</keyword>
+<keyword id="KW-0413">Isomerase</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0472">Membrane</keyword>
+<keyword id="KW-0496">Mitochondrion</keyword>
+<keyword id="KW-1000">Mitochondrion outer membrane</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="13">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="Phosphoglycerate mutase 1" id="PRO_0000179839">
+<location>
+<begin position="2"/>
+<end position="247"/>
+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="2 3 10">
+<location>
+<begin position="8"/>
+<end position="15"/>
+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="2 3">
+<location>
+<begin position="21"/>
+<end position="22"/>
+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="2 10">
+<location>
+<begin position="87"/>
+<end position="90"/>
+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="2">
+<location>
+<begin position="114"/>
+<end position="115"/>
+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="2 10">
+<location>
+<begin position="183"/>
+<end position="184"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Ala-rich">
+<location>
+<begin position="233"/>
+<end position="242"/>
+</location>
+</feature>
+<feature type="active site" description="Tele-phosphohistidine intermediate" evidence="1 3 10 12">
+<location>
+<position position="9"/>
+</location>
+</feature>
+<feature type="active site" description="Proton donor/acceptor" evidence="15">
+<location>
+<position position="87"/>
+</location>
+</feature>
+<feature type="binding site" description="Substrate" evidence="3">
+<location>
+<position position="60"/>
+</location>
+</feature>
+<feature type="binding site" description="Substrate" evidence="2">
+<location>
+<position position="98"/>
+</location>
+</feature>
+<feature type="site" description="Transition state stabilizer" evidence="15">
+<location>
+<position position="182"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="20">
+<location>
+<position position="12"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphotyrosine" evidence="23">
+<location>
+<position position="49"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="20 21 22 23">
+<location>
+<position position="116"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="22">
+<location>
+<position position="127"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="23">
+<location>
+<position position="128"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="20">
+<location>
+<position position="185"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="22 23">
+<location>
+<position position="197"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="24">
+<location>
+<position position="31"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="24">
+<location>
+<position position="57"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="24">
+<location>
+<position position="71"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="24">
+<location>
+<position position="139"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="24">
+<location>
+<position position="175"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="24">
+<location>
+<position position="191"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Causes dissociation of the homotetramer to dimers at low concentrations." evidence="11">
+<original>K</original>
+<variation>P</variation>
+<location>
+<position position="169"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Reduces kcat of the mutase reaction 10000-fold." evidence="4">
+<original>H</original>
+<variation>A</variation>
+<location>
+<position position="182"/>
+</location>
+</feature>
+<feature type="strand" evidence="18">
+<location>
+<begin position="3"/>
+<end position="8"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="13"/>
+<end position="16"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="30"/>
+<end position="45"/>
+</location>
+</feature>
+<feature type="strand" evidence="18">
+<location>
+<begin position="51"/>
+<end position="55"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="59"/>
+<end position="71"/>
+</location>
+</feature>
+<feature type="strand" evidence="18">
+<location>
+<begin position="79"/>
+<end position="81"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="83"/>
+<end position="85"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="91"/>
+<end position="93"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="98"/>
+<end position="115"/>
+</location>
+</feature>
+<feature type="strand" evidence="19">
+<location>
+<begin position="116"/>
+<end position="118"/>
+</location>
+</feature>
+<feature type="strand" evidence="19">
+<location>
+<begin position="126"/>
+<end position="130"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="136"/>
+<end position="138"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="143"/>
+<end position="145"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="152"/>
+<end position="165"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="167"/>
+<end position="172"/>
+</location>
+</feature>
+<feature type="strand" evidence="18">
+<location>
+<begin position="177"/>
+<end position="181"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="183"/>
+<end position="194"/>
+</location>
+</feature>
+<feature type="turn" evidence="18">
+<location>
+<begin position="198"/>
+<end position="200"/>
+</location>
+</feature>
+<feature type="helix" evidence="18">
+<location>
+<begin position="201"/>
+<end position="203"/>
+</location>
+</feature>
+<feature type="strand" evidence="19">
+<location>
+<begin position="208"/>
+<end position="210"/>
+</location>
+</feature>
+<feature type="strand" evidence="18">
+<location>
+<begin position="212"/>
+<end position="216"/>
+</location>
+</feature>
+<feature type="turn" evidence="19">
+<location>
+<begin position="218"/>
+<end position="220"/>
+</location>
+</feature>
+<feature type="strand" evidence="18">
+<location>
+<begin position="222"/>
+<end position="224"/>
+</location>
+</feature>
+<feature type="strand" evidence="18">
+<location>
+<begin position="227"/>
+<end position="230"/>
+</location>
+</feature>
+<feature type="turn" evidence="18">
+<location>
+<begin position="231"/>
+<end position="233"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="10064712"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="10369755"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="10531478"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="1386023"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000269">
+<source>
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+<accession>D6W3T6</accession>
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+<citation type="journal article" date="1991" name="Nucleic Acids Res." volume="19" first="2603" last="2608">
+<title>Yeast ribosomal proteins: XII. YS11 of Saccharomyces cerevisiae is a homologue to E. coli S4 according to the gene analysis.</title>
+<authorList>
+<person name="Mizuta K."/>
+<person name="Hashimoto T."/>
+<person name="Suzuki K."/>
+<person name="Otaka E."/>
+</authorList>
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+<dbReference type="DOI" id="10.1093/nar/19.10.2603"/>
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+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
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+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
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+<person name="Vo D.H."/>
+<person name="Hani J."/>
+</authorList>
+<dbReference type="PubMed" id="9169875"/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
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+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
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+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
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+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1982" name="Biochemistry" volume="21" first="4545" last="4550">
+<title>Isolation of seventeen proteins and amino-terminal amino acid sequences of eight proteins from cytoplasmic ribosomes of yeast.</title>
+<authorList>
+<person name="Otaka E."/>
+<person name="Higo K."/>
+<person name="Osawa S."/>
+</authorList>
+<dbReference type="PubMed" id="6814480"/>
+<dbReference type="DOI" id="10.1021/bi00262a005"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 2-24</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
+</authorList>
+<dbReference type="PubMed" id="9559554"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19980330)14:5&lt;471::aid-yea241>3.0.co;2-u"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2004" name="Eukaryot. Cell" volume="3" first="1619" last="1626">
+<title>The small-subunit processome is a ribosome assembly intermediate.</title>
+<authorList>
+<person name="Bernstein K.A."/>
+<person name="Gallagher J.E.G."/>
+<person name="Mitchell B.M."/>
+<person name="Granneman S."/>
+<person name="Baserga S.J."/>
+</authorList>
+<dbReference type="PubMed" id="15590835"/>
+<dbReference type="DOI" id="10.1128/ec.3.6.1619-1626.2004"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH MPP10 AND SNORNA U3</scope>
+<scope>IDENTIFICATION IN SSU PROCESSOME</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
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+<person name="Noller H.F."/>
+<person name="Ortega J."/>
+<person name="Panse V.G."/>
+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="10">
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+<title>Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions.</title>
+<authorList>
+<person name="Spahn C.M.T."/>
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+</authorList>
+<dbReference type="PubMed" id="11701127"/>
+<dbReference type="DOI" id="10.1016/s0092-8674(01)00539-6"/>
+</citation>
+<scope>3D-STRUCTURE MODELING OF 19-196</scope>
+<scope>ELECTRON MICROSCOPY</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2004" name="EMBO J." volume="23" first="1008" last="1019">
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+<authorList>
+<person name="Spahn C.M.T."/>
+<person name="Gomez-Lorenzo M.G."/>
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+<person name="Andersen G.R."/>
+<person name="Beckmann R."/>
+<person name="Penczek P.A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Frank J."/>
+</authorList>
+<dbReference type="PubMed" id="14976550"/>
+<dbReference type="DOI" id="10.1038/sj.emboj.7600102"/>
+</citation>
+<scope>3D-STRUCTURE MODELING OF 19-197</scope>
+<scope>ELECTRON MICROSCOPY</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2010" name="Science" volume="330" first="1203" last="1209">
+<title>Crystal structure of the eukaryotic ribosome.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="21109664"/>
+<dbReference type="DOI" id="10.1126/science.1194294"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME</scope>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<comment type="function">
+<text evidence="4 10">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).</text>
+</comment>
+<comment type="subunit">
+<text evidence="4 5 11">Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). Interacts with snoRNA U3. uS11 interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="5">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="4">Nucleus</location>
+<location evidence="4">Nucleolus</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 106000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="9">There are 2 genes for uS4 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="9">Belongs to the universal ribosomal protein uS4 family.</text>
+</comment>
+<dbReference type="EMBL" id="D00724">
+<property type="protein sequence ID" value="BAA00626.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
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+<property type="protein sequence ID" value="AAB68268.1"/>
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+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11352.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
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+<property type="entry name" value="S16822"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_015244.1">
+<property type="nucleotide sequence ID" value="NM_001183895.1"/>
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+<dbReference type="PDB" id="1K5X">
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+<scope>NOMENCLATURE</scope>
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+<reference key="8">
+<citation type="journal article" date="2010" name="Science" volume="330" first="1203" last="1209">
+<title>Crystal structure of the eukaryotic ribosome.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
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+<scope>X-RAY CRYSTALLOGRAPHY (4.00 ANGSTROMS) OF 80S RIBOSOME</scope>
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+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
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+<scope>X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME</scope>
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+<text evidence="7">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
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+<text evidence="3 8">Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<text evidence="2">Present with 30900 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="6">There are 2 genes for eS17 in yeast.</text>
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+<text evidence="6">Belongs to the eukaryotic ribosomal protein eS17 family.</text>
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+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
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+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
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+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
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+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19980330)14:5&lt;471::aid-yea241>3.0.co;2-u"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1999" name="J. Biol. Chem." volume="274" first="37035" last="37040">
+<title>The action of N-terminal acetyltransferases on yeast ribosomal proteins.</title>
+<authorList>
+<person name="Arnold R.J."/>
+<person name="Polevoda B."/>
+<person name="Reilly J.P."/>
+<person name="Sherman F."/>
+</authorList>
+<dbReference type="PubMed" id="10601260"/>
+<dbReference type="DOI" id="10.1074/jbc.274.52.37035"/>
+</citation>
+<scope>ANALYSIS OF N-TERMINUS</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
+<person name="Moore P.B."/>
+<person name="Noller H.F."/>
+<person name="Ortega J."/>
+<person name="Panse V.G."/>
+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2015" name="Biochem. J." volume="466" first="547" last="559">
+<title>Gcn1 contacts the small ribosomal protein Rps10, which is required for full activation of the protein kinase Gcn2.</title>
+<authorList>
+<person name="Lee S.J."/>
+<person name="Swanson M.J."/>
+<person name="Sattlegger E."/>
+</authorList>
+<dbReference type="PubMed" id="25437641"/>
+<dbReference type="DOI" id="10.1042/bj20140782"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH GCN1</scope>
+</reference>
+<comment type="function">
+<text evidence="5 9">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). eS10 plays a role as a positive regulator of the GCN2 kinase activity by stimulating GCN1-mediated GCN2 activation (PubMed:25437641).</text>
+</comment>
+<comment type="subunit">
+<text evidence="4 5 10">Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). eS10 interacts with GCN1 (via middle region); this interaction is direct and promotes GCN2 kinase activity (PubMed:25437641).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="2 4">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="PTM">
+<text evidence="1">The N-terminus is not modified.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 7650 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="8">There are 2 genes for eS10 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="8">Belongs to the eukaryotic ribosomal protein eS10 family.</text>
+</comment>
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+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="entry name" value="S57597"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013957.1">
+<property type="nucleotide sequence ID" value="NM_001182737.1"/>
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+<property type="chains" value="C0/c0=1-105"/>
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+<dbReference type="EnsemblFungi" id="YMR230W_mRNA">
+<property type="protein sequence ID" value="YMR230W"/>
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+<dbReference type="VEuPathDB" id="FungiDB:YMR230W"/>
+<dbReference type="eggNOG" id="KOG3344">
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+<dbReference type="Reactome" id="R-SCE-975956">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)"/>
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+<property type="component" value="Chromosome XIII"/>
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+<dbReference type="InterPro" id="IPR036388">
+<property type="entry name" value="WH-like_DNA-bd_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036390">
+<property type="entry name" value="WH_DNA-bd_sf"/>
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+<dbReference type="PANTHER" id="PTHR12146">
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+<dbReference type="SUPFAM" id="SSF46785">
+<property type="entry name" value="SSF46785"/>
+<property type="match status" value="1"/>
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+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<feature type="chain" description="40S ribosomal protein S10-B" id="PRO_0000116377">
+<location>
+<begin position="1"/>
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+</location>
+</feature>
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+</feature>
+<feature type="strand" evidence="11">
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+<feature type="helix" evidence="11">
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+<evidence key="1" type="ECO:0000269">
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+</evidence>
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+<dbReference type="PubMed" id="9559554"/>
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+</evidence>
+<evidence key="11" type="ECO:0007744">
+<source>
+<dbReference type="PDB" id="4U3M"/>
+</source>
+</evidence>
+<sequence length="105" mass="12738" checksum="BE50B625869963CF" modified="1995-11-01" version="1">MLMPKQERNKIHQYLFQEGVVVAKKDFNQAKHEEIDTKNLYVIKALQSLTSKGYVKTQFSWQYYYYTLTEEGVEYLREYLNLPEHIVPGTYIQERNPSQRPQRRY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1999-07-15" modified="2021-02-10" version="183">
+<accession>Q05911</accession>
+<accession>D6VYZ6</accession>
+<name>PUR8_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Adenylosuccinate lyase</fullName>
+<shortName>ASL</shortName>
+<ecNumber>4.3.2.2</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Adenylosuccinase</fullName>
+<shortName>ASase</shortName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">ADE13</name>
+<name type="ordered locus">YLR359W</name>
+<name type="ORF">L8039.12</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Louis E.J."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Scholler P."/>
+<person name="Schwager C."/>
+<person name="Schwarz S."/>
+<person name="Underwood A.P."/>
+<person name="Urrestarazu L.A."/>
+<person name="Vandenbol M."/>
+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
+<person name="Zollner A."/>
+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2003" name="Nat. Biotechnol." volume="21" first="921" last="926">
+<title>A proteomics approach to understanding protein ubiquitination.</title>
+<authorList>
+<person name="Peng J."/>
+<person name="Schwartz D."/>
+<person name="Elias J.E."/>
+<person name="Thoreen C.C."/>
+<person name="Cheng D."/>
+<person name="Marsischky G."/>
+<person name="Roelofs J."/>
+<person name="Finley D."/>
+<person name="Gygi S.P."/>
+</authorList>
+<dbReference type="PubMed" id="12872131"/>
+<dbReference type="DOI" id="10.1038/nbt849"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-196</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+<source>
+<strain>SUB592</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="catalytic activity">
+<reaction>
+<text>N(6)-(1,2-dicarboxyethyl)-AMP = AMP + fumarate</text>
+<dbReference type="Rhea" id="RHEA:16853"/>
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+<dbReference type="ChEBI" id="CHEBI:57567"/>
+<dbReference type="ChEBI" id="CHEBI:456215"/>
+<dbReference type="EC" id="4.3.2.2"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>(2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate = 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide + fumarate</text>
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+<dbReference type="ChEBI" id="CHEBI:58475"/>
+<dbReference type="EC" id="4.3.2.2"/>
+</reaction>
+</comment>
+<comment type="pathway">
+<text>Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 2/2.</text>
+</comment>
+<comment type="pathway">
+<text>Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotetramer. Residues from neighboring subunits contribute catalytic and substrate-binding residues to each active site (By similarity).</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-14263">
+<id>Q05911</id>
+</interactant>
+<interactant intactId="EBI-8973">
+<id>P06103</id>
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+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="similarity">
+<text evidence="3">Belongs to the lyase 1 family. Adenylosuccinate lyase subfamily.</text>
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+<dbReference type="InterPro" id="IPR008948">
+<property type="entry name" value="L-Aspartase-like"/>
+</dbReference>
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+<dbReference type="Pfam" id="PF00206">
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+<dbReference type="PRINTS" id="PR00149">
+<property type="entry name" value="FUMRATELYASE"/>
+</dbReference>
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+<property type="entry name" value="ADSL_C"/>
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+</dbReference>
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+<property type="entry name" value="purB"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00163">
+<property type="entry name" value="FUMARATE_LYASES"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0456">Lyase</keyword>
+<keyword id="KW-0658">Purine biosynthesis</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="chain" description="Adenylosuccinate lyase" id="PRO_0000137899">
+<location>
+<begin position="1"/>
+<end position="482"/>
+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding; shared with neighboring subunit" evidence="1">
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+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="1">
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+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="1">
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+</feature>
+<feature type="active site" description="Proton donor/acceptor" evidence="1">
+<location>
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+</location>
+</feature>
+<feature type="active site" description="Proton donor/acceptor" evidence="1">
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+</feature>
+<feature type="binding site" description="Substrate" evidence="1">
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+</feature>
+<feature type="binding site" description="Substrate; shared with neighboring subunit" evidence="1">
+<location>
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+</location>
+</feature>
+<feature type="binding site" description="Substrate" evidence="1">
+<location>
+<position position="326"/>
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+</feature>
+<feature type="binding site" description="Substrate" evidence="1">
+<location>
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+</location>
+</feature>
+<feature type="binding site" description="Substrate" evidence="1">
+<location>
+<position position="335"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="2">
+<location>
+<position position="196"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
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+</source>
+</evidence>
+<evidence key="3" type="ECO:0000305"/>
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+</entry>
+<entry dataset="Swiss-Prot" created="1992-12-01" modified="2021-04-07" version="183">
+<accession>P28272</accession>
+<accession>D6VWY7</accession>
+<accession>Q2XN75</accession>
+<accession>Q70DC7</accession>
+<name>PYRD_YEAST</name>
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+<recommendedName>
+<fullName>Dihydroorotate dehydrogenase (fumarate)</fullName>
+<shortName>DHOD</shortName>
+<shortName>DHODase</shortName>
+<shortName>DHOdehase</shortName>
+<ecNumber>1.3.98.1</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Dihydroorotate oxidase</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">URA1</name>
+<name type="ordered locus">YKL216W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1992" name="Gene" volume="118" first="149" last="150">
+<title>Nucleotide sequence of the URA1 gene of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Roy A."/>
+</authorList>
+<dbReference type="PubMed" id="1511880"/>
+<dbReference type="DOI" id="10.1016/0378-1119(92)90265-q"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<scope>FUNCTION</scope>
+<source>
+<strain>ATCC 28383 / FL100 / VTT C-80102</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2004" name="Nucleic Acids Res." volume="32" first="2069" last="2078">
+<title>Differential evolution of the Saccharomyces cerevisiae DUP240 paralogs and implication of recombination in phylogeny.</title>
+<authorList>
+<person name="Leh-Louis V."/>
+<person name="Wirth B."/>
+<person name="Despons L."/>
+<person name="Wain-Hobson S."/>
+<person name="Potier S."/>
+<person name="Souciet J.-L."/>
+</authorList>
+<dbReference type="PubMed" id="15087486"/>
+<dbReference type="DOI" id="10.1093/nar/gkh529"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<scope>VARIANT LYS-58</scope>
+<source>
+<strain>CLIB 219</strain>
+<strain>CLIB 382</strain>
+<strain>CLIB 388</strain>
+<strain>CLIB 410</strain>
+<strain>CLIB 413</strain>
+<strain>CLIB 556</strain>
+<strain>CLIB 630</strain>
+<strain>CLIB 95</strain>
+<strain>K1</strain>
+<strain>R12</strain>
+<strain>R13</strain>
+<strain>Sigma 1278B</strain>
+<strain>YIIc12</strain>
+<strain>YIIc17</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1994" name="Yeast" volume="10" first="663" last="679">
+<title>The complete sequencing of a 24.6 kb segment of yeast chromosome XI identified the known loci URA1, SAC1 and TRP3, and revealed 6 new open reading frames including homologues to the threonine dehydratases, membrane transporters, hydantoinases and the phospholipase A2-activating protein.</title>
+<authorList>
+<person name="Tzermia M."/>
+<person name="Horaitis O."/>
+<person name="Alexandraki D."/>
+</authorList>
+<dbReference type="PubMed" id="7941750"/>
+<dbReference type="DOI" id="10.1002/yea.320100511"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1994" name="Nature" volume="369" first="371" last="378">
+<title>Complete DNA sequence of yeast chromosome XI.</title>
+<authorList>
+<person name="Dujon B."/>
+<person name="Alexandraki D."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Baladron V."/>
+<person name="Ballesta J.P.G."/>
+<person name="Banrevi A."/>
+<person name="Bolle P.-A."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Bossier P."/>
+<person name="Bou G."/>
+<person name="Boyer J."/>
+<person name="Buitrago M.J."/>
+<person name="Cheret G."/>
+<person name="Colleaux L."/>
+<person name="Daignan-Fornier B."/>
+<person name="del Rey F."/>
+<person name="Dion C."/>
+<person name="Domdey H."/>
+<person name="Duesterhoeft A."/>
+<person name="Duesterhus S."/>
+<person name="Entian K.-D."/>
+<person name="Erfle H."/>
+<person name="Esteban P.F."/>
+<person name="Feldmann H."/>
+<person name="Fernandes L."/>
+<person name="Fobo G.M."/>
+<person name="Fritz C."/>
+<person name="Fukuhara H."/>
+<person name="Gabel C."/>
+<person name="Gaillon L."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Garcia-Ramirez J.J."/>
+<person name="Gent M.E."/>
+<person name="Ghazvini M."/>
+<person name="Goffeau A."/>
+<person name="Gonzalez A."/>
+<person name="Grothues D."/>
+<person name="Guerreiro P."/>
+<person name="Hegemann J.H."/>
+<person name="Hewitt N."/>
+<person name="Hilger F."/>
+<person name="Hollenberg C.P."/>
+<person name="Horaitis O."/>
+<person name="Indge K.J."/>
+<person name="Jacquier A."/>
+<person name="James C.M."/>
+<person name="Jauniaux J.-C."/>
+<person name="Jimenez A."/>
+<person name="Keuchel H."/>
+<person name="Kirchrath L."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Legrain P."/>
+<person name="Liebl S."/>
+<person name="Louis E.J."/>
+<person name="Maia e Silva A."/>
+<person name="Marck C."/>
+<person name="Monnier A.-L."/>
+<person name="Moestl D."/>
+<person name="Mueller S."/>
+<person name="Obermaier B."/>
+<person name="Oliver S.G."/>
+<person name="Pallier C."/>
+<person name="Pascolo S."/>
+<person name="Pfeiffer F."/>
+<person name="Philippsen P."/>
+<person name="Planta R.J."/>
+<person name="Pohl F.M."/>
+<person name="Pohl T.M."/>
+<person name="Poehlmann R."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Puzos V."/>
+<person name="Ramezani Rad M."/>
+<person name="Rasmussen S.W."/>
+<person name="Remacha M.A."/>
+<person name="Revuelta J.L."/>
+<person name="Richard G.-F."/>
+<person name="Rieger M."/>
+<person name="Rodrigues-Pousada C."/>
+<person name="Rose M."/>
+<person name="Rupp T."/>
+<person name="Santos M.A."/>
+<person name="Schwager C."/>
+<person name="Sensen C."/>
+<person name="Skala J."/>
+<person name="Soares H."/>
+<person name="Sor F."/>
+<person name="Stegemann J."/>
+<person name="Tettelin H."/>
+<person name="Thierry A."/>
+<person name="Tzermia M."/>
+<person name="Urrestarazu L.A."/>
+<person name="van Dyck L."/>
+<person name="van Vliet-Reedijk J.C."/>
+<person name="Valens M."/>
+<person name="Vandenbol M."/>
+<person name="Vilela C."/>
+<person name="Vissers S."/>
+<person name="von Wettstein D."/>
+<person name="Voss H."/>
+<person name="Wiemann S."/>
+<person name="Xu G."/>
+<person name="Zimmermann J."/>
+<person name="Haasemann M."/>
+<person name="Becker I."/>
+<person name="Mewes H.-W."/>
+</authorList>
+<dbReference type="PubMed" id="8196765"/>
+<dbReference type="DOI" id="10.1038/369371a0"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1992" name="Proc. Natl. Acad. Sci. U.S.A." volume="89" first="8966" last="8970">
+<title>Divergent evolution of pyrimidine biosynthesis between anaerobic and aerobic yeasts.</title>
+<authorList>
+<person name="Nagy M."/>
+<person name="Lacroute F."/>
+<person name="Thomas D."/>
+</authorList>
+<dbReference type="PubMed" id="1409592"/>
+<dbReference type="DOI" id="10.1073/pnas.89.19.8966"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2000" name="Arch. Biochem. Biophys." volume="378" first="84" last="92">
+<title>Catalytic properties of dihydroorotate dehydrogenase from Saccharomyces cerevisiae: studies on pH, alternate substrates, and inhibitors.</title>
+<authorList>
+<person name="Jordan D.B."/>
+<person name="Bisaha J.J."/>
+<person name="Picollelli M.A."/>
+</authorList>
+<dbReference type="PubMed" id="10871048"/>
+<dbReference type="DOI" id="10.1006/abbi.2000.1823"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>SUBUNIT</scope>
+<scope>COFACTOR</scope>
+<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2004" name="FEBS Lett." volume="568" first="129" last="134">
+<title>Two different dihydroorotate dehydrogenases from yeast Saccharomyces kluyveri.</title>
+<authorList>
+<person name="Zameitat E."/>
+<person name="Knecht W."/>
+<person name="Piskur J."/>
+<person name="Loeffler M."/>
+</authorList>
+<dbReference type="PubMed" id="15196933"/>
+<dbReference type="DOI" id="10.1016/j.febslet.2004.05.017"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>CATALYTIC ACTIVITY</scope>
+<scope>SUBSTRATE SPECIFICITY</scope>
+<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2004" name="Mol. Genet. Genomics" volume="271" first="387" last="393">
+<title>Horizontal gene transfer promoted evolution of the ability to propagate under anaerobic conditions in yeasts.</title>
+<authorList>
+<person name="Gojkovic Z."/>
+<person name="Knecht W."/>
+<person name="Zameitat E."/>
+<person name="Warneboldt J."/>
+<person name="Coutelis J.-B."/>
+<person name="Pynyaha Y."/>
+<person name="Neuveglise C."/>
+<person name="Moeller K."/>
+<person name="Loeffler M."/>
+<person name="Piskur J."/>
+</authorList>
+<dbReference type="PubMed" id="15014982"/>
+<dbReference type="DOI" id="10.1007/s00438-004-0995-7"/>
+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2007" name="FEMS Yeast Res." volume="7" first="897" last="904">
+<title>Dihydroorotate dehydrogenase from Saccharomyces cerevisiae: spectroscopic investigations with the recombinant enzyme throw light on catalytic properties and metabolism of fumarate analogues.</title>
+<authorList>
+<person name="Zameitat E."/>
+<person name="Pierik A.J."/>
+<person name="Zocher K."/>
+<person name="Loeffler M."/>
+</authorList>
+<dbReference type="PubMed" id="17617217"/>
+<dbReference type="DOI" id="10.1111/j.1567-1364.2007.00275.x"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>BIOPHYSICOCHEMICAL PROPERTIES</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="2 3 5 7 8 9">Catalyzes the conversion of dihydroorotate to orotate with fumarate as the electron acceptor. Molecular oxygen can replace fumarate in vitro. Does not use oxaloacetate or NAD or NADP as electron acceptors.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="8">
+<text>(S)-dihydroorotate + fumarate = orotate + succinate</text>
+<dbReference type="Rhea" id="RHEA:30059"/>
+<dbReference type="ChEBI" id="CHEBI:29806"/>
+<dbReference type="ChEBI" id="CHEBI:30031"/>
+<dbReference type="ChEBI" id="CHEBI:30839"/>
+<dbReference type="ChEBI" id="CHEBI:30864"/>
+<dbReference type="EC" id="1.3.98.1"/>
+</reaction>
+</comment>
+<comment type="cofactor">
+<cofactor evidence="2">
+<name>FMN</name>
+<dbReference type="ChEBI" id="CHEBI:58210"/>
+</cofactor>
+<text evidence="2">Binds 1 FMN per subunit.</text>
+</comment>
+<comment type="activity regulation">
+<text>The activity is independent of the presence of oxygen.</text>
+</comment>
+<comment type="biophysicochemical properties">
+<kinetics>
+<KM evidence="2 8 9">8.4 uM for (S)-dihydroorotate (at pH 7.5)</KM>
+<KM evidence="2 8 9">45 uM for fumarate (at pH 7.5)</KM>
+<KM evidence="2 8 9">115 uM for 2,6-dichloroindophenol</KM>
+<Vmax evidence="2 8 9">20.4 umol/min/mg enzyme (with 2,6-dichloroindophenol as electron acceptor)</Vmax>
+<Vmax evidence="2 8 9">5.1 umol/min/mg enzyme (with fumarate as electron acceptor)</Vmax>
+</kinetics>
+<phDependence>
+<text evidence="2 8 9">Optimum pH is 8.5. Active from pH 7 to pH 10.</text>
+</phDependence>
+</comment>
+<comment type="pathway">
+<text>Pyrimidine metabolism; UMP biosynthesis via de novo pathway.</text>
+</comment>
+<comment type="subunit">
+<text evidence="2">Homodimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="3">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 264000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="10">Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.</text>
+</comment>
+<dbReference type="EC" id="1.3.98.1"/>
+<dbReference type="EMBL" id="M83295">
+<property type="protein sequence ID" value="AAA34566.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X59371">
+<property type="protein sequence ID" value="CAA42014.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AJ585637">
+<property type="protein sequence ID" value="CAE52157.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="protein sequence ID" value="CAE52158.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="AJ585639">
+<property type="protein sequence ID" value="CAE52159.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="AJ585640">
+<property type="protein sequence ID" value="CAE52160.1"/>
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+<property type="protein sequence ID" value="CAE52161.1"/>
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+<dbReference type="EMBL" id="AJ585644">
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+<property type="protein sequence ID" value="CAE52169.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AJ585650">
+<property type="protein sequence ID" value="CAE52170.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AJ585651">
+<property type="protein sequence ID" value="CAE52171.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X75951">
+<property type="protein sequence ID" value="CAA53557.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z28216">
+<property type="protein sequence ID" value="CAA82061.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006944">
+<property type="protein sequence ID" value="DAA08953.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="JC1276">
+<property type="entry name" value="JC1276"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_012706.1">
+<property type="nucleotide sequence ID" value="NM_001179781.1"/>
+</dbReference>
+<dbReference type="SMR" id="P28272"/>
+<dbReference type="BioGRID" id="33949">
+<property type="interactions" value="106"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-6573N"/>
+<dbReference type="IntAct" id="P28272">
+<property type="interactions" value="4"/>
+</dbReference>
+<dbReference type="MINT" id="P28272"/>
+<dbReference type="STRING" id="4932.YKL216W"/>
+<dbReference type="BindingDB" id="P28272"/>
+<dbReference type="ChEMBL" id="CHEMBL5621"/>
+<dbReference type="iPTMnet" id="P28272"/>
+<dbReference type="MaxQB" id="P28272"/>
+<dbReference type="PaxDb" id="P28272"/>
+<dbReference type="PRIDE" id="P28272"/>
+<dbReference type="EnsemblFungi" id="YKL216W_mRNA">
+<property type="protein sequence ID" value="YKL216W"/>
+<property type="gene ID" value="YKL216W"/>
+</dbReference>
+<dbReference type="GeneID" id="853664"/>
+<dbReference type="KEGG" id="sce:YKL216W"/>
+<dbReference type="SGD" id="S000001699">
+<property type="gene designation" value="URA1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YKL216W"/>
+<dbReference type="eggNOG" id="KOG1436">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00500000044896"/>
+<dbReference type="HOGENOM" id="CLU_042042_3_0_1"/>
+<dbReference type="InParanoid" id="P28272"/>
+<dbReference type="OMA" id="SCPHAKG"/>
+<dbReference type="BioCyc" id="MetaCyc:YKL216W-MONOMER"/>
+<dbReference type="SABIO-RK" id="P28272"/>
+<dbReference type="UniPathway" id="UPA00070"/>
+<dbReference type="PRO" id="PR:P28272"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XI"/>
+</dbReference>
+<dbReference type="RNAct" id="P28272">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0019898">
+<property type="term" value="C:extrinsic component of membrane"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:1990663">
+<property type="term" value="F:dihydroorotate dehydrogenase (fumarate) activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004152">
+<property type="term" value="F:dihydroorotate dehydrogenase activity"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006207">
+<property type="term" value="P:'de novo' pyrimidine nucleobase biosynthetic process"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0044205">
+<property type="term" value="P:'de novo' UMP biosynthetic process"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-UniPathway"/>
+</dbReference>
+<dbReference type="CDD" id="cd04741">
+<property type="entry name" value="DHOD_1A_like"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="2.30.26.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.20.20.70">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="HAMAP" id="MF_00224">
+<property type="entry name" value="DHO_dh_type1"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013785">
+<property type="entry name" value="Aldolase_TIM"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR033886">
+<property type="entry name" value="DHOD_1A"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR023359">
+<property type="entry name" value="Dihydro_DH_chainA_dom2"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR005720">
+<property type="entry name" value="Dihydroorotate_DH"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR024920">
+<property type="entry name" value="Dihydroorotate_DH_1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012135">
+<property type="entry name" value="Dihydroorotate_DH_1_2"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001295">
+<property type="entry name" value="Dihydroorotate_DH_CS"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01180">
+<property type="entry name" value="DHO_dh"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PIRSF" id="PIRSF000164">
+<property type="entry name" value="DHO_oxidase"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="TIGRFAMs" id="TIGR01037">
+<property type="entry name" value="pyrD_sub1_fam"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00911">
+<property type="entry name" value="DHODEHASE_1"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00912">
+<property type="entry name" value="DHODEHASE_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0285">Flavoprotein</keyword>
+<keyword id="KW-0288">FMN</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0560">Oxidoreductase</keyword>
+<keyword id="KW-0665">Pyrimidine biosynthesis</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="chain" description="Dihydroorotate dehydrogenase (fumarate)" id="PRO_0000148506">
+<location>
+<begin position="1"/>
+<end position="314"/>
+</location>
+</feature>
+<feature type="nucleotide phosphate-binding region" description="FMN" evidence="1">
+<location>
+<begin position="46"/>
+<end position="47"/>
+</location>
+</feature>
+<feature type="nucleotide phosphate-binding region" description="FMN" evidence="1">
+<location>
+<begin position="252"/>
+<end position="253"/>
+</location>
+</feature>
+<feature type="nucleotide phosphate-binding region" description="FMN" evidence="1">
+<location>
+<begin position="274"/>
+<end position="275"/>
+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="1">
+<location>
+<begin position="70"/>
+<end position="74"/>
+</location>
+</feature>
+<feature type="region of interest" description="Substrate binding" evidence="1">
+<location>
+<begin position="196"/>
+<end position="197"/>
+</location>
+</feature>
+<feature type="active site" description="Nucleophile" evidence="1">
+<location>
+<position position="133"/>
+</location>
+</feature>
+<feature type="binding site" description="Substrate" evidence="1">
+<location>
+<position position="46"/>
+</location>
+</feature>
+<feature type="binding site" description="FMN" evidence="1">
+<location>
+<position position="130"/>
+</location>
+</feature>
+<feature type="binding site" description="Substrate" evidence="1">
+<location>
+<position position="130"/>
+</location>
+</feature>
+<feature type="binding site" description="FMN" evidence="1">
+<location>
+<position position="167"/>
+</location>
+</feature>
+<feature type="binding site" description="FMN; via carbonyl oxygen" evidence="1">
+<location>
+<position position="195"/>
+</location>
+</feature>
+<feature type="binding site" description="FMN; via amide nitrogen" evidence="1">
+<location>
+<position position="224"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="11">
+<location>
+<position position="46"/>
+</location>
+</feature>
+<feature type="sequence variant" description="In strain: CLIB 95, CLIB 219, CLIB 382, CLIB 388, CLIB 413, CLIB 556, CLIB 630, K1, R12, R13, YIIc12 and YIIc17." evidence="6">
+<original>E</original>
+<variation>K</variation>
+<location>
+<position position="58"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000269">
+<source>
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+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
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+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
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+</evidence>
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+<source>
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+</source>
+</evidence>
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+<source>
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+</source>
+</evidence>
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+<source>
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+</evidence>
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+<source>
+<dbReference type="PubMed" id="15196933"/>
+</source>
+</evidence>
+<evidence key="9" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="17617217"/>
+</source>
+</evidence>
+<evidence key="10" type="ECO:0000305"/>
+<evidence key="11" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22106047"/>
+</source>
+</evidence>
+<sequence length="314" mass="34801" checksum="0F1FF9BDA7F8D68E" modified="1992-12-01" version="1">MTASLTTKFLNNTYENPFMNASGVHCMTTQELDELANSKAGAFITKSATTLEREGNPEPRYISVPLGSINSMGLPNEGIDYYLSYVLNRQKNYPDAPAIFFSVAGMSIDENLNLLRKIQDSEFNGITELNLSCPNVPGKPQVAYDFDLTKETLEKVFAFFKKPLGVKLPPYFDFAHFDIMAKILNEFPLAYVNSINSIGNGLFIDVEKESVVVKPKNGFGGIGGEYVKPTALANVRAFYTRLRPEIKVIGTGGIKSGKDAFEHLLCGASMLQIGTELQKEGVKIFERIEKELKDIMEAKGYTSIDQFRGKLNSI</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1993-04-01" modified="2021-04-07" version="184">
+<accession>Q00816</accession>
+<accession>D6VS13</accession>
+<name>REG1_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Resistance to glucose repression protein 1</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Protein HEX2</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Second-site suppressor of the rna1-1 mutation 1</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">REG1</name>
+<name type="synonym">HEX2</name>
+<name type="synonym">PZF240</name>
+<name type="synonym">SPP43</name>
+<name type="synonym">SRN1</name>
+<name type="ordered locus">YDR028C</name>
+<name type="ORF">YD9813.06C</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1991" name="Eur. J. Biochem." volume="200" first="311" last="319">
+<title>Characterization of Hex2 protein, a negative regulatory element necessary for glucose repression in yeast.</title>
+<authorList>
+<person name="Niederacher D."/>
+<person name="Entian K.-D."/>
+</authorList>
+<dbReference type="PubMed" id="1889400"/>
+<dbReference type="DOI" id="10.1111/j.1432-1033.1991.tb16187.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1992" name="Mol. Cell. Biol." volume="12" first="2673" last="2680">
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+<authorList>
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+</authorList>
+<dbReference type="PubMed" id="1588964"/>
+<dbReference type="DOI" id="10.1128/mcb.12.6.2673"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="3">
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+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
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+<person name="Bargues M."/>
+<person name="Baron L."/>
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+<person name="Kucaba T."/>
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+<person name="Mardis E."/>
+<person name="Menezes S."/>
+<person name="Miller N."/>
+<person name="Nhan M."/>
+<person name="Pauley A."/>
+<person name="Peluso D."/>
+<person name="Rifkin L."/>
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+<person name="Trevaskis E."/>
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+<person name="Mewes H.-W."/>
+<person name="Zollner A."/>
+<person name="Zaccaria P."/>
+</authorList>
+<dbReference type="PubMed" id="9169867"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
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+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
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+<person name="Costanzo M.C."/>
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+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
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+<person name="Miyasato S.R."/>
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+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
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+<authorList>
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+<person name="Sander C."/>
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+<dbReference type="PubMed" id="8896275"/>
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+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 775-1014</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1995" name="EMBO J." volume="14" first="5939" last="5946">
+<title>REG1 binds to protein phosphatase type 1 and regulates glucose repression in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Tu J.L."/>
+<person name="Carlson M."/>
+</authorList>
+<dbReference type="PubMed" id="8846786"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1995.tb00282.x"/>
+</citation>
+<scope>INTERACTION WITH PP1</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
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+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2005" name="Mol. Cell. Proteomics" volume="4" first="310" last="327">
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+<person name="Mohammed S."/>
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+<person name="Faergeman N.J."/>
+<person name="Mann M."/>
+<person name="Jensen O.N."/>
+</authorList>
+<dbReference type="PubMed" id="15665377"/>
+<dbReference type="DOI" id="10.1074/mcp.m400219-mcp200"/>
+</citation>
+<scope>ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2</scope>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>YAL6B</strain>
+</source>
+</reference>
+<reference key="9">
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+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
+<person name="Haas W."/>
+<person name="Villen J."/>
+<person name="Elias J.E."/>
+<person name="Gygi S.P."/>
+</authorList>
+<dbReference type="PubMed" id="17330950"/>
+<dbReference type="DOI" id="10.1021/pr060559j"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-421; SER-572 AND SER-576</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ADR376</strain>
+</source>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
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+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-73; SER-75; TYR-480 AND SER-490</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
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+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-254; SER-311; SER-421; SER-576 AND SER-680</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-242; SER-421; SER-570; SER-572; SER-576; SER-610; SER-614; THR-896; SER-898 AND SER-980</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2011" name="Eukaryot. Cell" volume="10" first="313" last="319">
+<title>Interaction of SNF1 protein kinase with its activating kinase Sak1.</title>
+<authorList>
+<person name="Liu Y."/>
+<person name="Xu X."/>
+<person name="Carlson M."/>
+</authorList>
+<dbReference type="PubMed" id="21216941"/>
+<dbReference type="DOI" id="10.1128/ec.00291-10"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH SAK1</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS]</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="3">Involved in RNA processing and negative regulation of glucose repression. Regulates the level of two antigens, P43 and P70. Binds to protein phosphatase type 1. Functions with REG2 and SNF1 protein kinase to regulate growth. Might regulate SNF1 directly or indirectly.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 4">Interacts with SAK1.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8270">
+<id>Q00816</id>
+</interactant>
+<interactant intactId="EBI-13715">
+<id>P32598</id>
+<label>GLC7</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>4</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-8270">
+<id>Q00816</id>
+</interactant>
+<interactant intactId="EBI-17516">
+<id>P06782</id>
+<label>SNF1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>7</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 2560 molecules/cell in log phase SD medium.</text>
+</comment>
+<dbReference type="EMBL" id="M33703">
+<property type="protein sequence ID" value="AAA34670.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="protein sequence ID" value="CAA87807.1"/>
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+<dbReference type="EMBL" id="Z74324">
+<property type="protein sequence ID" value="CAA98850.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="X95966">
+<property type="protein sequence ID" value="CAA65223.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006938">
+<property type="protein sequence ID" value="DAA11873.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S32613">
+<property type="entry name" value="S32613"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_010311.1">
+<property type="nucleotide sequence ID" value="NM_001180336.1"/>
+</dbReference>
+<dbReference type="SMR" id="Q00816"/>
+<dbReference type="BioGRID" id="32078">
+<property type="interactions" value="139"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1266">
+<property type="entry name" value="REG1-GLC7 phosphatase complex"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-2513N"/>
+<dbReference type="ELM" id="Q00816"/>
+<dbReference type="IntAct" id="Q00816">
+<property type="interactions" value="24"/>
+</dbReference>
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+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2008" name="Mol. Cell. Biol." volume="28" first="1313" last="1325">
+<title>Phosphorylation by casein kinase 2 regulates Nap1 localization and function.</title>
+<authorList>
+<person name="Calvert M.E.K."/>
+<person name="Keck K.M."/>
+<person name="Ptak C."/>
+<person name="Shabanowitz J."/>
+<person name="Hunt D.F."/>
+<person name="Pemberton L.F."/>
+</authorList>
+<dbReference type="PubMed" id="18086883"/>
+<dbReference type="DOI" id="10.1128/mcb.01035-07"/>
+</citation>
+<scope>INTERACTION WITH NAP1</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-116</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="960" last="972">
+<title>Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases.</title>
+<authorList>
+<person name="Couttas T.A."/>
+<person name="Raftery M.J."/>
+<person name="Padula M.P."/>
+<person name="Herbert B.R."/>
+<person name="Wilkins M.R."/>
+</authorList>
+<dbReference type="PubMed" id="22522802"/>
+<dbReference type="DOI" id="10.1002/pmic.201100570"/>
+</citation>
+<scope>METHYLATION AT LYS-50</scope>
+</reference>
+<reference key="15">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
+<person name="Moore P.B."/>
+<person name="Noller H.F."/>
+<person name="Ortega J."/>
+<person name="Panse V.G."/>
+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="16">
+<citation type="journal article" date="2012" name="Nat. Struct. Mol. Biol." volume="19" first="1228" last="1233">
+<title>Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to the 60S ribosomal subunit.</title>
+<authorList>
+<person name="Greber B.J."/>
+<person name="Boehringer D."/>
+<person name="Montellese C."/>
+<person name="Ban N."/>
+</authorList>
+<dbReference type="PubMed" id="23142985"/>
+<dbReference type="DOI" id="10.1038/nsmb.2425"/>
+</citation>
+<scope>STRUCTURE BY ELECTRON MICROSCOPY (8.10 ANGSTROMS)</scope>
+</reference>
+<comment type="function">
+<text evidence="10">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="4 5 11">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). eL18 interacts with NAP1 (PubMed:18086883).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="2 5">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="mass spectrometry" mass="20419.431" method="Electrospray" evidence="1">
+<text>Monoisotopic mass.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 63700 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="9">There are 2 genes for eL18 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="9">Belongs to the eukaryotic ribosomal protein eL18 family.</text>
+</comment>
+<dbReference type="EMBL" id="X01100">
+<property type="protein sequence ID" value="CAA25574.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="U23084">
+<property type="protein sequence ID" value="AAC49097.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z71577">
+<property type="protein sequence ID" value="CAA96219.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006947">
+<property type="protein sequence ID" value="DAA10259.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S05867">
+<property type="entry name" value="R5BY8E"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_014098.1">
+<property type="nucleotide sequence ID" value="NM_001183139.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_014521.1">
+<property type="nucleotide sequence ID" value="NM_001183374.1"/>
+</dbReference>
+<dbReference type="PDB" id="4V8T">
+<property type="method" value="EM"/>
+<property type="resolution" value="8.10"/>
+<property type="chains" value="Q=1-186"/>
+</dbReference>
+<dbReference type="PDBsum" id="4V8T"/>
+<dbReference type="SMR" id="P0CX50"/>
+<dbReference type="BioGRID" id="34281">
+<property type="interactions" value="94"/>
+</dbReference>
+<dbReference type="BioGRID" id="35537">
+<property type="interactions" value="128"/>
+</dbReference>
+<dbReference type="IntAct" id="P0CX50">
+<property type="interactions" value="2"/>
+</dbReference>
+<dbReference type="MINT" id="P0CX50"/>
+<dbReference type="CarbonylDB" id="P0CX50"/>
+<dbReference type="iPTMnet" id="P0CX50"/>
+<dbReference type="PRIDE" id="P0CX50"/>
+<dbReference type="EnsemblFungi" id="YNL301C_mRNA">
+<property type="protein sequence ID" value="YNL301C"/>
+<property type="gene ID" value="YNL301C"/>
+</dbReference>
+<dbReference type="EnsemblFungi" id="YOL120C_mRNA">
+<property type="protein sequence ID" value="YOL120C"/>
+<property type="gene ID" value="YOL120C"/>
+</dbReference>
+<dbReference type="GeneID" id="854029"/>
+<dbReference type="GeneID" id="855415"/>
+<dbReference type="KEGG" id="sce:YNL301C"/>
+<dbReference type="KEGG" id="sce:YOL120C"/>
+<dbReference type="SGD" id="S000005245">
+<property type="gene designation" value="RPL18B"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00390000012976"/>
+<dbReference type="HOGENOM" id="CLU_080024_0_1_1"/>
+<dbReference type="InParanoid" id="P0CX50"/>
+<dbReference type="OMA" id="TNRPPMS"/>
+<dbReference type="Reactome" id="R-SCE-156827">
+<property type="pathway name" value="L13a-mediated translational silencing of Ceruloplasmin expression"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-1799339">
+<property type="pathway name" value="SRP-dependent cotranslational protein targeting to membrane"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72689">
+<property type="pathway name" value="Formation of a pool of free 40S subunits"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72706">
+<property type="pathway name" value="GTP hydrolysis and joining of the 60S ribosomal subunit"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975956">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975957">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="PRO" id="PR:P0CX50"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XIV"/>
+</dbReference>
+<dbReference type="RNAct" id="P0CX50">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="ExpressionAtlas" id="P0CX50">
+<property type="expression patterns" value="differential"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="GO" id="GO:0022625">
+<property type="term" value="C:cytosolic large ribosomal subunit"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003735">
+<property type="term" value="F:structural constituent of ribosome"/>
+<property type="evidence" value="ECO:0000305"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0002181">
+<property type="term" value="P:cytoplasmic translation"/>
+<property type="evidence" value="ECO:0000305"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006415">
+<property type="term" value="P:translational termination"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036227">
+<property type="entry name" value="L18e/L15P_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000039">
+<property type="entry name" value="Ribosomal_L18e"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR021131">
+<property type="entry name" value="Ribosomal_L18e/L15P"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR021132">
+<property type="entry name" value="Ribosomal_L18e_CS"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR10934">
+<property type="entry name" value="PTHR10934"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF17135">
+<property type="entry name" value="Ribosomal_L18"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF52080">
+<property type="entry name" value="SSF52080"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS01106">
+<property type="entry name" value="RIBOSOMAL_L18E"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0488">Methylation</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="1">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="60S ribosomal protein L18-B" id="PRO_0000409771">
+<location>
+<begin position="2"/>
+<end position="186"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6,N6,N6-trimethyllysine" evidence="6">
+<location>
+<position position="50"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="12">
+<location>
+<position position="116"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11983894"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="18086883"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22522802"/>
+</source>
+</evidence>
+<evidence key="7" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="24524803"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="9" type="ECO:0000305"/>
+<evidence key="10" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="11" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="12" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22106047"/>
+</source>
+</evidence>
+<sequence length="186" mass="20563" checksum="D097B187F369EACD" modified="2011-06-28" version="1">MGIDHTSKQHKRSGHRTAPKSDNVYLKLLVKLYTFLARRTDAPFNKVVLKALFLSKINRPPVSVSRIARALKQEGAANKTVVVVGTVTDDARIFEFPKTTVAALRFTAGARAKIVKAGGECITLDQLAVRAPKGQNTLILRGPRNSREAVRHFGMGPHKGKAPRILSTGRKFERARGRRRSKGFKV</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2021-04-07" version="88">
+<accession>P0CX82</accession>
+<accession>D6VPX3</accession>
+<accession>P05735</accession>
+<name>RL19A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="8">60S ribosomal protein L19-A</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>L23</fullName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="7">Large ribosomal subunit protein eL19-A</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>RP15L</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>RP33</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>YL14</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="8">RPL19A</name>
+<name type="synonym">RPL23A</name>
+<name type="synonym">YL14A</name>
+<name type="ordered locus">YBR084C-A</name>
+<name type="ORF">YBR084BC</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="383" last="389">
+<title>Nucleotide sequence and characterization of the Saccharomyces cerevisiae RPL19A gene encoding a homolog of the mammalian ribosomal protein L19.</title>
+<authorList>
+<person name="Song J.M."/>
+<person name="Cheung E."/>
+<person name="Rabinowitz J.C."/>
+</authorList>
+<dbReference type="PubMed" id="7785339"/>
+<dbReference type="DOI" id="10.1002/yea.320110411"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="submission" date="1993-07" db="EMBL/GenBank/DDBJ databases">
+<authorList>
+<person name="Suzuki K."/>
+<person name="Tomiyoshi A."/>
+<person name="Otaka E."/>
+</authorList>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [MRNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1994" name="EMBO J." volume="13" first="5795" last="5809">
+<title>Complete DNA sequence of yeast chromosome II.</title>
+<authorList>
+<person name="Feldmann H."/>
+<person name="Aigle M."/>
+<person name="Aljinovic G."/>
+<person name="Andre B."/>
+<person name="Baclet M.C."/>
+<person name="Barthe C."/>
+<person name="Baur A."/>
+<person name="Becam A.-M."/>
+<person name="Biteau N."/>
+<person name="Boles E."/>
+<person name="Brandt T."/>
+<person name="Brendel M."/>
+<person name="Brueckner M."/>
+<person name="Bussereau F."/>
+<person name="Christiansen C."/>
+<person name="Contreras R."/>
+<person name="Crouzet M."/>
+<person name="Cziepluch C."/>
+<person name="Demolis N."/>
+<person name="Delaveau T."/>
+<person name="Doignon F."/>
+<person name="Domdey H."/>
+<person name="Duesterhus S."/>
+<person name="Dubois E."/>
+<person name="Dujon B."/>
+<person name="El Bakkoury M."/>
+<person name="Entian K.-D."/>
+<person name="Feuermann M."/>
+<person name="Fiers W."/>
+<person name="Fobo G.M."/>
+<person name="Fritz C."/>
+<person name="Gassenhuber J."/>
+<person name="Glansdorff N."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="de Haan M."/>
+<person name="Hein C."/>
+<person name="Herbert C.J."/>
+<person name="Hollenberg C.P."/>
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+<comment type="function">
+<text evidence="10">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eL19 may play a role in the last stages of translation initiation, in particular subunit joining and shedding/releasing factors.</text>
+</comment>
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+<text evidence="5 11">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eL19 lies in close proximity to the binding site for eukaryotic initiation factor eIF4G (PubMed:9559554, PubMed:22096102).</text>
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+<comment type="mass spectrometry" mass="21573.159" method="Electrospray" evidence="1">
+<text>Average mass.</text>
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+<comment type="miscellaneous">
+<text evidence="3">Present with 97700 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="9">There are 2 genes for eL19 in yeast.</text>
+</comment>
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+<text evidence="9">Belongs to the eukaryotic ribosomal protein eL19 family.</text>
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+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
+<person name="Moore P.B."/>
+<person name="Noller H.F."/>
+<person name="Ortega J."/>
+<person name="Panse V.G."/>
+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<comment type="function">
+<text evidence="7">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 8">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1 3">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 54200 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="6">There are 2 genes for eL13 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the eukaryotic ribosomal protein eL13 family.</text>
+</comment>
+<dbReference type="EMBL" id="Z47071">
+<property type="protein sequence ID" value="CAA87356.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006946">
+<property type="protein sequence ID" value="DAA10038.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
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+<property type="entry name" value="S50398"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013862.1">
+<property type="nucleotide sequence ID" value="NM_001182644.1"/>
+</dbReference>
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+<property type="method" value="EM"/>
+<property type="resolution" value="3.70"/>
+<property type="chains" value="L=1-199"/>
+</dbReference>
+<dbReference type="PDBsum" id="4V91"/>
+<dbReference type="SMR" id="P40212"/>
+<dbReference type="BioGRID" id="35318">
+<property type="interactions" value="84"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-2591N"/>
+<dbReference type="IntAct" id="P40212">
+<property type="interactions" value="61"/>
+</dbReference>
+<dbReference type="MINT" id="P40212"/>
+<dbReference type="STRING" id="4932.YMR142C"/>
+<dbReference type="iPTMnet" id="P40212"/>
+<dbReference type="MaxQB" id="P40212"/>
+<dbReference type="PaxDb" id="P40212"/>
+<dbReference type="PRIDE" id="P40212"/>
+<dbReference type="TopDownProteomics" id="P40212"/>
+<dbReference type="EnsemblFungi" id="YMR142C_mRNA">
+<property type="protein sequence ID" value="YMR142C"/>
+<property type="gene ID" value="YMR142C"/>
+</dbReference>
+<dbReference type="GeneID" id="855173"/>
+<dbReference type="KEGG" id="sce:YMR142C"/>
+<dbReference type="SGD" id="S000004750">
+<property type="gene designation" value="RPL13B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YMR142C"/>
+<dbReference type="eggNOG" id="KOG3295">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00390000007818"/>
+<dbReference type="HOGENOM" id="CLU_075696_1_0_1"/>
+<dbReference type="InParanoid" id="P40212"/>
+<dbReference type="OMA" id="KVRRHEN"/>
+<dbReference type="Reactome" id="R-SCE-156827">
+<property type="pathway name" value="L13a-mediated translational silencing of Ceruloplasmin expression"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-1799339">
+<property type="pathway name" value="SRP-dependent cotranslational protein targeting to membrane"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72689">
+<property type="pathway name" value="Formation of a pool of free 40S subunits"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72706">
+<property type="pathway name" value="GTP hydrolysis and joining of the 60S ribosomal subunit"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975956">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975957">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="ChiTaRS" id="RPL16A">
+<property type="organism name" value="yeast"/>
+</dbReference>
+<dbReference type="PRO" id="PR:P40212"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XIII"/>
+</dbReference>
+<dbReference type="RNAct" id="P40212">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="GO" id="GO:0022625">
+<property type="term" value="C:cytosolic large ribosomal subunit"/>
+<property type="evidence" value="ECO:0000314"/>
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+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003735">
+<property type="term" value="F:structural constituent of ribosome"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0002181">
+<property type="term" value="P:cytoplasmic translation"/>
+<property type="evidence" value="ECO:0000305"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0016236">
+<property type="term" value="P:macroautophagy"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006415">
+<property type="term" value="P:translational termination"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="HAMAP" id="MF_00499">
+<property type="entry name" value="Ribosomal_L13e"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001380">
+<property type="entry name" value="Ribosomal_L13e"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR018256">
+<property type="entry name" value="Ribosomal_L13e_CS"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR11722">
+<property type="entry name" value="PTHR11722"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01294">
+<property type="entry name" value="Ribosomal_L13e"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS01104">
+<property type="entry name" value="RIBOSOMAL_L13E"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<feature type="chain" description="60S ribosomal protein L13-B" id="PRO_0000192939">
+<location>
+<begin position="1"/>
+<end position="199"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphothreonine" evidence="9">
+<location>
+<position position="144"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphothreonine" evidence="9">
+<location>
+<position position="152"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="24524803"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000305"/>
+<evidence key="7" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="9" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="19779198"/>
+</source>
+</evidence>
+<sequence length="199" mass="22525" checksum="BEA3B423EE76EF23" modified="1995-02-01" version="1">MAISKNLPILKNHFRKHWQERVKVHFDQAGKKVSRRNARAARAAKIAPRPLDLLRPVVRAPTVKYNRKVRAGRGFTLAEVKAAGLTAAYARTIGIAVDHRRQNRNQEIFDANVQRLKEYQSKIIVFPRDGKAPEAEQVLSAAATFPIAQPATDVEARAVQDNGESAFRTLRLARSEKKFRGIREKRAREKAEAEAEKKK</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1997-11-01" modified="2021-04-07" version="173">
+<accession>Q12690</accession>
+<accession>D6VRR7</accession>
+<name>RL13A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="6">60S ribosomal protein L13-A</fullName>
+</recommendedName>
+<alternativeName>
+<fullName evidence="5">Large ribosomal subunit protein eL13-A</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="6">RPL13A</name>
+<name type="ordered locus">YDL082W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="75" last="78">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
+<person name="Jacq C."/>
+<person name="Alt-Moerbe J."/>
+<person name="Andre B."/>
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+<person name="Bahr A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Bargues M."/>
+<person name="Baron L."/>
+<person name="Becker A."/>
+<person name="Biteau N."/>
+<person name="Bloecker H."/>
+<person name="Blugeon C."/>
+<person name="Boskovic J."/>
+<person name="Brandt P."/>
+<person name="Brueckner M."/>
+<person name="Buitrago M.J."/>
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+</authorList>
+<dbReference type="PubMed" id="9169867"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
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+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
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+</citation>
+<scope>NOMENCLATURE</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="4">
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+<person name="Lindahl L."/>
+<person name="Liljas A."/>
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+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
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+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
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+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
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+<reference key="7">
+<citation type="journal article" date="2010" name="Science" volume="330" first="1203" last="1209">
+<title>Crystal structure of the eukaryotic ribosome.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
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+<scope>X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME</scope>
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+<reference key="8">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
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+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME</scope>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<comment type="function">
+<text evidence="8">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="4 9">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<location evidence="2 4">Cytoplasm</location>
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+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 133000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="7">There are 2 genes for eL13 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="7">Belongs to the eukaryotic ribosomal protein eL13 family.</text>
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+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
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+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
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+<comment type="function">
+<text evidence="8">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
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+<text evidence="4 9">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<text evidence="7">There are 2 genes for uL13 in yeast.</text>
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+<scope>NOMENCLATURE</scope>
+</reference>
+<comment type="function">
+<text evidence="10">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eL19 may play a role in the last stages of translation initiation, in particular subunit joining and shedding/releasing factors.</text>
+</comment>
+<comment type="subunit">
+<text evidence="5 11">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eL19 lies in close proximity to the binding site for eukaryotic initiation factor eIF4G (PubMed:9559554, PubMed:22096102).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="2 5">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="mass spectrometry" mass="21573.159" method="Electrospray" evidence="1">
+<text>Average mass.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 225000 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="9">There are 2 genes for eL19 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="9">Belongs to the eukaryotic ribosomal protein eL19 family.</text>
+</comment>
+<comment type="sequence caution" evidence="9">
+<conflict type="erroneous gene model prediction">
+<sequence resource="EMBL-CDS" id="CAA54504" version="1"/>
+</conflict>
+</comment>
+<dbReference type="EMBL" id="U16015">
+<property type="protein sequence ID" value="AAB60318.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="D17338">
+<property type="protein sequence ID" value="BAA04156.1"/>
+<property type="molecule type" value="mRNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X77291">
+<property type="protein sequence ID" value="CAA54504.1"/>
+<property type="status" value="ALT_SEQ"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z35788">
+<property type="protein sequence ID" value="CAA84846.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006936">
+<property type="protein sequence ID" value="DAA07093.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S44597">
+<property type="entry name" value="S44597"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_009526.1">
+<property type="nucleotide sequence ID" value="NM_001178267.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_009641.1">
+<property type="nucleotide sequence ID" value="NM_001180057.1"/>
+</dbReference>
+<dbReference type="PDB" id="4V8T">
+<property type="method" value="EM"/>
+<property type="resolution" value="8.10"/>
+<property type="chains" value="R=1-189"/>
+</dbReference>
+<dbReference type="PDB" id="4V8Y">
+<property type="method" value="EM"/>
+<property type="resolution" value="4.30"/>
+<property type="chains" value="BR=2-189"/>
+</dbReference>
+<dbReference type="PDB" id="4V8Z">
+<property type="method" value="EM"/>
+<property type="resolution" value="6.60"/>
+<property type="chains" value="BR=2-189"/>
+</dbReference>
+<dbReference type="PDBsum" id="4V8T"/>
+<dbReference type="PDBsum" id="4V8Y"/>
+<dbReference type="PDBsum" id="4V8Z"/>
+<dbReference type="SMR" id="P0CX83"/>
+<dbReference type="BioGRID" id="32671">
+<property type="interactions" value="286"/>
+</dbReference>
+<dbReference type="BioGRID" id="32789">
+<property type="interactions" value="138"/>
+</dbReference>
+<dbReference type="IntAct" id="P0CX83">
+<property type="interactions" value="4"/>
+</dbReference>
+<dbReference type="MINT" id="P0CX83"/>
+<dbReference type="BindingDB" id="P0CX83"/>
+<dbReference type="CarbonylDB" id="P0CX83"/>
+<dbReference type="iPTMnet" id="P0CX83"/>
+<dbReference type="PRIDE" id="P0CX83"/>
+<dbReference type="EnsemblFungi" id="YBL027W_mRNA">
+<property type="protein sequence ID" value="YBL027W"/>
+<property type="gene ID" value="YBL027W"/>
+</dbReference>
+<dbReference type="EnsemblFungi" id="YBR084C-A_mRNA">
+<property type="protein sequence ID" value="YBR084C-A"/>
+<property type="gene ID" value="YBR084C-A"/>
+</dbReference>
+<dbReference type="GeneID" id="852254"/>
+<dbReference type="GeneID" id="852379"/>
+<dbReference type="KEGG" id="sce:YBL027W"/>
+<dbReference type="KEGG" id="sce:YBR084C-A"/>
+<dbReference type="SGD" id="S000000123">
+<property type="gene designation" value="RPL19B"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00390000012628"/>
+<dbReference type="HOGENOM" id="CLU_083919_0_0_1"/>
+<dbReference type="InParanoid" id="P0CX83"/>
+<dbReference type="OMA" id="NRVWIDP"/>
+<dbReference type="Reactome" id="R-SCE-156827">
+<property type="pathway name" value="L13a-mediated translational silencing of Ceruloplasmin expression"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-1799339">
+<property type="pathway name" value="SRP-dependent cotranslational protein targeting to membrane"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72689">
+<property type="pathway name" value="Formation of a pool of free 40S subunits"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72706">
+<property type="pathway name" value="GTP hydrolysis and joining of the 60S ribosomal subunit"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975956">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975957">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="PRO" id="PR:P0CX83"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome II"/>
+</dbReference>
+<dbReference type="RNAct" id="P0CX83">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="ExpressionAtlas" id="P0CX83">
+<property type="expression patterns" value="differential"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="GO" id="GO:0022625">
+<property type="term" value="C:cytosolic large ribosomal subunit"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003735">
+<property type="term" value="F:structural constituent of ribosome"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0002181">
+<property type="term" value="P:cytoplasmic translation"/>
+<property type="evidence" value="ECO:0000305"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006415">
+<property type="term" value="P:translational termination"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="CDD" id="cd01417">
+<property type="entry name" value="Ribosomal_L19e_E"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="1.10.1650.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="HAMAP" id="MF_01475">
+<property type="entry name" value="Ribosomal_L19e"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR035970">
+<property type="entry name" value="60S_ribosomal_L19/L19e_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000196">
+<property type="entry name" value="Ribosomal_L19/L19e"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR023638">
+<property type="entry name" value="Ribosomal_L19/L19e_CS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015972">
+<property type="entry name" value="Ribosomal_L19/L19e_dom1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR033935">
+<property type="entry name" value="Ribosomal_L19_euka"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR039547">
+<property type="entry name" value="RPL19"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR10722">
+<property type="entry name" value="PTHR10722"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01280">
+<property type="entry name" value="Ribosomal_L19e"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM01416">
+<property type="entry name" value="Ribosomal_L19e"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF48140">
+<property type="entry name" value="SSF48140"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00526">
+<property type="entry name" value="RIBOSOMAL_L19E"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="4 6">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="60S ribosomal protein L19-B" id="PRO_0000410446">
+<location>
+<begin position="2"/>
+<end position="189"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="12">
+<location>
+<position position="30"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="12">
+<location>
+<position position="37"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="12">
+<location>
+<position position="91"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="21"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="53"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="60"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="146"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="186"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11983894"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="1544921"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="6355773"/>
+</source>
+</evidence>
+<evidence key="7" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="24524803"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="9" type="ECO:0000305"/>
+<evidence key="10" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="11" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="12" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="19779198"/>
+</source>
+</evidence>
+<evidence key="13" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22106047"/>
+</source>
+</evidence>
+<sequence length="189" mass="21704" checksum="776C3AB3D348EE99" modified="2011-06-28" version="1">MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1993-07-01" modified="2021-04-07" version="179">
+<accession>Q02753</accession>
+<accession>D6VQI5</accession>
+<name>RL21A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="6">60S ribosomal protein L21-A</fullName>
+</recommendedName>
+<alternativeName>
+<fullName evidence="5">Large ribosomal subunit protein eL21-A</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="6">RPL21A</name>
+<name type="synonym">URP1</name>
+<name type="ordered locus">YBR191W</name>
+<name type="ORF">YBR1401</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1993" name="Curr. Genet." volume="23" first="15" last="18">
+<title>Yeast single copy gene URP1 is a homolog of rat ribosomal protein gene L21.</title>
+<authorList>
+<person name="Jank B."/>
+<person name="Waldherr M."/>
+<person name="Schweyen R.J."/>
+</authorList>
+<dbReference type="PubMed" id="8428379"/>
+<dbReference type="DOI" id="10.1007/bf00336743"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1994" name="EMBO J." volume="13" first="5795" last="5809">
+<title>Complete DNA sequence of yeast chromosome II.</title>
+<authorList>
+<person name="Feldmann H."/>
+<person name="Aigle M."/>
+<person name="Aljinovic G."/>
+<person name="Andre B."/>
+<person name="Baclet M.C."/>
+<person name="Barthe C."/>
+<person name="Baur A."/>
+<person name="Becam A.-M."/>
+<person name="Biteau N."/>
+<person name="Boles E."/>
+<person name="Brandt T."/>
+<person name="Brendel M."/>
+<person name="Brueckner M."/>
+<person name="Bussereau F."/>
+<person name="Christiansen C."/>
+<person name="Contreras R."/>
+<person name="Crouzet M."/>
+<person name="Cziepluch C."/>
+<person name="Demolis N."/>
+<person name="Delaveau T."/>
+<person name="Doignon F."/>
+<person name="Domdey H."/>
+<person name="Duesterhus S."/>
+<person name="Dubois E."/>
+<person name="Dujon B."/>
+<person name="El Bakkoury M."/>
+<person name="Entian K.-D."/>
+<person name="Feuermann M."/>
+<person name="Fiers W."/>
+<person name="Fobo G.M."/>
+<person name="Fritz C."/>
+<person name="Gassenhuber J."/>
+<person name="Glansdorff N."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="de Haan M."/>
+<person name="Hein C."/>
+<person name="Herbert C.J."/>
+<person name="Hollenberg C.P."/>
+<person name="Holmstroem K."/>
+<person name="Jacq C."/>
+<person name="Jacquet M."/>
+<person name="Jauniaux J.-C."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kallesoee T."/>
+<person name="Kiesau P."/>
+<person name="Kirchrath L."/>
+<person name="Koetter P."/>
+<person name="Korol S."/>
+<person name="Liebl S."/>
+<person name="Logghe M."/>
+<person name="Lohan A.J.E."/>
+<person name="Louis E.J."/>
+<person name="Li Z.Y."/>
+<person name="Maat M.J."/>
+<person name="Mallet L."/>
+<person name="Mannhaupt G."/>
+<person name="Messenguy F."/>
+<person name="Miosga T."/>
+<person name="Molemans F."/>
+<person name="Mueller S."/>
+<person name="Nasr F."/>
+<person name="Obermaier B."/>
+<person name="Perea J."/>
+<person name="Pierard A."/>
+<person name="Piravandi E."/>
+<person name="Pohl F.M."/>
+<person name="Pohl T.M."/>
+<person name="Potier S."/>
+<person name="Proft M."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rieger M."/>
+<person name="Rose M."/>
+<person name="Schaaff-Gerstenschlaeger I."/>
+<person name="Scherens B."/>
+<person name="Schwarzlose C."/>
+<person name="Skala J."/>
+<person name="Slonimski P.P."/>
+<person name="Smits P.H.M."/>
+<person name="Souciet J.-L."/>
+<person name="Steensma H.Y."/>
+<person name="Stucka R."/>
+<person name="Urrestarazu L.A."/>
+<person name="van der Aart Q.J.M."/>
+<person name="Van Dyck L."/>
+<person name="Vassarotti A."/>
+<person name="Vetter I."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Wagner G."/>
+<person name="de Wergifosse P."/>
+<person name="Wolfe K.H."/>
+<person name="Zagulski M."/>
+<person name="Zimmermann F.K."/>
+<person name="Mewes H.-W."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="7813418"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1994.tb06923.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1994" name="Yeast" volume="10" first="1511" last="1525">
+<title>A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes encoding ribosomal proteins and six putative new genes, one of which encodes a putative transcriptional factor.</title>
+<authorList>
+<person name="Demolis N."/>
+<person name="Jacquet M."/>
+<person name="Mallet L."/>
+</authorList>
+<dbReference type="PubMed" id="7871891"/>
+<dbReference type="DOI" id="10.1002/yea.320101116"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1993" name="Yeast" volume="9" first="645" last="659">
+<title>RIM2, MSI1 and PGI1 are located within an 8 kb segment of Saccharomyces cerevisiae chromosome II, which also contains the putative ribosomal gene L21 and a new putative essential gene with a leucine zipper motif.</title>
+<authorList>
+<person name="Demolis N."/>
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+<person name="Jacquet M."/>
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+<strain>ATCC 204508 / S288c</strain>
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+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
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+<citation type="journal article" date="1999" name="J. Biol. Chem." volume="274" first="37035" last="37040">
+<title>The action of N-terminal acetyltransferases on yeast ribosomal proteins.</title>
+<authorList>
+<person name="Arnold R.J."/>
+<person name="Polevoda B."/>
+<person name="Reilly J.P."/>
+<person name="Sherman F."/>
+</authorList>
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+<dbReference type="DOI" id="10.1074/jbc.274.52.37035"/>
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+<scope>CLEAVAGE OF INITIATOR METHIONINE</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
+<person name="Moore P.B."/>
+<person name="Noller H.F."/>
+<person name="Ortega J."/>
+<person name="Panse V.G."/>
+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
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+<reference key="10">
+<citation type="journal article" date="2001" name="Cell" volume="107" first="373" last="386">
+<title>Structure of the 80S ribosome from Saccharomyces cerevisiae -- tRNA-ribosome and subunit-subunit interactions.</title>
+<authorList>
+<person name="Spahn C.M.T."/>
+<person name="Beckmann R."/>
+<person name="Eswar N."/>
+<person name="Penczek P.A."/>
+<person name="Sali A."/>
+<person name="Blobel G."/>
+<person name="Frank J."/>
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+</reference>
+<reference key="11">
+<citation type="journal article" date="2004" name="EMBO J." volume="23" first="1008" last="1019">
+<title>Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation.</title>
+<authorList>
+<person name="Spahn C.M.T."/>
+<person name="Gomez-Lorenzo M.G."/>
+<person name="Grassucci R.A."/>
+<person name="Joergensen R."/>
+<person name="Andersen G.R."/>
+<person name="Beckmann R."/>
+<person name="Penczek P.A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Frank J."/>
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+<scope>3D-STRUCTURE MODELING OF 2-100</scope>
+<scope>ELECTRON MICROSCOPY</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2010" name="Science" volume="330" first="1203" last="1209">
+<title>Crystal structure of the eukaryotic ribosome.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="21109664"/>
+<dbReference type="DOI" id="10.1126/science.1194294"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME</scope>
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+</reference>
+<comment type="function">
+<text evidence="8">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="4 9">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<text evidence="7">There are 2 genes for eL21 in yeast.</text>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="93" last="98">
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+<scope>ACETYLATION AT SER-2 BY NATA</scope>
+</reference>
+<reference key="5">
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+<reference key="7">
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+<reference key="8">
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+<person name="Smolka M.B."/>
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+<reference key="10">
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+<reference key="11">
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+<authorList>
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+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
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+<reference key="14">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
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+<authorList>
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+<person name="Beckmann R."/>
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+<text evidence="7">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
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+<text evidence="3 8">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<text evidence="1 2">N-terminally acetylated by acetyltransferase NatA.</text>
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+<text evidence="6">There are 2 genes for uL13 in yeast.</text>
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+<person name="Beckmann R."/>
+<person name="Eswar N."/>
+<person name="Penczek P.A."/>
+<person name="Sali A."/>
+<person name="Blobel G."/>
+<person name="Frank J."/>
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+<citation type="journal article" date="2004" name="EMBO J." volume="23" first="1008" last="1019">
+<title>Domain movements of elongation factor eEF2 and the eukaryotic 80S ribosome facilitate tRNA translocation.</title>
+<authorList>
+<person name="Spahn C.M.T."/>
+<person name="Gomez-Lorenzo M.G."/>
+<person name="Grassucci R.A."/>
+<person name="Joergensen R."/>
+<person name="Andersen G.R."/>
+<person name="Beckmann R."/>
+<person name="Penczek P.A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Frank J."/>
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+<reference key="15">
+<citation type="journal article" date="2010" name="Proc. Natl. Acad. Sci. U.S.A." volume="107" first="19748" last="19753">
+<title>Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution.</title>
+<authorList>
+<person name="Armache J.P."/>
+<person name="Jarasch A."/>
+<person name="Anger A.M."/>
+<person name="Villa E."/>
+<person name="Becker T."/>
+<person name="Bhushan S."/>
+<person name="Jossinet F."/>
+<person name="Habeck M."/>
+<person name="Dindar G."/>
+<person name="Franckenberg S."/>
+<person name="Marquez V."/>
+<person name="Mielke T."/>
+<person name="Thomm M."/>
+<person name="Berninghausen O."/>
+<person name="Beatrix B."/>
+<person name="Soding J."/>
+<person name="Westhof E."/>
+<person name="Wilson D.N."/>
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+<citation type="journal article" date="2010" name="Science" volume="330" first="1203" last="1209">
+<title>Crystal structure of the eukaryotic ribosome.</title>
+<authorList>
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+<person name="Jenner L."/>
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+<person name="Yusupov M."/>
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+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
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+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
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+<person name="Yusupov M."/>
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+<text evidence="8">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
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+<text evidence="2 3 9">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). eL18 interacts with NAP1 (PubMed:18086883).</text>
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+<text evidence="7">There are 2 genes for eL18 in yeast.</text>
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+<text evidence="7">Belongs to the eukaryotic ribosomal protein eL18 family.</text>
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+<accession>Q08961</accession>
+<accession>D6W3G2</accession>
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+</recommendedName>
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+<name type="common">Baker's yeast</name>
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+<lineage>
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+<taxon>Ascomycota</taxon>
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+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
+<person name="Albermann K."/>
+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
+<person name="Brueckner M."/>
+<person name="Carpenter J."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Churcher C.M."/>
+<person name="Coster F."/>
+<person name="Davis K."/>
+<person name="Davis R.W."/>
+<person name="Dietrich F.S."/>
+<person name="Delius H."/>
+<person name="DiPaolo T."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Duncan M."/>
+<person name="Floeth M."/>
+<person name="Fortin N."/>
+<person name="Friesen J.D."/>
+<person name="Fritz C."/>
+<person name="Goffeau A."/>
+<person name="Hall J."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Hilbert H."/>
+<person name="Hillier L.W."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Johnston M."/>
+<person name="Kalman S."/>
+<person name="Kleine K."/>
+<person name="Komp C."/>
+<person name="Kurdi O."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin A."/>
+<person name="Lin D."/>
+<person name="Louis E.J."/>
+<person name="Marathe R."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
+<person name="Nentwich U."/>
+<person name="Oefner P."/>
+<person name="Pearson D."/>
+<person name="Petel F.X."/>
+<person name="Pohl T.M."/>
+<person name="Purnelle B."/>
+<person name="Rajandream M.A."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Roberts D."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
+<person name="Ushinsky S."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Voss H."/>
+<person name="Walsh S.V."/>
+<person name="Wambutt R."/>
+<person name="Wang Y."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Winnett E."/>
+<person name="Zhong W.-W."/>
+<person name="Zollner A."/>
+<person name="Vo D.H."/>
+<person name="Hani J."/>
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+<dbReference type="PubMed" id="9169875"/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="J. Biol. Chem." volume="280" first="34590" last="34598">
+<title>A novel SET domain methyltransferase modifies ribosomal protein Rpl23ab in yeast.</title>
+<authorList>
+<person name="Porras-Yakushi T.R."/>
+<person name="Whitelegge J.P."/>
+<person name="Miranda T.B."/>
+<person name="Clarke S."/>
+</authorList>
+<dbReference type="PubMed" id="16096273"/>
+<dbReference type="DOI" id="10.1074/jbc.m507672200"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>CATALYTIC ACTIVITY</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2007" name="J. Biol. Chem." volume="282" first="12368" last="12376">
+<title>Yeast ribosomal/cytochrome c SET domain methyltransferase subfamily: identification of Rpl23ab methylation sites and recognition motifs.</title>
+<authorList>
+<person name="Porras-Yakushi T.R."/>
+<person name="Whitelegge J.P."/>
+<person name="Clarke S."/>
+</authorList>
+<dbReference type="PubMed" id="17327221"/>
+<dbReference type="DOI" id="10.1074/jbc.m611896200"/>
+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="960" last="972">
+<title>Methylation of translation-associated proteins in Saccharomyces cerevisiae: Identification of methylated lysines and their methyltransferases.</title>
+<authorList>
+<person name="Couttas T.A."/>
+<person name="Raftery M.J."/>
+<person name="Padula M.P."/>
+<person name="Herbert B.R."/>
+<person name="Wilkins M.R."/>
+</authorList>
+<dbReference type="PubMed" id="22522802"/>
+<dbReference type="DOI" id="10.1002/pmic.201100570"/>
+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<comment type="function">
+<text evidence="5 6">S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates ribosomal protein S18 (RPS18A and RPS18B) at 'Lys-48' and dimethylates ribosomal protein L23 (RPL23A and RPL23B) at 'Lys-106' and 'Lys-110'.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="3">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="3">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 4800 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="2 8">Belongs to the class V-like SAM-binding methyltransferase superfamily. RKM1 family.</text>
+</comment>
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+<dbReference type="SGD" id="S000006129">
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+<dbReference type="eggNOG" id="KOG1337">
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+<dbReference type="GeneTree" id="ENSGT00940000153577"/>
+<dbReference type="HOGENOM" id="CLU_030667_2_0_1"/>
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+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
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+<property type="term" value="P:peptidyl-lysine monomethylation"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR017119">
+<property type="entry name" value="Efm1/Rkm1"/>
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+<dbReference type="InterPro" id="IPR001214">
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+<property type="entry name" value="Ribosomal_Lys-mtfrase-1"/>
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+<dbReference type="PROSITE" id="PS50280">
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+<property type="match status" value="1"/>
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+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0175">Coiled coil</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0489">Methyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<feature type="chain" description="Ribosomal lysine N-methyltransferase 1" id="PRO_0000228984">
+<location>
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+<end position="583"/>
+</location>
+</feature>
+<feature type="domain" description="SET" evidence="2">
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+</location>
+</feature>
+<feature type="coiled-coil region" evidence="1">
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+<feature type="coiled-coil region" evidence="1">
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+<feature type="binding site" description="S-adenosyl-L-methionine" evidence="2">
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+<entry dataset="Swiss-Prot" created="1992-05-01" modified="2021-04-07" version="198">
+<accession>P26321</accession>
+<accession>D6W3N6</accession>
+<name>RL5_YEAST</name>
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+</recommendedName>
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+<fullName>L1</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>L1a</fullName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="4">Large ribosomal subunit protein uL18</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Ribosomal 5S RNA-binding protein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>YL3</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="5">RPL5</name>
+<name type="synonym">RPL1</name>
+<name type="synonym">RPL1A</name>
+<name type="ordered locus">YPL131W</name>
+<name type="ORF">LPI14W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1991" name="J. Biol. Chem." volume="266" first="6120" last="6123">
+<title>Structure of the yeast ribosomal 5 S RNA-binding protein YL3.</title>
+<authorList>
+<person name="Tang B."/>
+<person name="Nazar R.N."/>
+</authorList>
+<dbReference type="PubMed" id="2007570"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1992" name="J. Biol. Chem." volume="267" first="17738" last="17742">
+<title>Unbalanced regulation of the ribosomal 5 S RNA-binding protein in Saccharomyces cerevisiae expressing mutant 5 S rRNAs.</title>
+<authorList>
+<person name="Tang B."/>
+<person name="Nazar R.N."/>
+</authorList>
+<dbReference type="PubMed" id="1325447"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1993" name="Mol. Cell. Biol." volume="13" first="2835" last="2845">
+<title>Yeast ribosomal protein L1 is required for the stability of newly synthesized 5S rRNA and the assembly of 60S ribosomal subunits.</title>
+<authorList>
+<person name="Deshmukh M.P."/>
+<person name="Tsay Y.F."/>
+<person name="Paulovich A.G."/>
+<person name="Woolford J.L. Jr."/>
+</authorList>
+<dbReference type="PubMed" id="8474444"/>
+<dbReference type="DOI" id="10.1128/mcb.13.5.2835"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
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+<dbReference type="PubMed" id="9169875"/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
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+<dbReference type="PubMed" id="24374639"/>
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+<scope>GENOME REANNOTATION</scope>
+<source>
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+<scope>SUBUNIT</scope>
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+</authorList>
+<dbReference type="PubMed" id="14562095"/>
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+<source>
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+<dbReference type="PubMed" id="17287358"/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<dbReference type="PubMed" id="22814378"/>
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+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-164</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="14">
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+</authorList>
+<dbReference type="PubMed" id="23118189"/>
+<dbReference type="DOI" id="10.1126/science.1226960"/>
+</citation>
+<scope>INTERACTION WITH RPL11A; RPL11B AND SYO1</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="15">
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+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
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+<scope>NOMENCLATURE</scope>
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+<dbReference type="DOI" id="10.1016/s0092-8674(01)00539-6"/>
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+<scope>ELECTRON MICROSCOPY</scope>
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+<dbReference type="PubMed" id="14976550"/>
+<dbReference type="DOI" id="10.1038/sj.emboj.7600102"/>
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+<scope>3D-STRUCTURE MODELING OF 11-232</scope>
+<scope>ELECTRON MICROSCOPY</scope>
+</reference>
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+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
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+</authorList>
+<dbReference type="PubMed" id="21109664"/>
+<dbReference type="DOI" id="10.1126/science.1194294"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME</scope>
+</reference>
+<reference key="19">
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+<person name="Ben-Shem A."/>
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+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
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+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<comment type="function">
+<text evidence="7">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="1 2 8">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). uL18 forms a heterotrimeric complex with SYO1 and uL5 (RPL11A/RPL11B). Interaction of this complex with KAP104 allows the nuclear import of the heterotrimer (PubMed:23118189).</text>
+</comment>
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+<id>P26321</id>
+</interactant>
+<interactant intactId="EBI-12105">
+<id>Q02892</id>
+<label>NOG1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="2">Nucleus</location>
+</subcellularLocation>
+<text evidence="2">The SYO1-uL5-uL18 complex is transported into the nucleus by KAP104.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the universal ribosomal protein uL18 family.</text>
+</comment>
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+<person name="Hesselberth J.R."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="17351133"/>
+<dbReference type="DOI" id="10.1101/gr.6049107"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [MRNA] OF 1-121</scope>
+<source>
+<strain>ATCC 201390 / BY4743</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
+</authorList>
+<dbReference type="PubMed" id="9559554"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19980330)14:5&lt;471::aid-yea241>3.0.co;2-u"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="17846" last="17851">
+<title>A large-scale full-length cDNA analysis to explore the budding yeast transcriptome.</title>
+<authorList>
+<person name="Miura F."/>
+<person name="Kawaguchi N."/>
+<person name="Sese J."/>
+<person name="Toyoda A."/>
+<person name="Hattori M."/>
+<person name="Morishita S."/>
+<person name="Ito T."/>
+</authorList>
+<dbReference type="PubMed" id="17101987"/>
+<dbReference type="DOI" id="10.1073/pnas.0605645103"/>
+</citation>
+<scope>IDENTIFICATION OF INTRON</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
+</authorList>
+<dbReference type="PubMed" id="17287358"/>
+<dbReference type="DOI" id="10.1073/pnas.0607084104"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
+</authorList>
+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-125; LYS-131 AND LYS-149</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
+<person name="Moore P.B."/>
+<person name="Noller H.F."/>
+<person name="Ortega J."/>
+<person name="Panse V.G."/>
+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<comment type="function">
+<text evidence="6">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="2 7">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eL20 forms multiple interactions with RNA and proteins in the central protuberance, connecting components of core functional centers that are locatzed far apart (PubMed:9559554, PubMed:22096102).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1 2">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="5">There are 2 genes for eL20 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="5">Belongs to the eukaryotic ribosomal protein eL20 family.</text>
+</comment>
+<comment type="sequence caution" evidence="5">
+<conflict type="erroneous gene model prediction">
+<sequence resource="EMBL-CDS" id="CAA62167" version="1"/>
+</conflict>
+</comment>
+<comment type="sequence caution" evidence="5">
+<conflict type="erroneous gene model prediction">
+<sequence resource="EMBL-CDS" id="CAA99632" version="1"/>
+</conflict>
+</comment>
+<dbReference type="EMBL" id="X90565">
+<property type="protein sequence ID" value="CAA62167.1"/>
+<property type="status" value="ALT_SEQ"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="protein sequence ID" value="CAA99632.1"/>
+<property type="status" value="ALT_SEQ"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="EF138822">
+<property type="protein sequence ID" value="ABL89190.1"/>
+<property type="molecule type" value="mRNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006948">
+<property type="protein sequence ID" value="DAA11077.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S56056">
+<property type="entry name" value="S56056"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013969.3">
+<property type="nucleotide sequence ID" value="NM_001182749.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_014957.2">
+<property type="nucleotide sequence ID" value="NM_001183732.1"/>
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+<dbReference type="PDB" id="4V8Y">
+<property type="method" value="EM"/>
+<property type="resolution" value="4.30"/>
+<property type="chains" value="BS=1-172"/>
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+<dbReference type="PDB" id="4V8Z">
+<property type="method" value="EM"/>
+<property type="resolution" value="6.60"/>
+<property type="chains" value="BS=1-172"/>
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+<dbReference type="PDBsum" id="4V8Y"/>
+<dbReference type="PDBsum" id="4V8Z"/>
+<dbReference type="SMR" id="P0CX24"/>
+<dbReference type="BioGRID" id="34700">
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+<dbReference type="BioGRID" id="35421">
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+</dbReference>
+<dbReference type="IntAct" id="P0CX24">
+<property type="interactions" value="1"/>
+</dbReference>
+<dbReference type="MINT" id="P0CX24"/>
+<dbReference type="iPTMnet" id="P0CX24"/>
+<dbReference type="PRIDE" id="P0CX24"/>
+<dbReference type="GeneID" id="854489"/>
+<dbReference type="GeneID" id="855283"/>
+<dbReference type="KEGG" id="sce:YMR242C"/>
+<dbReference type="KEGG" id="sce:YOR312C"/>
+<dbReference type="SGD" id="S000005839">
+<property type="gene designation" value="RPL20B"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_080773_1_1_1"/>
+<dbReference type="InParanoid" id="P0CX24"/>
+<dbReference type="OMA" id="RFWYFMK"/>
+<dbReference type="Reactome" id="R-SCE-156827">
+<property type="pathway name" value="L13a-mediated translational silencing of Ceruloplasmin expression"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-1799339">
+<property type="pathway name" value="SRP-dependent cotranslational protein targeting to membrane"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72689">
+<property type="pathway name" value="Formation of a pool of free 40S subunits"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72706">
+<property type="pathway name" value="GTP hydrolysis and joining of the 60S ribosomal subunit"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975956">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975957">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="PRO" id="PR:P0CX24"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XV"/>
+</dbReference>
+<dbReference type="RNAct" id="P0CX24">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
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+<dbReference type="GO" id="GO:0022625">
+<property type="term" value="C:cytosolic large ribosomal subunit"/>
+<property type="evidence" value="ECO:0000314"/>
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+<dbReference type="GO" id="GO:0003735">
+<property type="term" value="F:structural constituent of ribosome"/>
+<property type="evidence" value="ECO:0000305"/>
+<property type="project" value="SGD"/>
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+<dbReference type="GO" id="GO:0002181">
+<property type="term" value="P:cytoplasmic translation"/>
+<property type="evidence" value="ECO:0000305"/>
+<property type="project" value="SGD"/>
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+<property type="term" value="P:translational termination"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
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+<property type="entry name" value="Ribosomal_L18Ae"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR028877">
+<property type="entry name" value="50S_L18Ae/Ribosomal_L18a/L20"/>
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+<dbReference type="InterPro" id="IPR023573">
+<property type="entry name" value="Ribosomal_L18a//L18Ae/LX"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR021138">
+<property type="entry name" value="Ribosomal_L18a/L20_eukaryotes"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR10052">
+<property type="entry name" value="PTHR10052"/>
+<property type="match status" value="1"/>
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+<dbReference type="Pfam" id="PF01775">
+<property type="entry name" value="Ribosomal_L18A"/>
+<property type="match status" value="1"/>
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+<dbReference type="PIRSF" id="PIRSF002190">
+<property type="entry name" value="Ribosomal_L18a"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="chain" description="60S ribosomal protein L20-B" id="PRO_0000409758">
+<location>
+<begin position="1"/>
+<end position="172"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="8">
+<location>
+<position position="32"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="9">
+<location>
+<position position="125"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="9">
+<location>
+<position position="131"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="9">
+<location>
+<position position="149"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="24524803"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9559554"/>
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+</evidence>
+<evidence key="5" type="ECO:0000305"/>
+<evidence key="6" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="7" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="17287358"/>
+</source>
+</evidence>
+<evidence key="9" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22106047"/>
+</source>
+</evidence>
+<sequence length="172" mass="20437" checksum="28D470F11A48A43A" modified="2011-06-28" version="1">MAHFKEYQVIGRRLPTESVPEPKLFRMRIFASNEVIAKSRYWYFLQKLHKVKKASGEIVSINQINEAHPTKVKNFGVWVRYDSRSGTHNMYKEIRDVSRVAAVETLYQDMAARHRARFRSIHILKVAEIEKTADVKRQYVKQFLTKDLKFPLPHRVQKSTKTFSYKRPSTFY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2021-04-07" version="80">
+<accession>P0CX46</accession>
+<accession>D6VTR2</accession>
+<accession>P05736</accession>
+<name>RL2B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="7">60S ribosomal protein L2-B</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>L5</fullName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="6">Large ribosomal subunit protein uL2-B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>RP8</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>YL6</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="7">RPL2B</name>
+<name type="synonym">RPL5A</name>
+<name type="ordered locus">YIL018W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="Mol. Gen. Genet." volume="247" first="247" last="254">
+<title>Characterisation of Saccharomyces cerevisiae genes encoding ribosomal protein YL6.</title>
+<authorList>
+<person name="Moore J."/>
+<person name="Jacobs H.T."/>
+<person name="Kaiser K."/>
+</authorList>
+<dbReference type="PubMed" id="7753035"/>
+<dbReference type="DOI" id="10.1007/bf00705656"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [MRNA]</scope>
+<source>
+<strain>ATCC 204660 / DBY746</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="84" last="87">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.</title>
+<authorList>
+<person name="Churcher C.M."/>
+<person name="Bowman S."/>
+<person name="Badcock K."/>
+<person name="Bankier A.T."/>
+<person name="Brown D."/>
+<person name="Chillingworth T."/>
+<person name="Connor R."/>
+<person name="Devlin K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
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+<person name="Horsnell T."/>
+<person name="Hunt S."/>
+<person name="Jagels K."/>
+<person name="Jones M."/>
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+<person name="Moule S."/>
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+<person name="Pearson D."/>
+<person name="Rajandream M.A."/>
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+<person name="Rowley N."/>
+<person name="Skelton J."/>
+<person name="Smith V."/>
+<person name="Walsh S.V."/>
+<person name="Whitehead S."/>
+<person name="Barrell B.G."/>
+</authorList>
+<dbReference type="PubMed" id="9169870"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1984" name="Mol. Gen. Genet." volume="195" first="544" last="546">
+<title>Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence characterization of twenty-four proteins from cytoplasmic ribosomes.</title>
+<authorList>
+<person name="Otaka E."/>
+<person name="Higo K."/>
+<person name="Itoh T."/>
+</authorList>
+<dbReference type="PubMed" id="18782943"/>
+<dbReference type="DOI" id="10.1007/bf00341461"/>
+</citation>
+<scope>PARTIAL PROTEIN SEQUENCE OF 2-41</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1992" name="J. Biol. Chem." volume="267" first="5442" last="5445">
+<title>NH2-terminal acetylation of ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Takakura H."/>
+<person name="Tsunasawa S."/>
+<person name="Miyagi M."/>
+<person name="Warner J.R."/>
+</authorList>
+<dbReference type="PubMed" id="1544921"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 2-21</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
+</authorList>
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+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19980330)14:5&lt;471::aid-yea241>3.0.co;2-u"/>
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+<scope>NOMENCLATURE</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2002" name="Proc. Natl. Acad. Sci. U.S.A." volume="99" first="5942" last="5947">
+<title>Direct mass spectrometric analysis of intact proteins of the yeast large ribosomal subunit using capillary LC/FTICR.</title>
+<authorList>
+<person name="Lee S.-W."/>
+<person name="Berger S.J."/>
+<person name="Martinovic S."/>
+<person name="Pasa-Tolic L."/>
+<person name="Anderson G.A."/>
+<person name="Shen Y."/>
+<person name="Zhao R."/>
+<person name="Smith R.D."/>
+</authorList>
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+<dbReference type="DOI" id="10.1073/pnas.082119899"/>
+</citation>
+<scope>MASS SPECTROMETRY</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
+<person name="Chi A."/>
+<person name="Huttenhower C."/>
+<person name="Geer L.Y."/>
+<person name="Coon J.J."/>
+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
+<person name="Burke D.J."/>
+<person name="Troyanskaya O.G."/>
+<person name="Hunt D.F."/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52; SER-159; SER-160 AND SER-249</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-95</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-93; LYS-119 AND LYS-145</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
+<person name="Moore P.B."/>
+<person name="Noller H.F."/>
+<person name="Ortega J."/>
+<person name="Panse V.G."/>
+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
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+<scope>NOMENCLATURE</scope>
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+<text evidence="5 10">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<comment type="mass spectrometry" mass="27277.347" method="Electrospray" evidence="1">
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+<comment type="miscellaneous">
+<text evidence="8">There are 2 genes for uL2 in yeast.</text>
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+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
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+<keyword id="KW-0687">Ribonucleoprotein</keyword>
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+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0699">rRNA-binding</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
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+<feature type="modified residue" description="Phosphoserine" evidence="11">
+<location>
+<position position="249"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="46"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="93"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="119"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="145"/>
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+</entry>
+<entry dataset="Swiss-Prot" created="1997-11-01" modified="2021-04-07" version="162">
+<accession>Q12672</accession>
+<accession>D6W3T7</accession>
+<name>RL21B_YEAST</name>
+<protein>
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+<fullName evidence="5">60S ribosomal protein L21-B</fullName>
+</recommendedName>
+<alternativeName>
+<fullName evidence="4">Large ribosomal subunit protein eL21-B</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="5">RPL21B</name>
+<name type="ordered locus">YPL079W</name>
+<name type="ORF">LPF6W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
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+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
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+<person name="Carpenter J."/>
+<person name="Cherry J.M."/>
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+<person name="Dubois E."/>
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+<person name="Duncan M."/>
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+<person name="Fortin N."/>
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+<person name="Fritz C."/>
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+<person name="Louis E.J."/>
+<person name="Marathe R."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
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+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
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+<person name="Vissers S."/>
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+<person name="Vo D.H."/>
+<person name="Hani J."/>
+</authorList>
+<dbReference type="PubMed" id="9169875"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
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+<authorList>
+<person name="Engel S.R."/>
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+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
+</authorList>
+<dbReference type="PubMed" id="9559554"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19980330)14:5&lt;471::aid-yea241>3.0.co;2-u"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="6">
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+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-32</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
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+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<comment type="function">
+<text evidence="7">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 8">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1 3">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2 3">Present with 66400 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="6">There are 2 genes for eL21 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the eukaryotic ribosomal protein eL21 family.</text>
+</comment>
+<dbReference type="EMBL" id="U41849">
+<property type="protein sequence ID" value="AAB68259.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11353.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S61108">
+<property type="entry name" value="S61108"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_015246.1">
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+<dbReference type="IntAct" id="Q12672">
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+<dbReference type="iPTMnet" id="Q12672"/>
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+<dbReference type="EnsemblFungi" id="YPL079W_mRNA">
+<property type="protein sequence ID" value="YPL079W"/>
+<property type="gene ID" value="YPL079W"/>
+</dbReference>
+<dbReference type="GeneID" id="856026"/>
+<dbReference type="KEGG" id="sce:YPL079W"/>
+<dbReference type="SGD" id="S000006000">
+<property type="gene designation" value="RPL21B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YPL079W"/>
+<dbReference type="eggNOG" id="KOG1732">
+<property type="taxonomic scope" value="Eukaryota"/>
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+<dbReference type="HOGENOM" id="CLU_103610_0_1_1"/>
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+<dbReference type="OMA" id="HVQASRC"/>
+<dbReference type="PRO" id="PR:Q12672"/>
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+<dbReference type="RNAct" id="Q12672">
+<property type="molecule type" value="protein"/>
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+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000304"/>
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+<property type="evidence" value="ECO:0000318"/>
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+<property type="term" value="P:cytoplasmic translation"/>
+<property type="evidence" value="ECO:0000305"/>
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+<dbReference type="InterPro" id="IPR036948">
+<property type="entry name" value="Ribosomal_L21_sf"/>
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+<dbReference type="InterPro" id="IPR001147">
+<property type="entry name" value="Ribosomal_L21e"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR018259">
+<property type="entry name" value="Ribosomal_L21e_CS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR008991">
+<property type="entry name" value="Translation_prot_SH3-like_sf"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR20981">
+<property type="entry name" value="PTHR20981"/>
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+<dbReference type="Pfam" id="PF01157">
+<property type="entry name" value="Ribosomal_L21e"/>
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+<dbReference type="SUPFAM" id="SSF50104">
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+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="chain" description="60S ribosomal protein L21-B" id="PRO_0000149683">
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+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="9">
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+<evidence key="3" type="ECO:0000269">
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+</evidence>
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+</evidence>
+<evidence key="9" type="ECO:0007744">
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+</source>
+</evidence>
+<sequence length="160" mass="18274" checksum="733AF5208D555F7E" modified="1996-11-01" version="1">MGKSHGYRSRTRYMFQRDFRKHGAVHMSTYLKIYKVGDIVDIKANGSIQKGMPHKFYQGKTGVVYNVTKSSVGVIINKMVGNRYLEKRLNLRVEHIKHSKCRQEFLERVKANAAKRAEAKAQGVAVQLKRQPAQPRESRIVSTEGNVPQTLAPVPYETFI</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1995-02-01" modified="2021-04-07" version="165">
+<accession>P41056</accession>
+<accession>D6W2T8</accession>
+<name>RL33B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="7">60S ribosomal protein L33-B</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>L37</fullName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="6">Large ribosomal subunit protein eL33-B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>RP47</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>YL37</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="7">RPL33B</name>
+<name type="synonym">RPL37B</name>
+<name type="ordered locus">YOR234C</name>
+<name type="ORF">O5224</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1994" name="Curr. Genet." volume="25" first="480" last="487">
+<title>Saccharomyces cerevisiae ribosomal protein L37 is encoded by duplicate genes that are differentially expressed.</title>
+<authorList>
+<person name="Tornow J."/>
+<person name="Santangelo G.M."/>
+</authorList>
+<dbReference type="PubMed" id="8082197"/>
+<dbReference type="DOI" id="10.1007/bf00351666"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1996" name="Yeast" volume="12" first="1575" last="1586">
+<title>Sequence and analysis of a 26.9 kb fragment from chromosome XV of the yeast Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Boyer J."/>
+<person name="Michaux G."/>
+<person name="Fairhead C."/>
+<person name="Gaillon L."/>
+<person name="Dujon B."/>
+</authorList>
+<dbReference type="PubMed" id="8972580"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199612)12:15&lt;1575::aid-yea45>3.0.co;2-e"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 96604 / S288c / FY1679</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="98" last="102">
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+<authorList>
+<person name="Dujon B."/>
+<person name="Albermann K."/>
+<person name="Aldea M."/>
+<person name="Alexandraki D."/>
+<person name="Ansorge W."/>
+<person name="Arino J."/>
+<person name="Benes V."/>
+<person name="Bohn C."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Bordonne R."/>
+<person name="Boyer J."/>
+<person name="Camasses A."/>
+<person name="Casamayor A."/>
+<person name="Casas C."/>
+<person name="Cheret G."/>
+<person name="Cziepluch C."/>
+<person name="Daignan-Fornier B."/>
+<person name="Dang V.-D."/>
+<person name="de Haan M."/>
+<person name="Delius H."/>
+<person name="Durand P."/>
+<person name="Fairhead C."/>
+<person name="Feldmann H."/>
+<person name="Gaillon L."/>
+<person name="Galisson F."/>
+<person name="Gamo F.-J."/>
+<person name="Gancedo C."/>
+<person name="Goffeau A."/>
+<person name="Goulding S.E."/>
+<person name="Grivell L.A."/>
+<person name="Habbig B."/>
+<person name="Hand N.J."/>
+<person name="Hani J."/>
+<person name="Hattenhorst U."/>
+<person name="Hebling U."/>
+<person name="Hernando Y."/>
+<person name="Herrero E."/>
+<person name="Heumann K."/>
+<person name="Hiesel R."/>
+<person name="Hilger F."/>
+<person name="Hofmann B."/>
+<person name="Hollenberg C.P."/>
+<person name="Hughes B."/>
+<person name="Jauniaux J.-C."/>
+<person name="Kalogeropoulos A."/>
+<person name="Katsoulou C."/>
+<person name="Kordes E."/>
+<person name="Lafuente M.J."/>
+<person name="Landt O."/>
+<person name="Louis E.J."/>
+<person name="Maarse A.C."/>
+<person name="Madania A."/>
+<person name="Mannhaupt G."/>
+<person name="Marck C."/>
+<person name="Martin R.P."/>
+<person name="Mewes H.-W."/>
+<person name="Michaux G."/>
+<person name="Paces V."/>
+<person name="Parle-McDermott A.G."/>
+<person name="Pearson B.M."/>
+<person name="Perrin A."/>
+<person name="Pettersson B."/>
+<person name="Poch O."/>
+<person name="Pohl T.M."/>
+<person name="Poirey R."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rechmann S."/>
+<person name="Schwager C."/>
+<person name="Schweizer M."/>
+<person name="Sor F."/>
+<person name="Sterky F."/>
+<person name="Tarassov I.A."/>
+<person name="Teodoru C."/>
+<person name="Tettelin H."/>
+<person name="Thierry A."/>
+<person name="Tobiasch E."/>
+<person name="Tzermia M."/>
+<person name="Uhlen M."/>
+<person name="Unseld M."/>
+<person name="Valens M."/>
+<person name="Vandenbol M."/>
+<person name="Vetter I."/>
+<person name="Vlcek C."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler H."/>
+<person name="Wiemann S."/>
+<person name="Winsor B."/>
+<person name="Wolfe K.H."/>
+<person name="Zollner A."/>
+<person name="Zumstein E."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="9169874"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1984" name="Mol. Gen. Genet." volume="195" first="544" last="546">
+<title>Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence characterization of twenty-four proteins from cytoplasmic ribosomes.</title>
+<authorList>
+<person name="Otaka E."/>
+<person name="Higo K."/>
+<person name="Itoh T."/>
+</authorList>
+<dbReference type="PubMed" id="18782943"/>
+<dbReference type="DOI" id="10.1007/bf00341461"/>
+</citation>
+<scope>PARTIAL PROTEIN SEQUENCE OF 2-26</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
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+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
+</authorList>
+<dbReference type="PubMed" id="9559554"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19980330)14:5&lt;471::aid-yea241>3.0.co;2-u"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
+<person name="Moore P.B."/>
+<person name="Noller H.F."/>
+<person name="Ortega J."/>
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+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<comment type="function">
+<text evidence="9">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="5 10">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="2 5">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="PTM">
+<text evidence="1">N-terminally acetylated by acetyltransferase NatA.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 65600 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="8">There are 2 genes for eL33 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="8">Belongs to the eukaryotic ribosomal protein eL33 family.</text>
+</comment>
+<dbReference type="EMBL" id="L23923">
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+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="Z75142">
+<property type="protein sequence ID" value="CAA99454.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<dbReference type="EMBL" id="BK006948">
+<property type="protein sequence ID" value="DAA11004.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S44069">
+<property type="entry name" value="S44069"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_014877.3">
+<property type="nucleotide sequence ID" value="NM_001183653.3"/>
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+<dbReference type="SMR" id="P41056"/>
+<dbReference type="BioGRID" id="34627">
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+<dbReference type="MINT" id="P41056"/>
+<dbReference type="STRING" id="4932.YOR234C"/>
+<dbReference type="iPTMnet" id="P41056"/>
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+<dbReference type="EnsemblFungi" id="YOR234C_mRNA">
+<property type="protein sequence ID" value="YOR234C"/>
+<property type="gene ID" value="YOR234C"/>
+</dbReference>
+<dbReference type="GeneID" id="854409"/>
+<dbReference type="KEGG" id="sce:YOR234C"/>
+<dbReference type="SGD" id="S000005760">
+<property type="gene designation" value="RPL33B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YOR234C"/>
+<dbReference type="eggNOG" id="KOG0887">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00390000016972"/>
+<dbReference type="HOGENOM" id="CLU_100745_2_0_1"/>
+<dbReference type="InParanoid" id="P41056"/>
+<dbReference type="OMA" id="CAKPIRG"/>
+<dbReference type="PRO" id="PR:P41056"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XV"/>
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+<dbReference type="RNAct" id="P41056">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
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+<dbReference type="GO" id="GO:0022625">
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+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003735">
+<property type="term" value="F:structural constituent of ribosome"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
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+<dbReference type="GO" id="GO:0002181">
+<property type="term" value="P:cytoplasmic translation"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0042273">
+<property type="term" value="P:ribosomal large subunit biogenesis"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006415">
+<property type="term" value="P:translational termination"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="Gene3D" id="2.40.10.190">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="HAMAP" id="MF_00573">
+<property type="entry name" value="Ribosomal_L35Ae"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR038661">
+<property type="entry name" value="L35A_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001780">
+<property type="entry name" value="Ribosomal_L35A"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR018266">
+<property type="entry name" value="Ribosomal_L35Ae_CS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR009000">
+<property type="entry name" value="Transl_B-barrel_sf"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR10902">
+<property type="entry name" value="PTHR10902"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01247">
+<property type="entry name" value="Ribosomal_L35Ae"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF50447">
+<property type="entry name" value="SSF50447"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS01105">
+<property type="entry name" value="RIBOSOMAL_L35AE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="4">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="60S ribosomal protein L33-B" id="PRO_0000192808">
+<location>
+<begin position="2"/>
+<end position="107"/>
+</location>
+</feature>
+<feature type="modified residue" description="N-acetylalanine; partial" evidence="1">
+<location>
+<position position="2"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="1">
+<location>
+<position position="47"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 5; AA sequence." ref="5" evidence="8">
+<original>N</original>
+<variation>D</variation>
+<location>
+<position position="24"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="P05744"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="18782943"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="24524803"/>
+</source>
+</evidence>
+<evidence key="7" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0000305"/>
+<evidence key="9" type="ECO:0000305">
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+</source>
+</evidence>
+<evidence key="10" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<sequence length="107" mass="12168" checksum="D33E8388903B5196" modified="2007-01-23" version="2">MAESHRLYVKGKHLSYQRSKRVNNPNVSLIKIEGVATPQEAQFYLGKRIAYVYRASKEVRGSKIRVMWGKVTRTHGNSGVVRATFRNNLPAKTFGASVRIFLYPSNI</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2021-04-07" version="87">
+<accession>P0CX23</accession>
+<accession>A1YV95</accession>
+<accession>A1YV96</accession>
+<accession>D6W068</accession>
+<accession>P0C2I0</accession>
+<accession>P0C2I1</accession>
+<accession>P47913</accession>
+<name>RL20A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="5">60S ribosomal protein L20-A</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>L18a</fullName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="4">Large ribosomal subunit protein eL20-A</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="5">RPL20A</name>
+<name type="synonym">RPL18A</name>
+<name type="synonym">RPL18A2</name>
+<name type="ordered locus">YMR242C</name>
+<name type="ORF">YM9408.04C</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="90" last="93">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.</title>
+<authorList>
+<person name="Bowman S."/>
+<person name="Churcher C.M."/>
+<person name="Badcock K."/>
+<person name="Brown D."/>
+<person name="Chillingworth T."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Devlin K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jagels K."/>
+<person name="Lye G."/>
+<person name="Moule S."/>
+<person name="Odell C."/>
+<person name="Pearson D."/>
+<person name="Rajandream M.A."/>
+<person name="Rice P."/>
+<person name="Skelton J."/>
+<person name="Walsh S.V."/>
+<person name="Whitehead S."/>
+<person name="Barrell B.G."/>
+</authorList>
+<dbReference type="PubMed" id="9169872"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="503" last="509">
+<title>Genome-wide identification of spliced introns using a tiling microarray.</title>
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+<scope>NUCLEOTIDE SEQUENCE [MRNA] OF 1-105</scope>
+<source>
+<strain>ATCC 201390 / BY4743</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
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+<authorList>
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+<person name="Mager W.H."/>
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+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
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+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
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+<person name="O'Shea E.K."/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
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+<authorList>
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+</authorList>
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+<dbReference type="DOI" id="10.1038/nature02046"/>
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+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="17846" last="17851">
+<title>A large-scale full-length cDNA analysis to explore the budding yeast transcriptome.</title>
+<authorList>
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+<person name="Ito T."/>
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+<dbReference type="DOI" id="10.1073/pnas.0605645103"/>
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+<scope>IDENTIFICATION OF INTRON</scope>
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+<reference key="8">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
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+<authorList>
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+<person name="Burke D.J."/>
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+<person name="Hunt D.F."/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
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+<reference key="10">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
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+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
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+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
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+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-125; LYS-131 AND LYS-149</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
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+<authorList>
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+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
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+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
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+<person name="Lipton J.M."/>
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+<person name="Ortega J."/>
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+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
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+<reference key="12">
+<citation type="journal article" date="2010" name="Science" volume="330" first="1203" last="1209">
+<title>Crystal structure of the eukaryotic ribosome.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
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+<dbReference type="DOI" id="10.1126/science.1194294"/>
+</citation>
+<scope>X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 80S RIBOSOME</scope>
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+<reference key="13">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
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+<scope>X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 80S RIBOSOME</scope>
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+</reference>
+<comment type="function">
+<text evidence="7">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 8">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes). eL20 forms multiple interactions with RNA and proteins in the central protuberance, connecting components of core functional centers that are locatzed far apart (PubMed:9559554, PubMed:22096102).</text>
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+<location evidence="1 3">Cytoplasm</location>
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+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 54300 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="6">There are 2 genes for eL20 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the eukaryotic ribosomal protein eL20 family.</text>
+</comment>
+<comment type="sequence caution" evidence="6">
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+<text evidence="9">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
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+<title>Screening a yeast promoter library leads to the isolation of the RP29/L32 and SNR17B/RPL37A divergent promoters and the discovery of a gene encoding ribosomal protein L37.</title>
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+<citation type="journal article" date="1996" name="Yeast" volume="12" first="1483" last="1492">
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+<reference key="3">
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+<reference key="5">
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+<scope>PARTIAL PROTEIN SEQUENCE OF 2-26</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE</scope>
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+<authorList>
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+<person name="Lo R.S."/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<reference key="9">
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+<citation type="journal article" date="2010" name="Science" volume="330" first="1203" last="1209">
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+<authorList>
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+<comment type="function">
+<text evidence="7">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 8">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<text evidence="1">N-terminally acetylated by acetyltransferase NatA.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="6">There are 2 genes for eL33 in yeast.</text>
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+<text evidence="6">Belongs to the eukaryotic ribosomal protein eL33 family.</text>
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+<person name="Suzuki K."/>
+<person name="Mizuta K."/>
+<person name="Otaka E."/>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
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+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Scholler P."/>
+<person name="Schwager C."/>
+<person name="Schwarz S."/>
+<person name="Underwood A.P."/>
+<person name="Urrestarazu L.A."/>
+<person name="Vandenbol M."/>
+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
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+<person name="Hani J."/>
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+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
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+<citation type="journal article" date="1984" name="Mol. Gen. Genet." volume="195" first="544" last="546">
+<title>Yeast ribosomal proteins. VIII. Isolation of two proteins and sequence characterization of twenty-four proteins from cytoplasmic ribosomes.</title>
+<authorList>
+<person name="Otaka E."/>
+<person name="Higo K."/>
+<person name="Itoh T."/>
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+<dbReference type="DOI" id="10.1007/bf00341461"/>
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+<scope>PARTIAL PROTEIN SEQUENCE OF 2-25</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
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+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19980330)14:5&lt;471::aid-yea241>3.0.co;2-u"/>
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+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
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+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
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+<reference key="8">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
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+</reference>
+<reference key="9">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
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+<person name="Noller H.F."/>
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+<person name="Spahn C.M.T."/>
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+<person name="Yusupov M."/>
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+<text evidence="9">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
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+<comment type="subunit">
+<text evidence="5 10">Component of the large ribosomal subunit (LSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<text evidence="3">Present with 38400 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="8">There are 2 genes for eL6 in yeast.</text>
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+<title>Cloning and characterization of RAD17, a gene controlling cell cycle responses to DNA damage in Saccharomyces cerevisiae.</title>
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+<person name="Siede W."/>
+<person name="Nusspaumer G."/>
+<person name="Portillo V."/>
+<person name="Rodriguez R."/>
+<person name="Friedberg E.C."/>
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+<dbReference type="DOI" id="10.1093/nar/24.9.1669"/>
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+<citation type="submission" date="1993-08" db="EMBL/GenBank/DDBJ databases">
+<title>Yeast homologue of ribosomal protein S12.</title>
+<authorList>
+<person name="Teply R."/>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="98" last="102">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.</title>
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+<person name="Dujon B."/>
+<person name="Albermann K."/>
+<person name="Aldea M."/>
+<person name="Alexandraki D."/>
+<person name="Ansorge W."/>
+<person name="Arino J."/>
+<person name="Benes V."/>
+<person name="Bohn C."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Bordonne R."/>
+<person name="Boyer J."/>
+<person name="Camasses A."/>
+<person name="Casamayor A."/>
+<person name="Casas C."/>
+<person name="Cheret G."/>
+<person name="Cziepluch C."/>
+<person name="Daignan-Fornier B."/>
+<person name="Dang V.-D."/>
+<person name="de Haan M."/>
+<person name="Delius H."/>
+<person name="Durand P."/>
+<person name="Fairhead C."/>
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+<person name="Gaillon L."/>
+<person name="Galisson F."/>
+<person name="Gamo F.-J."/>
+<person name="Gancedo C."/>
+<person name="Goffeau A."/>
+<person name="Goulding S.E."/>
+<person name="Grivell L.A."/>
+<person name="Habbig B."/>
+<person name="Hand N.J."/>
+<person name="Hani J."/>
+<person name="Hattenhorst U."/>
+<person name="Hebling U."/>
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+<person name="Herrero E."/>
+<person name="Heumann K."/>
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+<person name="Hofmann B."/>
+<person name="Hollenberg C.P."/>
+<person name="Hughes B."/>
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+<person name="Mewes H.-W."/>
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+<person name="Parle-McDermott A.G."/>
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+<person name="Tettelin H."/>
+<person name="Thierry A."/>
+<person name="Tobiasch E."/>
+<person name="Tzermia M."/>
+<person name="Uhlen M."/>
+<person name="Unseld M."/>
+<person name="Valens M."/>
+<person name="Vandenbol M."/>
+<person name="Vetter I."/>
+<person name="Vlcek C."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler H."/>
+<person name="Wiemann S."/>
+<person name="Winsor B."/>
+<person name="Wolfe K.H."/>
+<person name="Zollner A."/>
+<person name="Zumstein E."/>
+<person name="Kleine K."/>
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+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
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+<person name="Hitz B.C."/>
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+<person name="Wong E.D."/>
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+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
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+<reference key="5">
+<citation type="submission" date="1995-04" db="EMBL/GenBank/DDBJ databases">
+<authorList>
+<person name="Moore J."/>
+<person name="Jacobs H.T."/>
+<person name="Kaiser K."/>
+</authorList>
+</citation>
+<scope>PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 29-126</scope>
+<source>
+<strain>ATCC 204660 / DBY746</strain>
+</source>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
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+<reference key="7">
+<citation type="journal article" date="2007" name="Proc. Natl. Acad. Sci. U.S.A." volume="104" first="2193" last="2198">
+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
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+<person name="Huttenhower C."/>
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+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
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+<person name="Bafna V."/>
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+<person name="Zhou H."/>
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+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
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+</reference>
+<reference key="9">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-85; LYS-95 AND LYS-114</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
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+<person name="Lindahl L."/>
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+<person name="Lipton J.M."/>
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+<person name="Yonath A."/>
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+<reference key="11">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
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+<person name="Yusupov M."/>
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+<dbReference type="DOI" id="10.1126/science.1212642"/>
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+<scope>X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME</scope>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
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+<text evidence="1 6">Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
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+<text evidence="7">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 8">Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1 3">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 30500 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="6">There are 2 genes for eS17 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="6">Belongs to the eukaryotic ribosomal protein eS17 family.</text>
+</comment>
+<dbReference type="EMBL" id="K02480">
+<property type="protein sequence ID" value="AAA34991.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
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+<property type="protein sequence ID" value="AAB64890.1"/>
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+<property type="protein sequence ID" value="DAA12282.1"/>
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+<property type="entry name" value="R4BY7B"/>
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+<property type="nucleotide sequence ID" value="NM_001180755.3"/>
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+<dbReference type="PDBsum" id="6TB3"/>
+<dbReference type="PDBsum" id="6TNU"/>
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+<dbReference type="PDBsum" id="6XIQ"/>
+<dbReference type="PDBsum" id="6XIR"/>
+<dbReference type="PDBsum" id="7A1G"/>
+<dbReference type="SMR" id="P14127"/>
+<dbReference type="BioGRID" id="32502">
+<property type="interactions" value="172"/>
+</dbReference>
+<dbReference type="IntAct" id="P14127">
+<property type="interactions" value="62"/>
+</dbReference>
+<dbReference type="MINT" id="P14127"/>
+<dbReference type="STRING" id="4932.YDR447C"/>
+<dbReference type="iPTMnet" id="P14127"/>
+<dbReference type="MaxQB" id="P14127"/>
+<dbReference type="PaxDb" id="P14127"/>
+<dbReference type="EnsemblFungi" id="YDR447C_mRNA">
+<property type="protein sequence ID" value="YDR447C"/>
+<property type="gene ID" value="YDR447C"/>
+</dbReference>
+<dbReference type="GeneID" id="852058"/>
+<dbReference type="KEGG" id="sce:YDR447C"/>
+<dbReference type="SGD" id="S000002855">
+<property type="gene designation" value="RPS17B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YDR447C"/>
+<dbReference type="eggNOG" id="KOG0187">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00390000006548"/>
+<dbReference type="HOGENOM" id="CLU_112958_0_1_1"/>
+<dbReference type="InParanoid" id="P14127"/>
+<dbReference type="OMA" id="EKYYTRM"/>
+<dbReference type="Reactome" id="R-SCE-156827">
+<property type="pathway name" value="L13a-mediated translational silencing of Ceruloplasmin expression"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-1799339">
+<property type="pathway name" value="SRP-dependent cotranslational protein targeting to membrane"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72689">
+<property type="pathway name" value="Formation of a pool of free 40S subunits"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72695">
+<property type="pathway name" value="Formation of the ternary complex, and subsequently, the 43S complex"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72702">
+<property type="pathway name" value="Ribosomal scanning and start codon recognition"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72706">
+<property type="pathway name" value="GTP hydrolysis and joining of the 60S ribosomal subunit"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975956">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975957">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="PRO" id="PR:P14127"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome IV"/>
+</dbReference>
+<dbReference type="RNAct" id="P14127">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="GO" id="GO:0022627">
+<property type="term" value="C:cytosolic small ribosomal subunit"/>
+<property type="evidence" value="ECO:0000303"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003735">
+<property type="term" value="F:structural constituent of ribosome"/>
+<property type="evidence" value="ECO:0000303"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0002181">
+<property type="term" value="P:cytoplasmic translation"/>
+<property type="evidence" value="ECO:0000303"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000028">
+<property type="term" value="P:ribosomal small subunit assembly"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006415">
+<property type="term" value="P:translational termination"/>
+<property type="evidence" value="ECO:0000304"/>
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+</dbReference>
+<dbReference type="Gene3D" id="1.10.60.20">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="HAMAP" id="MF_00511">
+<property type="entry name" value="Ribosomal_S17e"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001210">
+<property type="entry name" value="Ribosomal_S17e"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR018273">
+<property type="entry name" value="Ribosomal_S17e_CS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036401">
+<property type="entry name" value="RPS17e-like_sf"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR10732">
+<property type="entry name" value="PTHR10732"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00833">
+<property type="entry name" value="Ribosomal_S17e"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF116820">
+<property type="entry name" value="SSF116820"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00712">
+<property type="entry name" value="RIBOSOMAL_S17E"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<feature type="chain" description="40S ribosomal protein S17-B" id="PRO_0000141547">
+<location>
+<begin position="1"/>
+<end position="136"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="24524803"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000305"/>
+<evidence key="7" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<sequence length="136" mass="15803" checksum="83EE5382870EA289" modified="1990-01-01" version="1">MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKRIQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLSVINVSAQRDRRYRKRN</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1988-11-01" modified="2021-04-07" version="194">
+<accession>P05755</accession>
+<accession>D6VQI4</accession>
+<name>RS9B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName evidence="7">40S ribosomal protein S9-B</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>RP21</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>S13</fullName>
+</alternativeName>
+<alternativeName>
+<fullName evidence="6">Small ribosomal subunit protein uS4-B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>YP28</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>YS11</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary" evidence="7">RPS9B</name>
+<name type="synonym">RPS13B</name>
+<name type="synonym">SUP46</name>
+<name type="ordered locus">YBR189W</name>
+<name type="ORF">YBR1317</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1992" name="Genetics" volume="132" first="375" last="386">
+<title>The yeast omnipotent suppressor SUP46 encodes a ribosomal protein which is a functional and structural homolog of the Escherichia coli S4 ram protein.</title>
+<authorList>
+<person name="Vincent A."/>
+<person name="Liebman S.W."/>
+</authorList>
+<dbReference type="PubMed" id="1427034"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1994" name="Yeast" volume="10" first="1511" last="1525">
+<title>A 12.5 kb fragment of the yeast chromosome II contains two adjacent genes encoding ribosomal proteins and six putative new genes, one of which encodes a putative transcriptional factor.</title>
+<authorList>
+<person name="Demolis N."/>
+<person name="Jacquet M."/>
+<person name="Mallet L."/>
+</authorList>
+<dbReference type="PubMed" id="7871891"/>
+<dbReference type="DOI" id="10.1002/yea.320101116"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1994" name="EMBO J." volume="13" first="5795" last="5809">
+<title>Complete DNA sequence of yeast chromosome II.</title>
+<authorList>
+<person name="Feldmann H."/>
+<person name="Aigle M."/>
+<person name="Aljinovic G."/>
+<person name="Andre B."/>
+<person name="Baclet M.C."/>
+<person name="Barthe C."/>
+<person name="Baur A."/>
+<person name="Becam A.-M."/>
+<person name="Biteau N."/>
+<person name="Boles E."/>
+<person name="Brandt T."/>
+<person name="Brendel M."/>
+<person name="Brueckner M."/>
+<person name="Bussereau F."/>
+<person name="Christiansen C."/>
+<person name="Contreras R."/>
+<person name="Crouzet M."/>
+<person name="Cziepluch C."/>
+<person name="Demolis N."/>
+<person name="Delaveau T."/>
+<person name="Doignon F."/>
+<person name="Domdey H."/>
+<person name="Duesterhus S."/>
+<person name="Dubois E."/>
+<person name="Dujon B."/>
+<person name="El Bakkoury M."/>
+<person name="Entian K.-D."/>
+<person name="Feuermann M."/>
+<person name="Fiers W."/>
+<person name="Fobo G.M."/>
+<person name="Fritz C."/>
+<person name="Gassenhuber J."/>
+<person name="Glansdorff N."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="de Haan M."/>
+<person name="Hein C."/>
+<person name="Herbert C.J."/>
+<person name="Hollenberg C.P."/>
+<person name="Holmstroem K."/>
+<person name="Jacq C."/>
+<person name="Jacquet M."/>
+<person name="Jauniaux J.-C."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kallesoee T."/>
+<person name="Kiesau P."/>
+<person name="Kirchrath L."/>
+<person name="Koetter P."/>
+<person name="Korol S."/>
+<person name="Liebl S."/>
+<person name="Logghe M."/>
+<person name="Lohan A.J.E."/>
+<person name="Louis E.J."/>
+<person name="Li Z.Y."/>
+<person name="Maat M.J."/>
+<person name="Mallet L."/>
+<person name="Mannhaupt G."/>
+<person name="Messenguy F."/>
+<person name="Miosga T."/>
+<person name="Molemans F."/>
+<person name="Mueller S."/>
+<person name="Nasr F."/>
+<person name="Obermaier B."/>
+<person name="Perea J."/>
+<person name="Pierard A."/>
+<person name="Piravandi E."/>
+<person name="Pohl F.M."/>
+<person name="Pohl T.M."/>
+<person name="Potier S."/>
+<person name="Proft M."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rieger M."/>
+<person name="Rose M."/>
+<person name="Schaaff-Gerstenschlaeger I."/>
+<person name="Scherens B."/>
+<person name="Schwarzlose C."/>
+<person name="Skala J."/>
+<person name="Slonimski P.P."/>
+<person name="Smits P.H.M."/>
+<person name="Souciet J.-L."/>
+<person name="Steensma H.Y."/>
+<person name="Stucka R."/>
+<person name="Urrestarazu L.A."/>
+<person name="van der Aart Q.J.M."/>
+<person name="Van Dyck L."/>
+<person name="Vassarotti A."/>
+<person name="Vetter I."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Wagner G."/>
+<person name="de Wergifosse P."/>
+<person name="Wolfe K.H."/>
+<person name="Zagulski M."/>
+<person name="Zimmermann F.K."/>
+<person name="Mewes H.-W."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="7813418"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1994.tb06923.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="journal article" date="1982" name="Biochemistry" volume="21" first="4545" last="4550">
+<title>Isolation of seventeen proteins and amino-terminal amino acid sequences of eight proteins from cytoplasmic ribosomes of yeast.</title>
+<authorList>
+<person name="Otaka E."/>
+<person name="Higo K."/>
+<person name="Osawa S."/>
+</authorList>
+<dbReference type="PubMed" id="6814480"/>
+<dbReference type="DOI" id="10.1021/bi00262a005"/>
+</citation>
+<scope>PROTEIN SEQUENCE OF 2-24</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1998" name="Yeast" volume="14" first="471" last="477">
+<title>The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Planta R.J."/>
+<person name="Mager W.H."/>
+</authorList>
+<dbReference type="PubMed" id="9559554"/>
+<dbReference type="DOI" id="10.1002/(sici)1097-0061(19980330)14:5&lt;471::aid-yea241>3.0.co;2-u"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+<scope>SUBUNIT</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2004" name="Eukaryot. Cell" volume="3" first="1619" last="1626">
+<title>The small-subunit processome is a ribosome assembly intermediate.</title>
+<authorList>
+<person name="Bernstein K.A."/>
+<person name="Gallagher J.E.G."/>
+<person name="Mitchell B.M."/>
+<person name="Granneman S."/>
+<person name="Baserga S.J."/>
+</authorList>
+<dbReference type="PubMed" id="15590835"/>
+<dbReference type="DOI" id="10.1128/ec.3.6.1619-1626.2004"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH MPP10 AND SNORNA U3</scope>
+<scope>IDENTIFICATION IN SSU PROCESSOME</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
+<person name="Haas W."/>
+<person name="Villen J."/>
+<person name="Elias J.E."/>
+<person name="Gygi S.P."/>
+</authorList>
+<dbReference type="PubMed" id="17330950"/>
+<dbReference type="DOI" id="10.1021/pr060559j"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ADR376</strain>
+</source>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2011" name="Science" volume="334" first="1524" last="1529">
+<title>The structure of the eukaryotic ribosome at 3.0 A resolution.</title>
+<authorList>
+<person name="Ben-Shem A."/>
+<person name="Garreau de Loubresse N."/>
+<person name="Melnikov S."/>
+<person name="Jenner L."/>
+<person name="Yusupova G."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="22096102"/>
+<dbReference type="DOI" id="10.1126/science.1212642"/>
+</citation>
+<scope>SUBUNIT</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-180</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="15">
+<citation type="journal article" date="2014" name="Curr. Opin. Struct. Biol." volume="24" first="165" last="169">
+<title>A new system for naming ribosomal proteins.</title>
+<authorList>
+<person name="Ban N."/>
+<person name="Beckmann R."/>
+<person name="Cate J.H.D."/>
+<person name="Dinman J.D."/>
+<person name="Dragon F."/>
+<person name="Ellis S.R."/>
+<person name="Lafontaine D.L.J."/>
+<person name="Lindahl L."/>
+<person name="Liljas A."/>
+<person name="Lipton J.M."/>
+<person name="McAlear M.A."/>
+<person name="Moore P.B."/>
+<person name="Noller H.F."/>
+<person name="Ortega J."/>
+<person name="Panse V.G."/>
+<person name="Ramakrishnan V."/>
+<person name="Spahn C.M.T."/>
+<person name="Steitz T.A."/>
+<person name="Tchorzewski M."/>
+<person name="Tollervey D."/>
+<person name="Warren A.J."/>
+<person name="Williamson J.R."/>
+<person name="Wilson D."/>
+<person name="Yonath A."/>
+<person name="Yusupov M."/>
+</authorList>
+<dbReference type="PubMed" id="24524803"/>
+<dbReference type="DOI" id="10.1016/j.sbi.2014.01.002"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<comment type="function">
+<text evidence="3 9">Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (PubMed:22096102). uS4 is involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly (PubMed:15590835).</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 4 10">Component of the small ribosomal subunit (SSU). Mature yeast ribosomes consist of a small (40S) and a large (60S) subunit. The 40S small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33 different proteins (encoded by 57 genes). The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102). Interacts with snoRNA U3. uS11 interacts with MPP10. Component of the ribosomal small subunit (SSU) processome composed of at least 40 protein subunits and snoRNA U3 (PubMed:15590835).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="4">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="3">Nucleus</location>
+<location evidence="3">Nucleolus</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 63300 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="8">There are 2 genes for uS4 in yeast.</text>
+</comment>
+<comment type="similarity">
+<text evidence="8">Belongs to the universal ribosomal protein uS4 family.</text>
+</comment>
+<dbReference type="EMBL" id="M88650">
+<property type="protein sequence ID" value="AAB59327.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="U02073">
+<property type="protein sequence ID" value="AAB60283.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z36058">
+<property type="protein sequence ID" value="CAA85151.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006936">
+<property type="protein sequence ID" value="DAA07304.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S31287">
+<property type="entry name" value="S31287"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_009748.3">
+<property type="nucleotide sequence ID" value="NM_001178537.3"/>
+</dbReference>
+<dbReference type="PDB" id="6WOO">
+<property type="method" value="EM"/>
+<property type="resolution" value="2.90"/>
+<property type="chains" value="JJ=2-183"/>
+</dbReference>
+<dbReference type="PDBsum" id="6WOO"/>
+<dbReference type="SMR" id="P05755"/>
+<dbReference type="BioGRID" id="32887">
+<property type="interactions" value="130"/>
+</dbReference>
+<dbReference type="IntAct" id="P05755">
+<property type="interactions" value="31"/>
+</dbReference>
+<dbReference type="MINT" id="P05755"/>
+<dbReference type="STRING" id="4932.YBR189W"/>
+<dbReference type="iPTMnet" id="P05755"/>
+<dbReference type="MaxQB" id="P05755"/>
+<dbReference type="PaxDb" id="P05755"/>
+<dbReference type="PRIDE" id="P05755"/>
+<dbReference type="TopDownProteomics" id="P05755"/>
+<dbReference type="EnsemblFungi" id="YBR189W_mRNA">
+<property type="protein sequence ID" value="YBR189W"/>
+<property type="gene ID" value="YBR189W"/>
+</dbReference>
+<dbReference type="GeneID" id="852487"/>
+<dbReference type="KEGG" id="sce:YBR189W"/>
+<dbReference type="SGD" id="S000000393">
+<property type="gene designation" value="RPS9B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YBR189W"/>
+<dbReference type="eggNOG" id="KOG3301">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00550000074829"/>
+<dbReference type="HOGENOM" id="CLU_089738_0_0_1"/>
+<dbReference type="InParanoid" id="P05755"/>
+<dbReference type="OMA" id="THGHIAI"/>
+<dbReference type="Reactome" id="R-SCE-156827">
+<property type="pathway name" value="L13a-mediated translational silencing of Ceruloplasmin expression"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-1799339">
+<property type="pathway name" value="SRP-dependent cotranslational protein targeting to membrane"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-6791226">
+<property type="pathway name" value="Major pathway of rRNA processing in the nucleolus and cytosol"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72689">
+<property type="pathway name" value="Formation of a pool of free 40S subunits"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72695">
+<property type="pathway name" value="Formation of the ternary complex, and subsequently, the 43S complex"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72702">
+<property type="pathway name" value="Ribosomal scanning and start codon recognition"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-72706">
+<property type="pathway name" value="GTP hydrolysis and joining of the 60S ribosomal subunit"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975956">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-975957">
+<property type="pathway name" value="Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC)"/>
+</dbReference>
+<dbReference type="PRO" id="PR:P05755"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome II"/>
+</dbReference>
+<dbReference type="RNAct" id="P05755">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0030686">
+<property type="term" value="C:90S preribosome"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005829">
+<property type="term" value="C:cytosol"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="GO" id="GO:0022627">
+<property type="term" value="C:cytosolic small ribosomal subunit"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005730">
+<property type="term" value="C:nucleolus"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015935">
+<property type="term" value="C:small ribosomal subunit"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032040">
+<property type="term" value="C:small-subunit processome"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0019843">
+<property type="term" value="F:rRNA binding"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003735">
+<property type="term" value="F:structural constituent of ribosome"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000462">
+<property type="term" value="P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA)"/>
+<property type="evidence" value="ECO:0000316"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0045903">
+<property type="term" value="P:positive regulation of translational fidelity"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006415">
+<property type="term" value="P:translational termination"/>
+<property type="evidence" value="ECO:0000304"/>
+<property type="project" value="Reactome"/>
+</dbReference>
+<dbReference type="CDD" id="cd00165">
+<property type="entry name" value="S4"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.10.290.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR022801">
+<property type="entry name" value="Ribosomal_S4/S9"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR005710">
+<property type="entry name" value="Ribosomal_S4/S9_euk/arc"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001912">
+<property type="entry name" value="Ribosomal_S4/S9_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR018079">
+<property type="entry name" value="Ribosomal_S4_CS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR002942">
+<property type="entry name" value="S4_RNA-bd"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036986">
+<property type="entry name" value="S4_RNA-bd_sf"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR11831">
+<property type="entry name" value="PTHR11831"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01479">
+<property type="entry name" value="S4"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM01390">
+<property type="entry name" value="Ribosomal_S4"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM00363">
+<property type="entry name" value="S4"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="TIGRFAMs" id="TIGR01018">
+<property type="entry name" value="uS4_arch"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00632">
+<property type="entry name" value="RIBOSOMAL_S4"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50889">
+<property type="entry name" value="S4"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0687">Ribonucleoprotein</keyword>
+<keyword id="KW-0689">Ribosomal protein</keyword>
+<keyword id="KW-0690">Ribosome biogenesis</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0698">rRNA processing</keyword>
+<keyword id="KW-0699">rRNA-binding</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="5">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="40S ribosomal protein S9-B" id="PRO_0000132704">
+<location>
+<begin position="2"/>
+<end position="195"/>
+</location>
+</feature>
+<feature type="domain" description="S4 RNA-binding" evidence="1">
+<location>
+<begin position="107"/>
+<end position="181"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="11 12 13">
+<location>
+<position position="184"/>
+</location>
+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="14">
+<location>
+<position position="180"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 5; AA sequence." ref="5" evidence="8">
+<original>ESS</original>
+<variation>QSB</variation>
+<location>
+<begin position="20"/>
+<end position="22"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00182"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="15590835"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="6814480"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="24524803"/>
+</source>
+</evidence>
+<evidence key="7" type="ECO:0000303">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="8" type="ECO:0000305"/>
+<evidence key="9" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="22096102"/>
+</source>
+</evidence>
+<evidence key="10" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9559554"/>
+</source>
+</evidence>
+<evidence key="11" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="17330950"/>
+</source>
+</evidence>
+<evidence key="12" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="18407956"/>
+</source>
+</evidence>
+<evidence key="13" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="19779198"/>
+</source>
+</evidence>
+<evidence key="14" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="22106047"/>
+</source>
+</evidence>
+<sequence length="195" mass="22299" checksum="F5BDCEA167003813" modified="2007-01-23" version="4">MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKREIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAAEEAEDEE</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1995-02-01" modified="2021-04-07" version="183">
+<accession>P40075</accession>
+<accession>D3DM26</accession>
+<name>SCS2_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Vesicle-associated membrane protein-associated protein SCS2</fullName>
+<shortName>VAMP-associated protein SCS2</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Choline sensitivity suppressor protein 2</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>VAP homolog 1</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">SCS2</name>
+<name type="ordered locus">YER120W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="J. Biochem." volume="118" first="39" last="45">
+<title>Cloning and sequence of the SCS2 gene, which can suppress the defect of INO1 expression in an inositol auxotrophic mutant of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Nikawa J."/>
+<person name="Murakami A."/>
+<person name="Esumi E."/>
+<person name="Hosaka K."/>
+</authorList>
+<dbReference type="PubMed" id="8537323"/>
+<dbReference type="DOI" id="10.1093/oxfordjournals.jbchem.a124889"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="78" last="81">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome V.</title>
+<authorList>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Hennessy K.M."/>
+<person name="Yelton M.A."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Brennan T."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Guzman E."/>
+<person name="Hartzell G."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Kayser A."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin D."/>
+<person name="Mosedale D."/>
+<person name="Nakahara K."/>
+<person name="Namath A."/>
+<person name="Norgren R."/>
+<person name="Oefner P."/>
+<person name="Oh C."/>
+<person name="Petel F.X."/>
+<person name="Roberts D."/>
+<person name="Sehl P."/>
+<person name="Schramm S."/>
+<person name="Shogren T."/>
+<person name="Smith V."/>
+<person name="Taylor P."/>
+<person name="Wei Y."/>
+<person name="Botstein D."/>
+<person name="Davis R.W."/>
+</authorList>
+<dbReference type="PubMed" id="9169868"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
+<person name="Rolfs A."/>
+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
+<person name="Zhu C."/>
+<person name="Berger M.F."/>
+<person name="Camargo A.A."/>
+<person name="Kelley F."/>
+<person name="McCarron S."/>
+<person name="Jepson D."/>
+<person name="Richardson A."/>
+<person name="Raphael J."/>
+<person name="Moreira D."/>
+<person name="Taycher E."/>
+<person name="Zuo D."/>
+<person name="Mohr S."/>
+<person name="Kane M.F."/>
+<person name="Williamson J."/>
+<person name="Simpson A.J.G."/>
+<person name="Bulyk M.L."/>
+<person name="Harlow E."/>
+<person name="Marsischky G."/>
+<person name="Kolodner R.D."/>
+<person name="LaBaer J."/>
+</authorList>
+<dbReference type="PubMed" id="17322287"/>
+<dbReference type="DOI" id="10.1101/gr.6037607"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="5">
+<citation type="submission" date="2005-06" db="UniProtKB">
+<authorList>
+<person name="Bienvenut W.V."/>
+<person name="Peters C."/>
+</authorList>
+</citation>
+<scope>PROTEIN SEQUENCE OF 2-14; 85-113; 144-156 AND 166-180</scope>
+<scope>CLEAVAGE OF INITIATOR METHIONINE</scope>
+<scope>ACETYLATION AT SER-2</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="1998" name="J. Bacteriol." volume="180" first="1700" last="1708">
+<title>The Saccharomyces cerevisiae SCS2 gene product, a homolog of a synaptobrevin-associated protein, is an integral membrane protein of the endoplasmic reticulum and is required for inositol metabolism.</title>
+<authorList>
+<person name="Kagiwada S."/>
+<person name="Hosaka K."/>
+<person name="Murata M."/>
+<person name="Nikawa J."/>
+<person name="Takatsuki A."/>
+</authorList>
+<dbReference type="PubMed" id="9537365"/>
+<dbReference type="DOI" id="10.1128/jb.180.7.1700-1708.1998"/>
+</citation>
+<scope>TOPOLOGY</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="EMBO J." volume="22" first="2025" last="2035">
+<title>A conserved ER targeting motif in three families of lipid binding proteins and in Opi1p binds VAP.</title>
+<authorList>
+<person name="Loewen C.J.R."/>
+<person name="Roy A."/>
+<person name="Levine T.P."/>
+</authorList>
+<dbReference type="PubMed" id="12727870"/>
+<dbReference type="DOI" id="10.1093/emboj/cdg201"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>INTERACTION WITH OPI1</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2004" name="PLoS Biol." volume="2" first="1843" last="1852">
+<title>Gene recruitment of the activated INO1 locus to the nuclear membrane.</title>
+<authorList>
+<person name="Brickner J.H."/>
+<person name="Walter P."/>
+</authorList>
+<dbReference type="PubMed" id="15455074"/>
+<dbReference type="DOI" id="10.1371/journal.pbio.0020342"/>
+</citation>
+<scope>INTERACTION WITH OPI1</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2005" name="J. Biol. Chem." volume="280" first="14097" last="14104">
+<title>A highly conserved binding site in vesicle-associated membrane protein-associated protein (VAP) for the FFAT motif of lipid-binding proteins.</title>
+<authorList>
+<person name="Loewen C.J.R."/>
+<person name="Levine T.P."/>
+</authorList>
+<dbReference type="PubMed" id="15668246"/>
+<dbReference type="DOI" id="10.1074/jbc.m500147200"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>MUTAGENESIS OF LYS-40; 41-THR-THR-42 AND LYS-120</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2005" name="Mol. Cell. Proteomics" volume="4" first="310" last="327">
+<title>Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway.</title>
+<authorList>
+<person name="Gruhler A."/>
+<person name="Olsen J.V."/>
+<person name="Mohammed S."/>
+<person name="Mortensen P."/>
+<person name="Faergeman N.J."/>
+<person name="Mann M."/>
+<person name="Jensen O.N."/>
+</authorList>
+<dbReference type="PubMed" id="15665377"/>
+<dbReference type="DOI" id="10.1074/mcp.m400219-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>YAL6B</strain>
+</source>
+</reference>
+<reference key="13">
+<citation type="journal article" date="2005" name="Structure" volume="13" first="1035" last="1045">
+<title>Structural basis of FFAT motif-mediated ER targeting.</title>
+<authorList>
+<person name="Kaiser S.E."/>
+<person name="Brickner J.H."/>
+<person name="Reilein A.R."/>
+<person name="Fenn T.D."/>
+<person name="Walter P."/>
+<person name="Brunger A.T."/>
+</authorList>
+<dbReference type="PubMed" id="16004875"/>
+<dbReference type="DOI" id="10.1016/j.str.2005.04.010"/>
+</citation>
+<scope>FFAT MOTIF-BINDING</scope>
+<scope>MUTAGENESIS OF LYS-84 AND LEU-86</scope>
+</reference>
+<reference key="14">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="3 6">Targets proteins containing a FFAT motif to endoplasmic reticulum membranes. Regulates phospholipid biosynthesis by modulating the subcellular localization of the transcriptional repressor OPI1.</text>
+</comment>
+<comment type="subunit">
+<text evidence="3 5">Interacts with OPI1.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-16735">
+<id>P40075</id>
+</interactant>
+<interactant intactId="EBI-12386">
+<id>Q00402</id>
+<label>NUM1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>4</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-16735">
+<id>P40075</id>
+</interactant>
+<interactant intactId="EBI-12555">
+<id>P21957</id>
+<label>OPI1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-16735">
+<id>P40075</id>
+</interactant>
+<interactant intactId="EBI-12630">
+<id>P38713</id>
+<label>OSH3</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-16735">
+<id>P40075</id>
+</interactant>
+<interactant intactId="EBI-22083">
+<id>Q07657</id>
+<label>SHS1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>4</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-16735">
+<id>P40075</id>
+</interactant>
+<interactant intactId="EBI-27256">
+<id>P39523</id>
+<label>YMR124W</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>4</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Endoplasmic reticulum membrane</location>
+<topology>Single-pass type IV membrane protein</topology>
+</subcellularLocation>
+<subcellularLocation>
+<location>Nucleus membrane</location>
+<topology>Single-pass type IV membrane protein</topology>
+</subcellularLocation>
+</comment>
+<comment type="domain">
+<text>The MSP domain is required for binding to the FFAT motif of target proteins.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="4">Present with 3497 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="9">Belongs to the VAMP-associated protein (VAP) (TC 9.B.17) family.</text>
+</comment>
+<dbReference type="EMBL" id="D44493">
+<property type="protein sequence ID" value="BAA07936.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="U18916">
+<property type="protein sequence ID" value="AAC03218.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY693125">
+<property type="protein sequence ID" value="AAT93144.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006939">
+<property type="protein sequence ID" value="DAA07780.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S50623">
+<property type="entry name" value="S50623"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_011046.3">
+<property type="nucleotide sequence ID" value="NM_001179010.3"/>
+</dbReference>
+<dbReference type="PDB" id="6LP4">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.05"/>
+<property type="chains" value="A=1-128"/>
+</dbReference>
+<dbReference type="PDBsum" id="6LP4"/>
+<dbReference type="SMR" id="P40075"/>
+<dbReference type="BioGRID" id="36865">
+<property type="interactions" value="349"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-2272N"/>
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+<dbReference type="MINT" id="P40075"/>
+<dbReference type="STRING" id="4932.YER120W"/>
+<dbReference type="iPTMnet" id="P40075"/>
+<dbReference type="MaxQB" id="P40075"/>
+<dbReference type="PaxDb" id="P40075"/>
+<dbReference type="PRIDE" id="P40075"/>
+<dbReference type="EnsemblFungi" id="YER120W_mRNA">
+<property type="protein sequence ID" value="YER120W"/>
+<property type="gene ID" value="YER120W"/>
+</dbReference>
+<dbReference type="GeneID" id="856856"/>
+<dbReference type="KEGG" id="sce:YER120W"/>
+<dbReference type="SGD" id="S000000922">
+<property type="gene designation" value="SCS2"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YER120W"/>
+<dbReference type="eggNOG" id="KOG0439">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00940000172509"/>
+<dbReference type="HOGENOM" id="CLU_072622_1_0_1"/>
+<dbReference type="InParanoid" id="P40075"/>
+<dbReference type="OMA" id="HEAIHEN"/>
+<dbReference type="Reactome" id="R-SCE-6798695">
+<property type="pathway name" value="Neutrophil degranulation"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-9609523">
+<property type="pathway name" value="Insertion of tail-anchored proteins into the endoplasmic reticulum membrane"/>
+</dbReference>
+<dbReference type="PRO" id="PR:P40075"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome V"/>
+</dbReference>
+<dbReference type="RNAct" id="P40075">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005935">
+<property type="term" value="C:cellular bud neck"/>
+<property type="evidence" value="ECO:0000353"/>
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+</dbReference>
+<dbReference type="GO" id="GO:0005934">
+<property type="term" value="C:cellular bud tip"/>
+<property type="evidence" value="ECO:0000314"/>
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+</dbReference>
+<dbReference type="GO" id="GO:0000781">
+<property type="term" value="C:chromosome, telomeric region"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="GOC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005783">
+<property type="term" value="C:endoplasmic reticulum"/>
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+</dbReference>
+<dbReference type="GO" id="GO:0005789">
+<property type="term" value="C:endoplasmic reticulum membrane"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0030176">
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+<dbReference type="GO" id="GO:0005635">
+<property type="term" value="C:nuclear envelope"/>
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+<dbReference type="GO" id="GO:0031965">
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+<dbReference type="GO" id="GO:0071561">
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+<dbReference type="GO" id="GO:0005886">
+<property type="term" value="C:plasma membrane"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0033149">
+<property type="term" value="F:FFAT motif binding"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0035091">
+<property type="term" value="F:phosphatidylinositol binding"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006348">
+<property type="term" value="P:chromatin silencing at telomere"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0048309">
+<property type="term" value="P:endoplasmic reticulum inheritance"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0090158">
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0061163">
+<property type="term" value="P:endoplasmic reticulum polarization"/>
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+<title>The sequence of a 30 kb fragment on the left arm of chromosome XV from Saccharomyces cerevisiae reveals 15 open reading frames, five of which correspond to previously identified genes.</title>
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+<person name="Sterky F."/>
+<person name="Holmberg A."/>
+<person name="Pettersson B."/>
+<person name="Uhlen M."/>
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+<dbReference type="DOI" id="10.1002/(sici)1097-0061(199609)12:10b&lt;1091::aid-yea22>3.0.co;2-i"/>
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+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
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+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
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+<scope>GENOME REANNOTATION</scope>
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+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="98" last="102">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.</title>
+<authorList>
+<person name="Dujon B."/>
+<person name="Albermann K."/>
+<person name="Aldea M."/>
+<person name="Alexandraki D."/>
+<person name="Ansorge W."/>
+<person name="Arino J."/>
+<person name="Benes V."/>
+<person name="Bohn C."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Bordonne R."/>
+<person name="Boyer J."/>
+<person name="Camasses A."/>
+<person name="Casamayor A."/>
+<person name="Casas C."/>
+<person name="Cheret G."/>
+<person name="Cziepluch C."/>
+<person name="Daignan-Fornier B."/>
+<person name="Dang V.-D."/>
+<person name="de Haan M."/>
+<person name="Delius H."/>
+<person name="Durand P."/>
+<person name="Fairhead C."/>
+<person name="Feldmann H."/>
+<person name="Gaillon L."/>
+<person name="Galisson F."/>
+<person name="Gamo F.-J."/>
+<person name="Gancedo C."/>
+<person name="Goffeau A."/>
+<person name="Goulding S.E."/>
+<person name="Grivell L.A."/>
+<person name="Habbig B."/>
+<person name="Hand N.J."/>
+<person name="Hani J."/>
+<person name="Hattenhorst U."/>
+<person name="Hebling U."/>
+<person name="Hernando Y."/>
+<person name="Herrero E."/>
+<person name="Heumann K."/>
+<person name="Hiesel R."/>
+<person name="Hilger F."/>
+<person name="Hofmann B."/>
+<person name="Hollenberg C.P."/>
+<person name="Hughes B."/>
+<person name="Jauniaux J.-C."/>
+<person name="Kalogeropoulos A."/>
+<person name="Katsoulou C."/>
+<person name="Kordes E."/>
+<person name="Lafuente M.J."/>
+<person name="Landt O."/>
+<person name="Louis E.J."/>
+<person name="Maarse A.C."/>
+<person name="Madania A."/>
+<person name="Mannhaupt G."/>
+<person name="Marck C."/>
+<person name="Martin R.P."/>
+<person name="Mewes H.-W."/>
+<person name="Michaux G."/>
+<person name="Paces V."/>
+<person name="Parle-McDermott A.G."/>
+<person name="Pearson B.M."/>
+<person name="Perrin A."/>
+<person name="Pettersson B."/>
+<person name="Poch O."/>
+<person name="Pohl T.M."/>
+<person name="Poirey R."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rechmann S."/>
+<person name="Schwager C."/>
+<person name="Schweizer M."/>
+<person name="Sor F."/>
+<person name="Sterky F."/>
+<person name="Tarassov I.A."/>
+<person name="Teodoru C."/>
+<person name="Tettelin H."/>
+<person name="Thierry A."/>
+<person name="Tobiasch E."/>
+<person name="Tzermia M."/>
+<person name="Uhlen M."/>
+<person name="Unseld M."/>
+<person name="Valens M."/>
+<person name="Vandenbol M."/>
+<person name="Vetter I."/>
+<person name="Vlcek C."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler H."/>
+<person name="Wiemann S."/>
+<person name="Winsor B."/>
+<person name="Wolfe K.H."/>
+<person name="Zollner A."/>
+<person name="Zumstein E."/>
+<person name="Kleine K."/>
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+<dbReference type="PubMed" id="9169874"/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
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+<reference key="4">
+<citation type="submission" date="2005-06" db="UniProtKB">
+<authorList>
+<person name="Bienvenut W.V."/>
+<person name="Peters C."/>
+</authorList>
+</citation>
+<scope>PROTEIN SEQUENCE OF 131-142 AND 158-171</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2002" name="Cell Stress Chaperones" volume="7" first="258" last="268">
+<title>Small glutamine-rich protein/viral protein U-binding protein is a novel cochaperone that affects heat shock protein 70 activity.</title>
+<authorList>
+<person name="Angeletti P.C."/>
+<person name="Walker D."/>
+<person name="Panganiban A.T."/>
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+<dbReference type="DOI" id="10.1379/1466-1268(2002)007&lt;0258:sgrpvp>2.0.co;2"/>
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+<scope>FUNCTION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
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+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2007" name="Cell Stress Chaperones" volume="12" first="59" last="70">
+<title>SGT2 and MDY2 interact with molecular chaperone YDJ1 in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Liou S.-T."/>
+<person name="Cheng M.-Y."/>
+<person name="Wang C."/>
+</authorList>
+<dbReference type="PubMed" id="17441508"/>
+<dbReference type="DOI" id="10.1379/csc-220r.1"/>
+</citation>
+<scope>INTERACTION WITH HSC82; HSP104; MDY2; SSA1 AND SSA2</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-308</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
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+<text evidence="1 2">Co-chaperone that binds to the molecular chaperone Hsp70 (SSA1 and SSA2). Regulates Hsp70 ATPase activity (By similarity). Required for recovery from heat shock.</text>
+</comment>
+<comment type="subunit">
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+<title>The complete DNA sequence of yeast chromosome III.</title>
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+<person name="van der Aart Q.J.M."/>
+<person name="Agostoni-Carbone M.L."/>
+<person name="Aigle M."/>
+<person name="Alberghina L."/>
+<person name="Alexandraki D."/>
+<person name="Antoine G."/>
+<person name="Anwar R."/>
+<person name="Ballesta J.P.G."/>
+<person name="Benit P."/>
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+<person name="Brown A."/>
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+<person name="Carcano C."/>
+<person name="Carignani G."/>
+<person name="Cederberg H."/>
+<person name="Chanet R."/>
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+<person name="Crouzet M."/>
+<person name="Daignan-Fornier B."/>
+<person name="Defoor E."/>
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+<person name="Xu G."/>
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+<person name="Gromadka R."/>
+</authorList>
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+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
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+<citation type="journal article" date="1992" name="Yeast" volume="8" first="681" last="687">
+<title>Nucleotide sequence of D10B, a BamHI fragment on the small-ring chromosome III of Saccharomyces cerevisiae.</title>
+<authorList>
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+<dbReference type="DOI" id="10.1002/yea.320080813"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-214</scope>
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+<citation type="journal article" date="1999" name="Nucleic Acids Res." volume="27" first="4598" last="4608">
+<title>Spb1p is a putative methyltransferase required for 60S ribosomal subunit biogenesis in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Kressler D."/>
+<person name="Rojo M."/>
+<person name="Linder P."/>
+<person name="de la Cruz J."/>
+</authorList>
+<dbReference type="PubMed" id="10556316"/>
+<dbReference type="DOI" id="10.1093/nar/27.23.4598"/>
+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2000" name="Mol. Cell. Biol." volume="20" first="1370" last="1381">
+<title>Spb1p is a yeast nucleolar protein associated with Nop1p and Nop58p that is able to bind S-adenosyl-L-methionine in vitro.</title>
+<authorList>
+<person name="Pintard L."/>
+<person name="Kressler D."/>
+<person name="Lapeyre B."/>
+</authorList>
+<dbReference type="PubMed" id="10648622"/>
+<dbReference type="DOI" id="10.1128/mcb.20.4.1370-1381.2000"/>
+</citation>
+<scope>BINDING TO S-ADENOSYL-L-METHIONINE</scope>
+<scope>INTERACTION WITH NOP1 AND NOP58</scope>
+<scope>SUBCELLULAR LOCATION</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2002" name="EMBO J." volume="21" first="5539" last="5547">
+<title>60S pre-ribosome formation viewed from assembly in the nucleolus until export to the cytoplasm.</title>
+<authorList>
+<person name="Nissan T.A."/>
+<person name="Bassler J."/>
+<person name="Petfalski E."/>
+<person name="Tollervey D."/>
+<person name="Hurt E."/>
+</authorList>
+<dbReference type="PubMed" id="12374754"/>
+<dbReference type="DOI" id="10.1093/emboj/cdf547"/>
+</citation>
+<scope>IDENTIFICATION IN THE PRE-60S RIBOSOMAL PARTICLE</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2003" name="Mol. Cell" volume="12" first="1309" last="1315">
+<title>Functional redundancy of Spb1p and a snR52-dependent mechanism for the 2'-O-ribose methylation of a conserved rRNA position in yeast.</title>
+<authorList>
+<person name="Bonnerot C."/>
+<person name="Pintard L."/>
+<person name="Lutfalla G."/>
+</authorList>
+<dbReference type="PubMed" id="14636587"/>
+<dbReference type="DOI" id="10.1016/s1097-2765(03)00435-0"/>
+</citation>
+<scope>FUNCTION</scope>
+<scope>CATALYTIC ACTIVITY</scope>
+<scope>MUTAGENESIS OF ASP-52</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2004" name="Mol. Cell" volume="16" first="663" last="669">
+<title>Spb1p-directed formation of Gm2922 in the ribosome catalytic center occurs at a late processing stage.</title>
+<authorList>
+<person name="Lapeyre B."/>
+<person name="Purushothaman S.K."/>
+</authorList>
+<dbReference type="PubMed" id="15546625"/>
+<dbReference type="DOI" id="10.1016/j.molcel.2004.10.022"/>
+</citation>
+<scope>FUNCTION</scope>
+</reference>
+<reference key="10">
+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
+<person name="Haas W."/>
+<person name="Villen J."/>
+<person name="Elias J.E."/>
+<person name="Gygi S.P."/>
+</authorList>
+<dbReference type="PubMed" id="17330950"/>
+<dbReference type="DOI" id="10.1021/pr060559j"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455 AND SER-529</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ADR376</strain>
+</source>
+</reference>
+<reference key="11">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="12">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455; SER-464 AND SER-529</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="1 2 5 6">Required for proper assembly of pre-ribosomal particles during the biogenesis of the 60S ribosomal subunit. Specifically methylates the guanosine in position 2922 of the 25S rRNA at the stage of 27S pre-rRNA maturation. Methylates also the uridine in position 2921 in the absence of methylation of this residue guided by snoRNA snR52 at the stage of 35S pre-rRNA maturation.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="5">
+<text>guanosine(2922) in 27S pre-rRNA + S-adenosyl-L-methionine = 2'-O-methylguanosine(2922) in 27S pre-rRNA + H(+) + S-adenosyl-L-homocysteine</text>
+<dbReference type="Rhea" id="RHEA:42724"/>
+<dbReference type="Rhea" id="RHEA-COMP:10200"/>
+<dbReference type="Rhea" id="RHEA-COMP:10201"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:57856"/>
+<dbReference type="ChEBI" id="CHEBI:59789"/>
+<dbReference type="ChEBI" id="CHEBI:74269"/>
+<dbReference type="ChEBI" id="CHEBI:74445"/>
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+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1 3 4">Component of the nucleolar and nucleoplasmic pre-60S ribosomal particle. Interacts with the snoRNA-associated proteins NOP1 and NOP58.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-17814">
+<id>P25582</id>
+</interactant>
+<interactant intactId="EBI-22906">
+<id>P43586</id>
+<label>LOC1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>4</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-17814">
+<id>P25582</id>
+</interactant>
+<interactant intactId="EBI-36093">
+<id>Q07896</id>
+<label>NOC3</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-17814">
+<id>P25582</id>
+</interactant>
+<interactant intactId="EBI-29395">
+<id>Q12080</id>
+<label>NOP53</label>
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+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-17814">
+<id>P25582</id>
+</interactant>
+<interactant intactId="EBI-15881">
+<id>P36160</id>
+<label>RPF2</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>6</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1 3">Nucleus</location>
+<location evidence="1 3">Nucleolus</location>
+</subcellularLocation>
+</comment>
+<comment type="similarity">
+<text evidence="1">Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.</text>
+</comment>
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+<property type="protein sequence ID" value="CAA42391.1"/>
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+<dbReference type="RefSeq" id="NP_009877.1">
+<property type="nucleotide sequence ID" value="NM_001178698.1"/>
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+<dbReference type="PDBsum" id="6ELZ"/>
+<dbReference type="PDBsum" id="6EM5"/>
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+<dbReference type="DIP" id="DIP-1777N"/>
+<dbReference type="IntAct" id="P25582">
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+<dbReference type="MINT" id="P25582"/>
+<dbReference type="STRING" id="4932.YCL054W"/>
+<dbReference type="iPTMnet" id="P25582"/>
+<dbReference type="MaxQB" id="P25582"/>
+<dbReference type="PaxDb" id="P25582"/>
+<dbReference type="PRIDE" id="P25582"/>
+<dbReference type="EnsemblFungi" id="YCL054W_mRNA">
+<property type="protein sequence ID" value="YCL054W"/>
+<property type="gene ID" value="YCL054W"/>
+</dbReference>
+<dbReference type="GeneID" id="850304"/>
+<dbReference type="KEGG" id="sce:YCL054W"/>
+<dbReference type="SGD" id="S000000559">
+<property type="gene designation" value="SPB1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YCL054W"/>
+<dbReference type="eggNOG" id="KOG1098">
+<property type="taxonomic scope" value="Eukaryota"/>
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+<dbReference type="GeneTree" id="ENSGT00550000075004"/>
+<dbReference type="HOGENOM" id="CLU_009422_8_1_1"/>
+<dbReference type="OMA" id="EILECCK"/>
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+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome III"/>
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+<dbReference type="GO" id="GO:0016435">
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+<dbReference type="GO" id="GO:0070039">
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+</dbReference>
+<dbReference type="HAMAP" id="MF_03163">
+<property type="entry name" value="RNA_methyltr_E_SPB1"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015507">
+<property type="entry name" value="rRNA-MeTfrase_E"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012920">
+<property type="entry name" value="rRNA_MeTfrase_Spb1_C"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR024576">
+<property type="entry name" value="rRNA_MeTfrase_Spb1_DUF3381"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR002877">
+<property type="entry name" value="rRNA_MeTrfase_FtsJ_dom"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR029063">
+<property type="entry name" value="SAM-dependent_MTases"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR028589">
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+</dbReference>
+<dbReference type="Pfam" id="PF11861">
+<property type="entry name" value="DUF3381"/>
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+</dbReference>
+<dbReference type="Pfam" id="PF01728">
+<property type="entry name" value="FtsJ"/>
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+<dbReference type="Pfam" id="PF07780">
+<property type="entry name" value="Spb1_C"/>
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+</dbReference>
+<dbReference type="SUPFAM" id="SSF53335">
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+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0175">Coiled coil</keyword>
+<keyword id="KW-0489">Methyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0690">Ribosome biogenesis</keyword>
+<keyword id="KW-0698">rRNA processing</keyword>
+<keyword id="KW-0949">S-adenosyl-L-methionine</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<feature type="chain" description="27S pre-rRNA (guanosine(2922)-2'-O)-methyltransferase" id="PRO_0000155604">
+<location>
+<begin position="1"/>
+<end position="841"/>
+</location>
+</feature>
+<feature type="coiled-coil region" evidence="1">
+<location>
+<begin position="360"/>
+<end position="389"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Lys-rich">
+<location>
+<begin position="704"/>
+<end position="841"/>
+</location>
+</feature>
+<feature type="active site" description="Proton acceptor" evidence="1">
+<location>
+<position position="159"/>
+</location>
+</feature>
+<feature type="binding site" description="S-adenosyl-L-methionine; via amide nitrogen" evidence="1">
+<location>
+<position position="58"/>
+</location>
+</feature>
+<feature type="binding site" description="S-adenosyl-L-methionine; via amide nitrogen" evidence="1">
+<location>
+<position position="60"/>
+</location>
+</feature>
+<feature type="binding site" description="S-adenosyl-L-methionine" evidence="1">
+<location>
+<position position="78"/>
+</location>
+</feature>
+<feature type="binding site" description="S-adenosyl-L-methionine" evidence="1">
+<location>
+<position position="94"/>
+</location>
+</feature>
+<feature type="binding site" description="S-adenosyl-L-methionine" evidence="1">
+<location>
+<position position="119"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="7 9">
+<location>
+<position position="455"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="9">
+<location>
+<position position="464"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="7 8 9">
+<location>
+<position position="529"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Abolishes methyltransferase activity." evidence="5">
+<original>D</original>
+<variation>A</variation>
+<location>
+<position position="52"/>
+</location>
+</feature>
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+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
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+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="10648622"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000269">
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+</source>
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+</source>
+</evidence>
+<evidence key="9" type="ECO:0007744">
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+</source>
+</evidence>
+<sequence length="841" mass="96485" checksum="D7A080299B0C7E24" modified="2000-05-30" version="2">MGKTQKKNSKGRLDRYYYLAKEKGYRARSSFKIIQINEKYGHFLEKSKVVIDLCAAPGSWCQVASKLCPVNSLIIGVDIVPMKPMPNVITFQSDITTEDCRSKLRGYMKTWKADTVLHDGAPNVGLGWVQDAFTQSQLTLQALKLAVENLVVNGTFVTKIFRSKDYNKLIWVFQQLFEKVEATKPPASRNVSAEIFVVCKGFKAPKRLDPRLLDPKEVFEELPDGQQNMESKIYNPEKKVRKRQGYEEGDNLLYHETSILDFVRTEDPISMLGEMNKFTIDENDHEWKILKKLKQTTDEFRSCIEDLKVLGKKDFKMILRWRKIAREILGIEVKDDAKTEIEVVPLTEEEQIEKDLQGLQEKQRLNVKRERRRKNEMKQKELQRMQMNMITPTDIGIEAASLGKESLFNLKTAEKTGILNDLAKGKKRMIFTDDELAKDNDIYIDENIMIKDKDSAADADDLESELNAMYSDYKTRRSERDAKFRAKQARGGDNEEEWTGFNEGSLEKKEEEGKDYIEDNDDEGVEGDSDDDEAITNLISKLKGQEGDHKLSSKARMIFNDPIFNNVEPDLPVNTVNDGIMSSESVGDISKLNKKRKHEEMHQKQDEADSSDESSSDDSDFEIVANDNASEEFDSDYDSEEEKNQTKKEKHSRDIDIATVEAMTLAHQLALGQKNKHDLVDEGFNRYTFRDTENLPDWFLEDEKEHSKINKPITKEAAMAIKEKIKAMNARPIKKVAEAKARKRMRAVARLEKIKKKAGLINDDSDKTEKDKAEEISRLMRKVTKKPKTKPKVTLVVASGRNKGLAGRPKGVKGKYKMVDGVMKNEQRALRRIAKKHHKKK</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1993-10-01" modified="2021-04-07" version="185">
+<accession>P32558</accession>
+<accession>D6VTU8</accession>
+<name>SPT16_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>FACT complex subunit SPT16</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Cell division control protein 68</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Facilitates chromatin transcription complex subunit SPT16</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Suppressor of Ty protein 16</fullName>
+</alternativeName>
+</protein>
+<gene>
+<name type="primary">SPT16</name>
+<name type="synonym">CDC68</name>
+<name type="synonym">SSF1</name>
+<name type="ordered locus">YGL207W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
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+<person name="Morgan D.O."/>
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+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="2 4 7 9 11 12 13">Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. Transcription elongation is promoted by the repression of transcription initiation from cryptic sites. Also acts in establishing transcription initiation complexes and promotes SPT15/TBP-binding to a TATA box. Together with replication factor-A protein (RPA), FACT may play a role in nucleosome deposition during DNA replication.</text>
+</comment>
+<comment type="subunit">
+<text evidence="2 3 5 6 8 14 15 16">Forms a stable heterodimer with POB3. The SPT16-POB3 dimer weakly associates with multiple molecules of NHP6 (NHP6A or NHP6B) to form the FACT (yFACT or SNP) complex. The FACT complex interacts with the CK2 (casein kinase II) complex subunits CKA1, CKA2, CKB1 and CKB2 and the components of the transcription machinery CHD1, CTR9, PAF1 and CDC73. The FACT complex interacts with the PAF1 complex. SPT16 interacts with SAS3 and POL1.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-4334">
+<id>P32558</id>
+</interactant>
+<interactant intactId="EBI-27863">
+<id>Q04636</id>
+<label>POB3</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>8</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-4334">
+<id>P32558</id>
+</interactant>
+<interactant intactId="EBI-17402">
+<id>P32908</id>
+<label>SMC1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Nucleus</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Chromosome</location>
+</subcellularLocation>
+<text>Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="10">Present with 18500 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="17">Belongs to the peptidase M24 family. SPT16 subfamily.</text>
+</comment>
+<comment type="caution">
+<text evidence="17">Although related to the peptidase M24 family, this protein lacks conserved active site residues suggesting that it may lack peptidase activity.</text>
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+<property type="pathway name" value="TP53 Regulates Transcription of DNA Repair Genes"/>
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+<dbReference type="Reactome" id="R-SCE-75955">
+<property type="pathway name" value="RNA Polymerase II Transcription Elongation"/>
+</dbReference>
+<dbReference type="EvolutionaryTrace" id="P32558"/>
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+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome VII"/>
+</dbReference>
+<dbReference type="RNAct" id="P32558">
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+<dbReference type="GO" id="GO:0000785">
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+<property type="term" value="P:regulation of sister chromatid cohesion"/>
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+</dbReference>
+<dbReference type="CDD" id="cd01091">
+<property type="entry name" value="CDC68-like"/>
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+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR029149">
+<property type="entry name" value="Creatin/AminoP/Spt16_NTD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036005">
+<property type="entry name" value="Creatinase/aminopeptidase-like"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013719">
+<property type="entry name" value="DUF1747"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR029148">
+<property type="entry name" value="FACT-Spt16_Nlobe"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013953">
+<property type="entry name" value="FACT_Spt16"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000994">
+<property type="entry name" value="Pept_M24"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR011993">
+<property type="entry name" value="PH-like_dom_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR040258">
+<property type="entry name" value="Spt16"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR033825">
+<property type="entry name" value="Spt16_M24"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR13980">
+<property type="entry name" value="PTHR13980"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF14826">
+<property type="entry name" value="FACT-Spt16_Nlob"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00557">
+<property type="entry name" value="Peptidase_M24"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF08512">
+<property type="entry name" value="Rtt106"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF08644">
+<property type="entry name" value="SPT16"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM01285">
+<property type="entry name" value="FACT-Spt16_Nlob"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM01287">
+<property type="entry name" value="Rtt106"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM01286">
+<property type="entry name" value="SPT16"/>
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+<dbReference type="SUPFAM" id="SSF55920">
+<property type="entry name" value="SSF55920"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0010">Activator</keyword>
+<keyword id="KW-0158">Chromosome</keyword>
+<keyword id="KW-0175">Coiled coil</keyword>
+<keyword id="KW-0227">DNA damage</keyword>
+<keyword id="KW-0234">DNA repair</keyword>
+<keyword id="KW-0235">DNA replication</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0678">Repressor</keyword>
+<keyword id="KW-0804">Transcription</keyword>
+<keyword id="KW-0805">Transcription regulation</keyword>
+<feature type="chain" description="FACT complex subunit SPT16" id="PRO_0000089448">
+<location>
+<begin position="1"/>
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+</feature>
+<feature type="coiled-coil region" evidence="1">
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+</feature>
+<feature type="coiled-coil region" evidence="1">
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+</feature>
+<feature type="coiled-coil region" evidence="1">
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+</feature>
+<feature type="compositionally biased region" description="Asp/Glu-rich (acidic)">
+<location>
+<begin position="958"/>
+<end position="1021"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="22">
+<location>
+<position position="526"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="22">
+<location>
+<position position="765"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with L-570." evidence="4">
+<original>P</original>
+<variation>S</variation>
+<location>
+<position position="565"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In spt16-4; induces a spt phenotype characterized by depletion of many mRNAs; when associated with S-565." evidence="4">
+<original>P</original>
+<variation>L</variation>
+<location>
+<position position="570"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In cdc68-1; induces a spt phenotype characterized by depletion of many mRNAs." evidence="16">
+<original>G</original>
+<variation>D</variation>
+<location>
+<position position="836"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In spt16-7; induces a spt phenotype characterized by depletion of many mRNAs." evidence="4">
+<original>TTD</original>
+<variation>IIY</variation>
+<location>
+<begin position="848"/>
+<end position="850"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="In spt16-6; induces a spt phenotype characterized by depletion of many mRNAs." evidence="4">
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+<location>
+<position position="920"/>
+</location>
+</feature>
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+<person name="Hata H."/>
+<person name="Mitsui H."/>
+<person name="Liu H."/>
+<person name="Bai Y."/>
+<person name="Denis C.L."/>
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+<title>A yeast gene product, G4p2, with a specific affinity for quadruplex nucleic acids.</title>
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+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
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+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
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+<person name="Rolfs A."/>
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+<person name="Williamson J."/>
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+<person name="Harlow E."/>
+<person name="Marsischky G."/>
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+<title>The yeast STM1 gene encodes a purine motif triple helical DNA-binding protein.</title>
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+<title>Similarity between the association factor of ribosomal subunits and the protein Stm1p from Saccharomyces cerevisiae.</title>
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+<title>STM1, a gene which encodes a guanine quadruplex binding protein, interacts with CDC13 in Saccharomyces cerevisiae.</title>
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+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
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+<person name="Huh W.-K."/>
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+<person name="Howson R.W."/>
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+<person name="Mehta D.V."/>
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+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
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+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
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+<title>Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.</title>
+<authorList>
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+<person name="Huttenhower C."/>
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+<person name="Syka J.E.P."/>
+<person name="Bai D.L."/>
+<person name="Shabanowitz J."/>
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+<person name="Smolka M.B."/>
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+<person name="Bafna V."/>
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+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="17">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-118</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="18">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
+</authorList>
+<dbReference type="PubMed" id="22106047"/>
+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-46; LYS-121; LYS-171 AND LYS-184</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="3">Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs. Acts with CDC13 to control telomere length homeostasis. Involved in the control of the apoptosis-like cell death.</text>
+</comment>
+<comment type="subunit">
+<text evidence="1 3">Interacts with CDC13. Associates with mature 80S ribosomes. Associates with the telomere-proximal Y' element.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-11238">
+<id>P39015</id>
+</interactant>
+<interactant intactId="EBI-701">
+<id>P33203</id>
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+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
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+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Nucleus</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Cytoplasm</location>
+<location>Perinuclear region</location>
+</subcellularLocation>
+<text>Concentrated in the perinuclear region.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 46842 molecules/cell in log phase SD medium.</text>
+</comment>
+<dbReference type="EMBL" id="D26183">
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+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0832">Ubl conjugation</keyword>
+<feature type="initiator methionine" description="Removed" evidence="4">
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+<position position="1"/>
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+</feature>
+<feature type="chain" description="Suppressor protein STM1" id="PRO_0000072278">
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+<end position="273"/>
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+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
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+<begin position="38"/>
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+</feature>
+<feature type="compositionally biased region" description="Ser/Thr-rich">
+<location>
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+</feature>
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+<position position="46"/>
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+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
+<location>
+<position position="121"/>
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+</feature>
+<feature type="cross-link" description="Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)" evidence="13">
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+</feature>
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+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.</title>
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+<person name="Tettelin H."/>
+<person name="Agostoni-Carbone M.L."/>
+<person name="Albermann K."/>
+<person name="Albers M."/>
+<person name="Arroyo J."/>
+<person name="Backes U."/>
+<person name="Barreiros T."/>
+<person name="Bertani I."/>
+<person name="Bjourson A.J."/>
+<person name="Brueckner M."/>
+<person name="Bruschi C.V."/>
+<person name="Carignani G."/>
+<person name="Castagnoli L."/>
+<person name="Cerdan E."/>
+<person name="Clemente M.L."/>
+<person name="Coblenz A."/>
+<person name="Coglievina M."/>
+<person name="Coissac E."/>
+<person name="Defoor E."/>
+<person name="Del Bino S."/>
+<person name="Delius H."/>
+<person name="Delneri D."/>
+<person name="de Wergifosse P."/>
+<person name="Dujon B."/>
+<person name="Durand P."/>
+<person name="Entian K.-D."/>
+<person name="Eraso P."/>
+<person name="Escribano V."/>
+<person name="Fabiani L."/>
+<person name="Fartmann B."/>
+<person name="Feroli F."/>
+<person name="Feuermann M."/>
+<person name="Frontali L."/>
+<person name="Garcia-Gonzalez M."/>
+<person name="Garcia-Saez M.I."/>
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+<person name="Guerreiro P."/>
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+<person name="Hebling U."/>
+<person name="Hernandez K."/>
+<person name="Heumann K."/>
+<person name="Hilger F."/>
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+<person name="Indge K.J."/>
+<person name="James C.M."/>
+<person name="Klima R."/>
+<person name="Koetter P."/>
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+<person name="Schaefer M."/>
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+<person name="Zollner A."/>
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+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
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+<citation type="journal article" date="1998" name="Eur. J. Biochem." volume="258" first="736" last="743">
+<title>Genes of succinyl-CoA ligase from Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Przybyla-Zawislak B."/>
+<person name="Dennis R.A."/>
+<person name="Zakharkin S.O."/>
+<person name="McCammon M.T."/>
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+<citation type="journal article" date="2003" name="Proc. Natl. Acad. Sci. U.S.A." volume="100" first="13207" last="13212">
+<title>The proteome of Saccharomyces cerevisiae mitochondria.</title>
+<authorList>
+<person name="Sickmann A."/>
+<person name="Reinders J."/>
+<person name="Wagner Y."/>
+<person name="Joppich C."/>
+<person name="Zahedi R.P."/>
+<person name="Meyer H.E."/>
+<person name="Schoenfisch B."/>
+<person name="Perschil I."/>
+<person name="Chacinska A."/>
+<person name="Guiard B."/>
+<person name="Rehling P."/>
+<person name="Pfanner N."/>
+<person name="Meisinger C."/>
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+<dbReference type="DOI" id="10.1073/pnas.2135385100"/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ATCC 76625 / YPH499</strain>
+</source>
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+<reference key="6">
+<citation type="journal article" date="2007" name="J. Proteome Res." volume="6" first="1190" last="1197">
+<title>Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Li X."/>
+<person name="Gerber S.A."/>
+<person name="Rudner A.D."/>
+<person name="Beausoleil S.A."/>
+<person name="Haas W."/>
+<person name="Villen J."/>
+<person name="Elias J.E."/>
+<person name="Gygi S.P."/>
+</authorList>
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+<dbReference type="DOI" id="10.1021/pr060559j"/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ADR376</strain>
+</source>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; SER-263 AND SER-276</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<text evidence="1 3">Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents the only step of substrate-level phosphorylation in the TCA (PubMed:9874242). The beta subunit provides nucleotide specificity of the enzyme and binds the substrate succinate, while the binding sites for coenzyme A and phosphate are found in the alpha subunit (By similarity).</text>
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+<text>ATP + CoA + succinate = ADP + phosphate + succinyl-CoA</text>
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+<text evidence="1">Binds 1 Mg(2+) ion per subunit.</text>
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+<text>Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1.</text>
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+<title>Snap helix with knob and hole: essential repeats in S. pombe nuclear protein nuc2+.</title>
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+<person name="Hirano T."/>
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+<title>Identification of a 60-kilodalton stress-related protein, p60, which interacts with hsp90 and hsp70.</title>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
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+<text>Part of a larger complex that includes HSP70, HSP90, and immunophilins.</text>
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+<title>Tom71, a novel homologue of the mitochondrial preprotein receptor Tom70.</title>
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+<person name="Lill R."/>
+<person name="Neupert W."/>
+<person name="Court D.A."/>
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+<title>Global analysis of protein localization in budding yeast.</title>
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+<person name="Sickmann A."/>
+<person name="Reinders J."/>
+<person name="Wagner Y."/>
+<person name="Joppich C."/>
+<person name="Zahedi R.P."/>
+<person name="Meyer H.E."/>
+<person name="Schoenfisch B."/>
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+<person name="Li X."/>
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+<citation type="journal article" date="1994" name="EMBO J." volume="13" first="5795" last="5809">
+<title>Complete DNA sequence of yeast chromosome II.</title>
+<authorList>
+<person name="Feldmann H."/>
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+<person name="Crouzet M."/>
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+<person name="Messenguy F."/>
+<person name="Miosga T."/>
+<person name="Molemans F."/>
+<person name="Mueller S."/>
+<person name="Nasr F."/>
+<person name="Obermaier B."/>
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+<person name="Pierard A."/>
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+<person name="Potier S."/>
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+<person name="Scherens B."/>
+<person name="Schwarzlose C."/>
+<person name="Skala J."/>
+<person name="Slonimski P.P."/>
+<person name="Smits P.H.M."/>
+<person name="Souciet J.-L."/>
+<person name="Steensma H.Y."/>
+<person name="Stucka R."/>
+<person name="Urrestarazu L.A."/>
+<person name="van der Aart Q.J.M."/>
+<person name="Van Dyck L."/>
+<person name="Vassarotti A."/>
+<person name="Vetter I."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Wagner G."/>
+<person name="de Wergifosse P."/>
+<person name="Wolfe K.H."/>
+<person name="Zagulski M."/>
+<person name="Zimmermann F.K."/>
+<person name="Mewes H.-W."/>
+<person name="Kleine K."/>
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+<dbReference type="DOI" id="10.1002/j.1460-2075.1994.tb06923.x"/>
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+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
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+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
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+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
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+<scope>GENOME REANNOTATION</scope>
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+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
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+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
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+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
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+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2004" name="EMBO Rep." volume="5" first="818" last="824">
+<title>Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation.</title>
+<authorList>
+<person name="Schuberth C."/>
+<person name="Richly H."/>
+<person name="Rumpf S."/>
+<person name="Buchberger A."/>
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+<dbReference type="DOI" id="10.1038/sj.embor.7400203"/>
+</citation>
+<scope>INTERACTION WITH CDC48</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-388</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2012" name="Proc. Natl. Acad. Sci. U.S.A." volume="109" first="12449" last="12454">
+<title>N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.</title>
+<authorList>
+<person name="Van Damme P."/>
+<person name="Lasa M."/>
+<person name="Polevoda B."/>
+<person name="Gazquez C."/>
+<person name="Elosegui-Artola A."/>
+<person name="Kim D.S."/>
+<person name="De Juan-Pardo E."/>
+<person name="Demeyer K."/>
+<person name="Hole K."/>
+<person name="Larrea E."/>
+<person name="Timmerman E."/>
+<person name="Prieto J."/>
+<person name="Arnesen T."/>
+<person name="Sherman F."/>
+<person name="Gevaert K."/>
+<person name="Aldabe R."/>
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+<dbReference type="PubMed" id="22814378"/>
+<dbReference type="DOI" id="10.1073/pnas.1210303109"/>
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+</reference>
+<reference key="9">
+<citation type="journal article" date="2012" name="Proteomics" volume="12" first="236" last="240">
+<title>Sites of ubiquitin attachment in Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Starita L.M."/>
+<person name="Lo R.S."/>
+<person name="Eng J.K."/>
+<person name="von Haller P.D."/>
+<person name="Fields S."/>
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+<dbReference type="DOI" id="10.1002/pmic.201100166"/>
+</citation>
+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-19</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Involved in CDC48-dependent protein degradation through the ubiquitin/proteasome pathway.</text>
+</comment>
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+<text evidence="5">Interacts with CDC48.</text>
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+<interactant intactId="EBI-21157">
+<id>P38349</id>
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+<interactant intactId="EBI-4308">
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+<text evidence="4">Present with 2190 molecules/cell in log phase SD medium.</text>
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+<keyword id="KW-1017">Isopeptide bond</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
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+<shortName>VDE</shortName>
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+<name type="synonym">TFP1</name>
+<name type="ordered locus">YDL185W</name>
+<name type="ORF">D1286</name>
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+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
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+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1990" name="J. Biol. Chem." volume="265" first="6726" last="6733">
+<title>Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hirata R."/>
+<person name="Ohsumi Y."/>
+<person name="Nakano A."/>
+<person name="Kawasaki H."/>
+<person name="Suzuki K."/>
+<person name="Anraku Y."/>
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+<dbReference type="PubMed" id="2139027"/>
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+<scope>PROTEIN SEQUENCE OF 181-196; 815-820; 826-836; 862-879; 925-936 AND 1004-1013</scope>
+<scope>SUBUNIT</scope>
+<source>
+<strain>ATCC 26786 / X2180-1A</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="961" last="966">
+<title>New open reading frames, one of which is similar to the nifV gene of Azotobacter vinelandii, found on a 12.5 kbp fragment of chromosome IV of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Verhasselt P."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+</authorList>
+<dbReference type="PubMed" id="8533471"/>
+<dbReference type="DOI" id="10.1002/yea.320111007"/>
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+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
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+<strain>ATCC 96604 / S288c / FY1679</strain>
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+</reference>
+<comment type="function">
+<text evidence="10">Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase (vacuolar ATPase) is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. It is an electrogenic proton pump that generates a proton motive force of 180 mV, inside positive and acidic, in the vacuolar membrane vesicles. It may participate in maintenance of cytoplasmic Ca(2+) homeostasis. This is a catalytic subunit.</text>
+</comment>
+<comment type="function">
+<text evidence="10">PI-SceI is an endonuclease that can cleave at a site present in a VMA1 allele that lacks the derived endonuclease segment of the open reading frame; cleavage at this site only occurs during meiosis and initiates 'homing', a genetic event that converts a VMA1 allele lacking VDE into one that contains it.</text>
+</comment>
+<comment type="catalytic activity">
+<reaction evidence="3">
+<text>ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate</text>
+<dbReference type="Rhea" id="RHEA:57720"/>
+<dbReference type="ChEBI" id="CHEBI:15377"/>
+<dbReference type="ChEBI" id="CHEBI:15378"/>
+<dbReference type="ChEBI" id="CHEBI:30616"/>
+<dbReference type="ChEBI" id="CHEBI:43474"/>
+<dbReference type="ChEBI" id="CHEBI:456216"/>
+<dbReference type="EC" id="7.1.2.2"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="5 11">V-ATPase is a heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'', d and e). Interacts with RAV1 and RAV2 components of the RAVE complex, which are essential for the stability and assembly of V-ATPase.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-20245">
+<id>P17255</id>
+</interactant>
+<interactant intactId="EBI-25471">
+<id>P47104</id>
+<label>RAV1</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>2</experiments>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-20245">
+<id>P17255</id>
+</interactant>
+<interactant intactId="EBI-20201">
+<id>P32366</id>
+<label>VMA6</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>6</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="8">Endomembrane system</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="14">Vacuole membrane</location>
+</subcellularLocation>
+<text>Membranes of various intracellular acidic compartments.</text>
+</comment>
+<comment type="PTM">
+<text>This protein undergoes a protein self splicing that involves a post-translational excision of the VDE intervening region (intein) followed by peptide ligation.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="9">Present with 199895 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="13">Belongs to the ATPase alpha/beta chains family.</text>
+</comment>
+<comment type="online information" name="Description of Sce VMA in Inbase">
+<link uri="http://tools.neb.com/inbase/intein.php?name=Sce+VMA"/>
+</comment>
+<dbReference type="EC" id="7.1.2.2"/>
+<dbReference type="EC" id="3.1.-.-"/>
+<dbReference type="EMBL" id="J05409">
+<property type="protein sequence ID" value="AAA34664.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X83276">
+<property type="protein sequence ID" value="CAA58261.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z74233">
+<property type="protein sequence ID" value="CAA98760.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z74233">
+<property type="protein sequence ID" value="CAA98761.1"/>
+<property type="status" value="ALT_SEQ"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z74233">
+<property type="protein sequence ID" value="CAA98762.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="X58857">
+<property type="protein sequence ID" value="CAA41657.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="M21609">
+<property type="protein sequence ID" value="AAB63978.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006938">
+<property type="protein sequence ID" value="DAA11677.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="A35746">
+<property type="entry name" value="PXBYVA"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_010096.1">
+<property type="nucleotide sequence ID" value="NM_001180245.1"/>
+</dbReference>
+<dbReference type="PDB" id="1DFA">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.00"/>
+<property type="chains" value="A=284-737"/>
+</dbReference>
+<dbReference type="PDB" id="1EF0">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.10"/>
+<property type="chains" value="A/B=283-741"/>
+</dbReference>
+<dbReference type="PDB" id="1GPP">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="1.35"/>
+<property type="chains" value="A=284-466, A=693-736"/>
+</dbReference>
+<dbReference type="PDB" id="1JVA">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.10"/>
+<property type="chains" value="A/B=274-747"/>
+</dbReference>
+<dbReference type="PDB" id="1LWS">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="3.50"/>
+<property type="chains" value="A=284-737"/>
+</dbReference>
+<dbReference type="PDB" id="1LWT">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="3.20"/>
+<property type="chains" value="A=284-737"/>
+</dbReference>
+<dbReference type="PDB" id="1UM2">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.90"/>
+<property type="chains" value="A/B=284-737, C/D=274-747"/>
+</dbReference>
+<dbReference type="PDB" id="1VDE">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="2.40"/>
+<property type="chains" value="A/B=284-737"/>
+</dbReference>
+<dbReference type="PDB" id="3J9T">
+<property type="method" value="EM"/>
+<property type="resolution" value="6.90"/>
+<property type="chains" value="A/C/E=2-1071"/>
+</dbReference>
+<dbReference type="PDB" id="3J9U">
+<property type="method" value="EM"/>
+<property type="resolution" value="7.60"/>
+<property type="chains" value="A/C/E=2-1071"/>
+</dbReference>
+<dbReference type="PDB" id="3J9V">
+<property type="method" value="EM"/>
+<property type="resolution" value="8.30"/>
+<property type="chains" value="A/C/E=2-1071"/>
+</dbReference>
+<dbReference type="PDB" id="5BW9">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="7.00"/>
+<property type="chains" value="A/B/C/a/b/c=1-1071"/>
+</dbReference>
+<dbReference type="PDB" id="5D80">
+<property type="method" value="X-ray"/>
+<property type="resolution" value="6.20"/>
+<property type="chains" value="A/B/C/a/b/c=1-1071"/>
+</dbReference>
+<dbReference type="PDB" id="5VOX">
+<property type="method" value="EM"/>
+<property type="resolution" value="6.80"/>
+<property type="chains" value="A/C/E=1-1071"/>
+</dbReference>
+<dbReference type="PDB" id="5VOY">
+<property type="method" value="EM"/>
+<property type="resolution" value="7.90"/>
+<property type="chains" value="A/C/E=1-1071"/>
+</dbReference>
+<dbReference type="PDB" id="5VOZ">
+<property type="method" value="EM"/>
+<property type="resolution" value="7.60"/>
+<property type="chains" value="A/C/E=1-1071"/>
+</dbReference>
+<dbReference type="PDBsum" id="1DFA"/>
+<dbReference type="PDBsum" id="1EF0"/>
+<dbReference type="PDBsum" id="1GPP"/>
+<dbReference type="PDBsum" id="1JVA"/>
+<dbReference type="PDBsum" id="1LWS"/>
+<dbReference type="PDBsum" id="1LWT"/>
+<dbReference type="PDBsum" id="1UM2"/>
+<dbReference type="PDBsum" id="1VDE"/>
+<dbReference type="PDBsum" id="3J9T"/>
+<dbReference type="PDBsum" id="3J9U"/>
+<dbReference type="PDBsum" id="3J9V"/>
+<dbReference type="PDBsum" id="5BW9"/>
+<dbReference type="PDBsum" id="5D80"/>
+<dbReference type="PDBsum" id="5VOX"/>
+<dbReference type="PDBsum" id="5VOY"/>
+<dbReference type="PDBsum" id="5VOZ"/>
+<dbReference type="SMR" id="P17255"/>
+<dbReference type="BioGRID" id="31859">
+<property type="interactions" value="493"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1192">
+<property type="entry name" value="Vacuolar proton translocating ATPase complex, Golgi variant"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1193">
+<property type="entry name" value="Vacuolar proton translocating ATPase complex, vacuole variant"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-2293N"/>
+<dbReference type="IntAct" id="P17255">
+<property type="interactions" value="103"/>
+</dbReference>
+<dbReference type="MINT" id="P17255"/>
+<dbReference type="STRING" id="4932.YDL185W"/>
+<dbReference type="MEROPS" id="N09.001"/>
+<dbReference type="REBASE" id="2615">
+<property type="entry name" value="PI-SceI"/>
+</dbReference>
+<dbReference type="TCDB" id="3.A.2.2.3">
+<property type="family name" value="the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily"/>
+</dbReference>
+<dbReference type="iPTMnet" id="P17255"/>
+<dbReference type="UCD-2DPAGE" id="P17255"/>
+<dbReference type="MaxQB" id="P17255"/>
+<dbReference type="PaxDb" id="P17255"/>
+<dbReference type="PRIDE" id="P17255"/>
+<dbReference type="EnsemblFungi" id="YDL185W_mRNA">
+<property type="protein sequence ID" value="YDL185W"/>
+<property type="gene ID" value="YDL185W"/>
+</dbReference>
+<dbReference type="GeneID" id="851342"/>
+<dbReference type="KEGG" id="sce:YDL185W"/>
+<dbReference type="SGD" id="S000002344">
+<property type="gene designation" value="VMA1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YDL185W"/>
+<dbReference type="eggNOG" id="KOG1352">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00550000074787"/>
+<dbReference type="HOGENOM" id="CLU_008162_0_1_1"/>
+<dbReference type="InParanoid" id="P17255"/>
+<dbReference type="OMA" id="HNTVTQH"/>
+<dbReference type="Reactome" id="R-SCE-1222556">
+<property type="pathway name" value="ROS and RNS production in phagocytes"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-77387">
+<property type="pathway name" value="Insulin receptor recycling"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-917977">
+<property type="pathway name" value="Transferrin endocytosis and recycling"/>
+</dbReference>
+<dbReference type="Reactome" id="R-SCE-9639288">
+<property type="pathway name" value="Amino acids regulate mTORC1"/>
+</dbReference>
+<dbReference type="EvolutionaryTrace" id="P17255"/>
+<dbReference type="PRO" id="PR:P17255"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome IV"/>
+</dbReference>
+<dbReference type="RNAct" id="P17255">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0012505">
+<property type="term" value="C:endomembrane system"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000329">
+<property type="term" value="C:fungal-type vacuole membrane"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="UniProtKB"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005886">
+<property type="term" value="C:plasma membrane"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005774">
+<property type="term" value="C:vacuolar membrane"/>
+<property type="evidence" value="ECO:0000318"/>
+<property type="project" value="GO_Central"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000221">
+<property type="term" value="C:vacuolar proton-transporting V-type ATPase, V1 domain"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004519">
+<property type="term" value="F:endonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003729">
+<property type="term" value="F:mRNA binding"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046933">
+<property type="term" value="F:proton-transporting ATP synthase activity, rotational mechanism"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046961">
+<property type="term" value="F:proton-transporting ATPase activity, rotational mechanism"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0044267">
+<property type="term" value="P:cellular protein metabolic process"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0016539">
+<property type="term" value="P:intein-mediated protein splicing"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="InterPro"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006314">
+<property type="term" value="P:intron homing"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0007035">
+<property type="term" value="P:vacuolar acidification"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="1.10.1140.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="2.40.30.20">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.10.28.10">
+<property type="match status" value="2"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR031686">
+<property type="entry name" value="ATP-synth_a_Xtn"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR023366">
+<property type="entry name" value="ATP_synth_asu-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR020003">
+<property type="entry name" value="ATPase_a/bsu_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR004100">
+<property type="entry name" value="ATPase_F1/V1/A1_a/bsu_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036121">
+<property type="entry name" value="ATPase_F1/V1/A1_a/bsu_N_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000194">
+<property type="entry name" value="ATPase_F1/V1/A1_a/bsu_nucl-bd"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR024034">
+<property type="entry name" value="ATPase_F1/V1_b/a_C"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR003586">
+<property type="entry name" value="Hint_dom_C"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR003587">
+<property type="entry name" value="Hint_dom_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036844">
+<property type="entry name" value="Hint_dom_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR007868">
+<property type="entry name" value="Hom_end_hint"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR007869">
+<property type="entry name" value="Homing_endonuc_PI-Sce"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR027434">
+<property type="entry name" value="Homing_endonucl"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR006142">
+<property type="entry name" value="INTEIN"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR030934">
+<property type="entry name" value="Intein_C"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR004042">
+<property type="entry name" value="Intein_endonuc"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR006141">
+<property type="entry name" value="Intein_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR027417">
+<property type="entry name" value="P-loop_NTPase"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR022878">
+<property type="entry name" value="V-ATPase_asu"/>
+</dbReference>
+<dbReference type="PANTHER" id="PTHR43607">
+<property type="entry name" value="PTHR43607"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00006">
+<property type="entry name" value="ATP-synt_ab"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF02874">
+<property type="entry name" value="ATP-synt_ab_N"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF16886">
+<property type="entry name" value="ATP-synt_ab_Xtn"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF05204">
+<property type="entry name" value="Hom_end"/>
+<property type="match status" value="2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF05203">
+<property type="entry name" value="Hom_end_hint"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PRINTS" id="PR00379">
+<property type="entry name" value="INTEIN"/>
+</dbReference>
+<dbReference type="SMART" id="SM00305">
+<property type="entry name" value="HintC"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SMART" id="SM00306">
+<property type="entry name" value="HintN"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF50615">
+<property type="entry name" value="SSF50615"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF51294">
+<property type="entry name" value="SSF51294"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF52540">
+<property type="entry name" value="SSF52540"/>
+<property type="match status" value="2"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF55608">
+<property type="entry name" value="SSF55608"/>
+<property type="match status" value="2"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00152">
+<property type="entry name" value="ATPASE_ALPHA_BETA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50818">
+<property type="entry name" value="INTEIN_C_TER"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50819">
+<property type="entry name" value="INTEIN_ENDONUCLEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50817">
+<property type="entry name" value="INTEIN_N_TER"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0002">3D-structure</keyword>
+<keyword id="KW-0007">Acetylation</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0068">Autocatalytic cleavage</keyword>
+<keyword id="KW-0903">Direct protein sequencing</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0375">Hydrogen ion transport</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0404">Intron homing</keyword>
+<keyword id="KW-0406">Ion transport</keyword>
+<keyword id="KW-0472">Membrane</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0651">Protein splicing</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-1278">Translocase</keyword>
+<keyword id="KW-0813">Transport</keyword>
+<keyword id="KW-0926">Vacuole</keyword>
+<feature type="initiator methionine" description="Removed" evidence="6 12 22">
+<location>
+<position position="1"/>
+</location>
+</feature>
+<feature type="chain" description="V-type proton ATPase catalytic subunit A, 1st part" id="PRO_0000002458">
+<location>
+<begin position="2"/>
+<end position="283"/>
+</location>
+</feature>
+<feature type="chain" description="Endonuclease PI-SceI" id="PRO_0000002459">
+<location>
+<begin position="284"/>
+<end position="737"/>
+</location>
+</feature>
+<feature type="chain" description="V-type proton ATPase catalytic subunit A, 2nd part" id="PRO_0000002460">
+<location>
+<begin position="738"/>
+<end position="1071"/>
+</location>
+</feature>
+<feature type="domain" description="DOD-type homing endonuclease" evidence="2">
+<location>
+<begin position="494"/>
+<end position="642"/>
+</location>
+</feature>
+<feature type="nucleotide phosphate-binding region" description="ATP" evidence="1">
+<location>
+<begin position="257"/>
+<end position="264"/>
+</location>
+</feature>
+<feature type="modified residue" description="N-acetylalanine" evidence="12 22">
+<location>
+<position position="2"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphothreonine" evidence="21">
+<location>
+<position position="131"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="21">
+<location>
+<position position="858"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="21">
+<location>
+<position position="928"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Reduces splicing reaction speed. Inhibits splicing; when associated with N-362; S-737 and S-738 in X10SSS VDE." evidence="4 6 7">
+<original>C</original>
+<variation>S</variation>
+<location>
+<position position="284"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Inhibits splicing; when associated with S-284; S-737 and S-738 in X10SSS VDE." evidence="6">
+<original>H</original>
+<variation>N</variation>
+<location>
+<position position="362"/>
+</location>
+</feature>
+<feature type="mutagenesis site" description="Inhibits splicing; when associated with S-284; N-362 and S-738 in X10SSS VDE." evidence="4 6">
+<original>N</original>
+<variation>S</variation>
+<location>
+<position position="737"/>
+</location>
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+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.</title>
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+<person name="Agostoni-Carbone M.L."/>
+<person name="Albermann K."/>
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+<person name="Backes U."/>
+<person name="Barreiros T."/>
+<person name="Bertani I."/>
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+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
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+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
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+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
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+<dbReference type="DOI" id="10.1159/000084940"/>
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+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>Q12141-1</id>
+<name>Transposon Ty1-GR1 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>Q12085-1</id>
+<name>Transposon Ty1-GR1 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-GR1 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YGR027W-A ORF.</text>
+</comment>
+<dbReference type="EC" id="3.4.23.-"/>
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+<property type="protein sequence ID" value="CAA97012.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z72813">
+<property type="protein sequence ID" value="CAA97014.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006941">
+<property type="protein sequence ID" value="DAA08122.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S40969">
+<property type="entry name" value="S40969"/>
+</dbReference>
+<dbReference type="PIR" id="S69838">
+<property type="entry name" value="S69838"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058158.1">
+<molecule id="Q12141-1"/>
+<property type="nucleotide sequence ID" value="NM_001184432.2"/>
+</dbReference>
+<dbReference type="BioGRID" id="33270">
+<property type="interactions" value="9"/>
+</dbReference>
+<dbReference type="IntAct" id="Q12141">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="iPTMnet" id="Q12141"/>
+<dbReference type="MaxQB" id="Q12141"/>
+<dbReference type="PaxDb" id="Q12141"/>
+<dbReference type="PRIDE" id="Q12141"/>
+<dbReference type="GeneID" id="852913"/>
+<dbReference type="KEGG" id="sce:YGR027W-B"/>
+<dbReference type="SGD" id="S000007406">
+<property type="gene designation" value="YGR027W-B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YGR027W-B"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="Q12141"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome VII"/>
+</dbReference>
+<dbReference type="RNAct" id="Q12141">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
+<property type="term" value="F:RNA-DNA hybrid ribonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-GR1 Gag-Pol polyprotein" id="PRO_0000279053">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279054" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279055" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279056" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279057" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<sequence length="1755" mass="198658" checksum="7A1035D04E57F716" modified="1996-11-01" version="1">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIDKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQQELELEEDDYKMKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSKQVLDMTYELIQFIWNTRDKQLIWHKSKPVKPTNKLVVISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELDKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2020-12-02" version="69">
+<accession>P0CX74</accession>
+<accession>D6VWK0</accession>
+<accession>P47097</accession>
+<accession>Q66R50</accession>
+<name>YJ11A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-JR1 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-JR1</name>
+<name type="synonym">YJRWTy1-1 GAG</name>
+<name type="ordered locus">YJR026W</name>
+<name type="ORF">J1555</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="1179" last="1186">
+<title>The sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon.</title>
+<authorList>
+<person name="Zagulski M."/>
+<person name="Babinska B."/>
+<person name="Gromadka R."/>
+<person name="Migdalski A."/>
+<person name="Rytka J."/>
+<person name="Sulicka J."/>
+<person name="Herbert C.J."/>
+</authorList>
+<dbReference type="PubMed" id="8619316"/>
+<dbReference type="DOI" id="10.1002/yea.320111208"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1996" name="EMBO J." volume="15" first="2031" last="2049">
+<title>Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.</title>
+<authorList>
+<person name="Galibert F."/>
+<person name="Alexandraki D."/>
+<person name="Baur A."/>
+<person name="Boles E."/>
+<person name="Chalwatzis N."/>
+<person name="Chuat J.-C."/>
+<person name="Coster F."/>
+<person name="Cziepluch C."/>
+<person name="de Haan M."/>
+<person name="Domdey H."/>
+<person name="Durand P."/>
+<person name="Entian K.-D."/>
+<person name="Gatius M."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="Hennemann A."/>
+<person name="Herbert C.J."/>
+<person name="Heumann K."/>
+<person name="Hilger F."/>
+<person name="Hollenberg C.P."/>
+<person name="Huang M.-E."/>
+<person name="Jacq C."/>
+<person name="Jauniaux J.-C."/>
+<person name="Katsoulou C."/>
+<person name="Kirchrath L."/>
+<person name="Kleine K."/>
+<person name="Kordes E."/>
+<person name="Koetter P."/>
+<person name="Liebl S."/>
+<person name="Louis E.J."/>
+<person name="Manus V."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Obermaier B."/>
+<person name="Perea J."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rasmussen S.W."/>
+<person name="Rose M."/>
+<person name="Rossau R."/>
+<person name="Schaaff-Gerstenschlaeger I."/>
+<person name="Smits P.H.M."/>
+<person name="Scarcez T."/>
+<person name="Soriano N."/>
+<person name="To Van D."/>
+<person name="Tzermia M."/>
+<person name="Van Broekhoven A."/>
+<person name="Vandenbol M."/>
+<person name="Wedler H."/>
+<person name="von Wettstein D."/>
+<person name="Wambutt R."/>
+<person name="Zagulski M."/>
+<person name="Zollner A."/>
+<person name="Karpfinger-Hartl L."/>
+</authorList>
+<dbReference type="PubMed" id="8641269"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1996.tb00557.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0CX74-1</id>
+<name>Transposon Ty1-JR1 Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P47098-1</id>
+<name>Transposon Ty1-JR1 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-JR1 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-JR1 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="X87297">
+<property type="protein sequence ID" value="CAA60721.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z49526">
+<property type="protein sequence ID" value="CAA89552.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006943">
+<property type="protein sequence ID" value="DAA08816.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S57044">
+<property type="entry name" value="S57044"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_012561.3">
+<molecule id="P0CX74-1"/>
+<property type="nucleotide sequence ID" value="NM_001181684.3"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013673.1">
+<molecule id="P0CX74-1"/>
+<property type="nucleotide sequence ID" value="NM_001182398.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058172.1">
+<molecule id="P0CX74-1"/>
+<property type="nucleotide sequence ID" value="NM_001184407.1"/>
+</dbReference>
+<dbReference type="SMR" id="P0CX74"/>
+<dbReference type="BioGRID" id="31496">
+<property type="interactions" value="3"/>
+</dbReference>
+<dbReference type="BioGRID" id="33779">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="BioGRID" id="35130">
+<property type="interactions" value="5"/>
+</dbReference>
+<dbReference type="STRING" id="4932.YML040W"/>
+<dbReference type="iPTMnet" id="P0CX74"/>
+<dbReference type="PaxDb" id="P0CX74"/>
+<dbReference type="TopDownProteomics" id="P0CX74-1">
+<molecule id="P0CX74-1"/>
+</dbReference>
+<dbReference type="GeneID" id="850926"/>
+<dbReference type="GeneID" id="853483"/>
+<dbReference type="GeneID" id="854968"/>
+<dbReference type="KEGG" id="sce:YJR026W"/>
+<dbReference type="KEGG" id="sce:YLR227W-A"/>
+<dbReference type="KEGG" id="sce:YML040W"/>
+<dbReference type="SGD" id="S000003787">
+<property type="gene designation" value="YJR026W"/>
+</dbReference>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="InParanoid" id="P0CX74"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome X"/>
+</dbReference>
+<dbReference type="RNAct" id="P0CX74">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-JR1 Gag polyprotein" id="PRO_0000203496">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279086" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000279087" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11884596"/>
+</source>
+</evidence>
+<sequence length="440" mass="48993" checksum="ACC50DD2AC8F4781" modified="2011-06-28" version="1">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2020-12-02" version="62">
+<accession>P0CX70</accession>
+<accession>D3DM44</accession>
+<accession>Q12162</accession>
+<name>YD15A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-DR6 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-DR6</name>
+<name type="synonym">YDRWTy1-5 GAG</name>
+<name type="ordered locus">YDR365W-A</name>
+<name type="ORF">D9481.12</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="75" last="78">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
+<person name="Jacq C."/>
+<person name="Alt-Moerbe J."/>
+<person name="Andre B."/>
+<person name="Arnold W."/>
+<person name="Bahr A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Bargues M."/>
+<person name="Baron L."/>
+<person name="Becker A."/>
+<person name="Biteau N."/>
+<person name="Bloecker H."/>
+<person name="Blugeon C."/>
+<person name="Boskovic J."/>
+<person name="Brandt P."/>
+<person name="Brueckner M."/>
+<person name="Buitrago M.J."/>
+<person name="Coster F."/>
+<person name="Delaveau T."/>
+<person name="del Rey F."/>
+<person name="Dujon B."/>
+<person name="Eide L.G."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Goffeau A."/>
+<person name="Gomez-Peris A."/>
+<person name="Granotier C."/>
+<person name="Hanemann V."/>
+<person name="Hankeln T."/>
+<person name="Hoheisel J.D."/>
+<person name="Jaeger W."/>
+<person name="Jimenez A."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kraemer C."/>
+<person name="Kuester H."/>
+<person name="Laamanen P."/>
+<person name="Legros Y."/>
+<person name="Louis E.J."/>
+<person name="Moeller-Rieker S."/>
+<person name="Monnet A."/>
+<person name="Moro M."/>
+<person name="Mueller-Auer S."/>
+<person name="Nussbaumer B."/>
+<person name="Paricio N."/>
+<person name="Paulin L."/>
+<person name="Perea J."/>
+<person name="Perez-Alonso M."/>
+<person name="Perez-Ortin J.E."/>
+<person name="Pohl T.M."/>
+<person name="Prydz H."/>
+<person name="Purnelle B."/>
+<person name="Rasmussen S.W."/>
+<person name="Remacha M.A."/>
+<person name="Revuelta J.L."/>
+<person name="Rieger M."/>
+<person name="Salom D."/>
+<person name="Saluz H.P."/>
+<person name="Saiz J.E."/>
+<person name="Saren A.-M."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Schmidt E.R."/>
+<person name="Schneider C."/>
+<person name="Scholler P."/>
+<person name="Schwarz S."/>
+<person name="Soler-Mira A."/>
+<person name="Urrestarazu L.A."/>
+<person name="Verhasselt P."/>
+<person name="Vissers S."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Wagner G."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Woelfl S."/>
+<person name="Harris D.E."/>
+<person name="Bowman S."/>
+<person name="Brown D."/>
+<person name="Churcher C.M."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jones L."/>
+<person name="McDonald S."/>
+<person name="Murphy L.D."/>
+<person name="Niblett D."/>
+<person name="Odell C."/>
+<person name="Oliver K."/>
+<person name="Rajandream M.A."/>
+<person name="Richards C."/>
+<person name="Shore L."/>
+<person name="Walsh S.V."/>
+<person name="Barrell B.G."/>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
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+<person name="Johnston M."/>
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+<person name="Fulton L."/>
+<person name="Gattung S."/>
+<person name="Greco T."/>
+<person name="Hallsworth K."/>
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+<person name="Jier M."/>
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+<person name="Johnston L."/>
+<person name="Kirsten J."/>
+<person name="Kucaba T."/>
+<person name="Langston Y."/>
+<person name="Latreille P."/>
+<person name="Le T."/>
+<person name="Mardis E."/>
+<person name="Menezes S."/>
+<person name="Miller N."/>
+<person name="Nhan M."/>
+<person name="Pauley A."/>
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+<person name="Heumann K."/>
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+<person name="Zollner A."/>
+<person name="Zaccaria P."/>
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+<dbReference type="PubMed" id="9169867"/>
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+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0CX70-1</id>
+<name>Transposon Ty1-DR6 Gag polyprotein</name>
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+</isoform>
+<isoform>
+<id>P0C2I3-1</id>
+<name>Transposon Ty1-DR6 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-DR6 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-DR6 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="U28373">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
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+<property type="protein sequence ID" value="DAA12206.1"/>
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+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-DR6 Gag polyprotein" id="PRO_0000279037">
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+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
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+</evidence>
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+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2020-12-02" version="53">
+<accession>P0CX71</accession>
+<accession>D3DM44</accession>
+<accession>Q12162</accession>
+<name>YE11A_YEAST</name>
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+<fullName>Transposon Ty1-ER1 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-ER1</name>
+<name type="synonym">YERCTy1-1 GAG</name>
+<name type="ordered locus">YER137C-A</name>
+<name type="ORF">YER138C-A</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="78" last="81">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome V.</title>
+<authorList>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Hennessy K.M."/>
+<person name="Yelton M.A."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Brennan T."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Guzman E."/>
+<person name="Hartzell G."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Kayser A."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin D."/>
+<person name="Mosedale D."/>
+<person name="Nakahara K."/>
+<person name="Namath A."/>
+<person name="Norgren R."/>
+<person name="Oefner P."/>
+<person name="Oh C."/>
+<person name="Petel F.X."/>
+<person name="Roberts D."/>
+<person name="Sehl P."/>
+<person name="Schramm S."/>
+<person name="Shogren T."/>
+<person name="Smith V."/>
+<person name="Taylor P."/>
+<person name="Wei Y."/>
+<person name="Botstein D."/>
+<person name="Davis R.W."/>
+</authorList>
+<dbReference type="PubMed" id="9169868"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0CX71-1</id>
+<name>Transposon Ty1-ER1 Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>Q03612-1</id>
+<name>Transposon Ty1-ER1 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-ER1 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-ER1 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="U18917">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
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+<dbReference type="RNAct" id="P0CX71">
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+</dbReference>
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+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
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+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-ER1 Gag polyprotein" id="PRO_0000409791">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000409792" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000409793" evidence="1">
+<location>
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+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11884596"/>
+</source>
+</evidence>
+<sequence length="440" mass="48953" checksum="B3C484A9901A8296" modified="2011-06-28" version="1">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-02-10" version="110">
+<accession>Q12085</accession>
+<accession>D6VUG2</accession>
+<name>YG11A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-GR1 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-GR1</name>
+<name type="synonym">YGRWTy1-1 GAG</name>
+<name type="ordered locus">YGR027W-A</name>
+<name type="ORF">G4052</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="81" last="84">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome VII.</title>
+<authorList>
+<person name="Tettelin H."/>
+<person name="Agostoni-Carbone M.L."/>
+<person name="Albermann K."/>
+<person name="Albers M."/>
+<person name="Arroyo J."/>
+<person name="Backes U."/>
+<person name="Barreiros T."/>
+<person name="Bertani I."/>
+<person name="Bjourson A.J."/>
+<person name="Brueckner M."/>
+<person name="Bruschi C.V."/>
+<person name="Carignani G."/>
+<person name="Castagnoli L."/>
+<person name="Cerdan E."/>
+<person name="Clemente M.L."/>
+<person name="Coblenz A."/>
+<person name="Coglievina M."/>
+<person name="Coissac E."/>
+<person name="Defoor E."/>
+<person name="Del Bino S."/>
+<person name="Delius H."/>
+<person name="Delneri D."/>
+<person name="de Wergifosse P."/>
+<person name="Dujon B."/>
+<person name="Durand P."/>
+<person name="Entian K.-D."/>
+<person name="Eraso P."/>
+<person name="Escribano V."/>
+<person name="Fabiani L."/>
+<person name="Fartmann B."/>
+<person name="Feroli F."/>
+<person name="Feuermann M."/>
+<person name="Frontali L."/>
+<person name="Garcia-Gonzalez M."/>
+<person name="Garcia-Saez M.I."/>
+<person name="Goffeau A."/>
+<person name="Guerreiro P."/>
+<person name="Hani J."/>
+<person name="Hansen M."/>
+<person name="Hebling U."/>
+<person name="Hernandez K."/>
+<person name="Heumann K."/>
+<person name="Hilger F."/>
+<person name="Hofmann B."/>
+<person name="Indge K.J."/>
+<person name="James C.M."/>
+<person name="Klima R."/>
+<person name="Koetter P."/>
+<person name="Kramer B."/>
+<person name="Kramer W."/>
+<person name="Lauquin G."/>
+<person name="Leuther H."/>
+<person name="Louis E.J."/>
+<person name="Maillier E."/>
+<person name="Marconi A."/>
+<person name="Martegani E."/>
+<person name="Mazon M.J."/>
+<person name="Mazzoni C."/>
+<person name="McReynolds A.D.K."/>
+<person name="Melchioretto P."/>
+<person name="Mewes H.-W."/>
+<person name="Minenkova O."/>
+<person name="Mueller-Auer S."/>
+<person name="Nawrocki A."/>
+<person name="Netter P."/>
+<person name="Neu R."/>
+<person name="Nombela C."/>
+<person name="Oliver S.G."/>
+<person name="Panzeri L."/>
+<person name="Paoluzi S."/>
+<person name="Plevani P."/>
+<person name="Portetelle D."/>
+<person name="Portillo F."/>
+<person name="Potier S."/>
+<person name="Purnelle B."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Rinaldi T."/>
+<person name="Robben J."/>
+<person name="Rodrigues-Pousada C."/>
+<person name="Rodriguez-Belmonte E."/>
+<person name="Rodriguez-Torres A.M."/>
+<person name="Rose M."/>
+<person name="Ruzzi M."/>
+<person name="Saliola M."/>
+<person name="Sanchez-Perez M."/>
+<person name="Schaefer B."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Schmidheini T."/>
+<person name="Schreer A."/>
+<person name="Skala J."/>
+<person name="Souciet J.-L."/>
+<person name="Steensma H.Y."/>
+<person name="Talla E."/>
+<person name="Thierry A."/>
+<person name="Vandenbol M."/>
+<person name="van der Aart Q.J.M."/>
+<person name="Van Dyck L."/>
+<person name="Vanoni M."/>
+<person name="Verhasselt P."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Wambutt R."/>
+<person name="Watson M.D."/>
+<person name="Weber N."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Wipfli P."/>
+<person name="Wolf K."/>
+<person name="Wright L.F."/>
+<person name="Zaccaria P."/>
+<person name="Zimmermann M."/>
+<person name="Zollner A."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="9169869"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>Q12085-1</id>
+<name>Transposon Ty1-GR1 Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>Q12141-1</id>
+<name>Transposon Ty1-GR1 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-GR1 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-GR1 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="Z72812">
+<property type="protein sequence ID" value="CAA97011.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z72813">
+<property type="protein sequence ID" value="CAA97013.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006941">
+<property type="protein sequence ID" value="DAA08123.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69837">
+<property type="entry name" value="S69837"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058159.1">
+<molecule id="Q12085-1"/>
+<property type="nucleotide sequence ID" value="NM_001184431.1"/>
+</dbReference>
+<dbReference type="SMR" id="Q12085"/>
+<dbReference type="BioGRID" id="33269">
+<property type="interactions" value="8"/>
+</dbReference>
+<dbReference type="STRING" id="4932.YGR027W-A"/>
+<dbReference type="iPTMnet" id="Q12085"/>
+<dbReference type="PaxDb" id="Q12085"/>
+<dbReference type="GeneID" id="852912"/>
+<dbReference type="KEGG" id="sce:YGR027W-A"/>
+<dbReference type="SGD" id="S000007405">
+<property type="gene designation" value="YGR027W-A"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YGR027W-A"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="InParanoid" id="Q12085"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome VII"/>
+</dbReference>
+<dbReference type="RNAct" id="Q12085">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-GR1 Gag polyprotein" id="PRO_0000279058">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279059" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000279060" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
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+<position position="416"/>
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+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
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+</source>
+</evidence>
+<sequence length="440" mass="49056" checksum="86A92FDF1337BB0D" modified="1996-11-01" version="1">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQTAQSHSPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2010-04-20" modified="2021-04-07" version="48">
+<accession>P0CF21</accession>
+<accession>P17324</accession>
+<accession>P40443</accession>
+<accession>P40444</accession>
+<accession>Q6Q579</accession>
+<name>YI168_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Putative truncated L-serine dehydratase YIL168W</fullName>
+<ecNumber>4.3.1.17</ecNumber>
+</recommendedName>
+</protein>
+<gene>
+<name type="ordered locus">YIL168W</name>
+<name type="ORF">YI9402.08A</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="84" last="87">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.</title>
+<authorList>
+<person name="Churcher C.M."/>
+<person name="Bowman S."/>
+<person name="Badcock K."/>
+<person name="Bankier A.T."/>
+<person name="Brown D."/>
+<person name="Chillingworth T."/>
+<person name="Connor R."/>
+<person name="Devlin K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Harris D.E."/>
+<person name="Horsnell T."/>
+<person name="Hunt S."/>
+<person name="Jagels K."/>
+<person name="Jones M."/>
+<person name="Lye G."/>
+<person name="Moule S."/>
+<person name="Odell C."/>
+<person name="Pearson D."/>
+<person name="Rajandream M.A."/>
+<person name="Rice P."/>
+<person name="Rowley N."/>
+<person name="Skelton J."/>
+<person name="Smith V."/>
+<person name="Walsh S.V."/>
+<person name="Whitehead S."/>
+<person name="Barrell B.G."/>
+</authorList>
+<dbReference type="PubMed" id="9169870"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
+<person name="Rolfs A."/>
+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
+<person name="Zhu C."/>
+<person name="Berger M.F."/>
+<person name="Camargo A.A."/>
+<person name="Kelley F."/>
+<person name="McCarron S."/>
+<person name="Jepson D."/>
+<person name="Richardson A."/>
+<person name="Raphael J."/>
+<person name="Moreira D."/>
+<person name="Taycher E."/>
+<person name="Zuo D."/>
+<person name="Mohr S."/>
+<person name="Kane M.F."/>
+<person name="Williamson J."/>
+<person name="Simpson A.J.G."/>
+<person name="Bulyk M.L."/>
+<person name="Harlow E."/>
+<person name="Marsischky G."/>
+<person name="Kolodner R.D."/>
+<person name="LaBaer J."/>
+</authorList>
+<dbReference type="PubMed" id="17322287"/>
+<dbReference type="DOI" id="10.1101/gr.6037607"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<comment type="catalytic activity">
+<reaction>
+<text>L-serine = NH4(+) + pyruvate</text>
+<dbReference type="Rhea" id="RHEA:19169"/>
+<dbReference type="ChEBI" id="CHEBI:15361"/>
+<dbReference type="ChEBI" id="CHEBI:28938"/>
+<dbReference type="ChEBI" id="CHEBI:33384"/>
+<dbReference type="EC" id="4.3.1.17"/>
+</reaction>
+</comment>
+<comment type="cofactor">
+<cofactor evidence="1">
+<name>pyridoxal 5'-phosphate</name>
+<dbReference type="ChEBI" id="CHEBI:597326"/>
+</cofactor>
+</comment>
+<comment type="pathway">
+<text>Carbohydrate biosynthesis; gluconeogenesis.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="similarity">
+<text evidence="2">Belongs to the serine/threonine dehydratase family.</text>
+</comment>
+<comment type="caution">
+<text evidence="3">Could be the product of a pseudogene unlikely to encode a functional protein. This is a truncated version of L-serine dehydratase. Strain S288c has a stop codon in position 128, which disrupts the gene coding for this protein and produces two ORFs YIL167W and YIL168W. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set. A contiguous sequence for L-serine dehydratase can be found in other strain backgrounds (AC P0CF23).</text>
+</comment>
+<dbReference type="EC" id="4.3.1.17"/>
+<dbReference type="EMBL" id="Z46921">
+<property type="protein sequence ID" value="CAA87024.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY558344">
+<property type="protein sequence ID" value="AAS56670.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S12731">
+<property type="entry name" value="S12731"/>
+</dbReference>
+<dbReference type="SMR" id="P0CF21"/>
+<dbReference type="PRIDE" id="P0CF21"/>
+<dbReference type="SGD" id="S000001430">
+<property type="gene designation" value="YIL168W"/>
+</dbReference>
+<dbReference type="InParanoid" id="P0CF21"/>
+<dbReference type="UniPathway" id="UPA00138"/>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003941">
+<property type="term" value="F:L-serine ammonia-lyase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0030170">
+<property type="term" value="F:pyridoxal phosphate binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="InterPro"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006520">
+<property type="term" value="P:cellular amino acid metabolic process"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="InterPro"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006094">
+<property type="term" value="P:gluconeogenesis"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-UniPathway"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.40.50.1100">
+<property type="match status" value="2"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001926">
+<property type="entry name" value="PLP-dep"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR000634">
+<property type="entry name" value="Ser/Thr_deHydtase_PyrdxlP-BS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036052">
+<property type="entry name" value="Trypto_synt_PLP_dependent"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00291">
+<property type="entry name" value="PALP"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53686">
+<property type="entry name" value="SSF53686"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00165">
+<property type="entry name" value="DEHYDRATASE_SER_THR"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="uncertain"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0312">Gluconeogenesis</keyword>
+<keyword id="KW-0456">Lyase</keyword>
+<keyword id="KW-0663">Pyridoxal phosphate</keyword>
+<feature type="chain" description="Putative truncated L-serine dehydratase YIL168W" id="PRO_0000393393">
+<location>
+<begin position="1"/>
+<end position="127"/>
+</location>
+</feature>
+<feature type="modified residue" description="N6-(pyridoxal phosphate)lysine" evidence="1">
+<location>
+<position position="39"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000305"/>
+<evidence key="3" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="24374639"/>
+</source>
+</evidence>
+<sequence length="127" mass="13943" checksum="3943C545FFE8B54C" modified="2010-04-20" version="1">MEMTYYEKTPLIRQFLNNGKTNSWFYVKHEMLQPGGSFKSRGIGHLIRKSNEEALSEGSGKLAVFSSSGGNAGLAAATACRSMALNCSVVVPKTTKPRMVKKIQSAGAKVIIHGDHWGEADEYLRHE</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2020-12-02" version="56">
+<accession>P0CX72</accession>
+<accession>D3DM44</accession>
+<accession>Q12162</accession>
+<name>YL12A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-LR2 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-LR2</name>
+<name type="synonym">YLRCTy1-2 GAG</name>
+<name type="ordered locus">YLR157C-A</name>
+<name type="ORF">L9632.7</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Louis E.J."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Scholler P."/>
+<person name="Schwager C."/>
+<person name="Schwarz S."/>
+<person name="Underwood A.P."/>
+<person name="Urrestarazu L.A."/>
+<person name="Vandenbol M."/>
+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
+<person name="Zollner A."/>
+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0CX72-1</id>
+<name>Transposon Ty1-LR2 Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0C2I5-1</id>
+<name>Transposon Ty1-LR2 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-LR2 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-LR2 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="U51921">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09475.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S53553">
+<property type="entry name" value="S53553"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058153.3">
+<molecule id="P0CX72-1"/>
+<property type="nucleotide sequence ID" value="NM_001184426.3"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058155.1">
+<molecule id="P0CX72-1"/>
+<property type="nucleotide sequence ID" value="NM_001184428.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058170.1">
+<molecule id="P0CX72-1"/>
+<property type="nucleotide sequence ID" value="NM_001184405.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058190.1">
+<molecule id="P0CX72-1"/>
+<property type="nucleotide sequence ID" value="NM_001184391.1"/>
+</dbReference>
+<dbReference type="SMR" id="P0CX72"/>
+<dbReference type="BioGRID" id="31430">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="BioGRID" id="32423">
+<property type="interactions" value="5"/>
+</dbReference>
+<dbReference type="BioGRID" id="35904">
+<property type="interactions" value="19"/>
+</dbReference>
+<dbReference type="BioGRID" id="36886">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="iPTMnet" id="P0CX72"/>
+<dbReference type="GeneID" id="850854"/>
+<dbReference type="GeneID" id="851970"/>
+<dbReference type="GeneID" id="855816"/>
+<dbReference type="GeneID" id="856880"/>
+<dbReference type="KEGG" id="sce:YDR365W-A"/>
+<dbReference type="KEGG" id="sce:YER137C-A"/>
+<dbReference type="KEGG" id="sce:YLR157C-A"/>
+<dbReference type="KEGG" id="sce:YPL257W-A"/>
+<dbReference type="SGD" id="S000007373">
+<property type="gene designation" value="YLR157C-A"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XII"/>
+</dbReference>
+<dbReference type="RNAct" id="P0CX72">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-LR2 Gag polyprotein" id="PRO_0000409794">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000409795" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000409796" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11884596"/>
+</source>
+</evidence>
+<sequence length="440" mass="48953" checksum="B3C484A9901A8296" modified="2011-06-28" version="1">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="114">
+<accession>P0C2I6</accession>
+<accession>D6VYM8</accession>
+<name>YL13B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-LR3 Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<shortName>RT-RH</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-LR3</name>
+<name type="synonym">YLRWTy1-3 POL</name>
+<name type="ordered locus">YLR227W-B</name>
+<name type="ORF">L8083.11</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Louis E.J."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Scholler P."/>
+<person name="Schwager C."/>
+<person name="Schwarz S."/>
+<person name="Underwood A.P."/>
+<person name="Urrestarazu L.A."/>
+<person name="Vandenbol M."/>
+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
+<person name="Zollner A."/>
+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0C2I6-1</id>
+<name>Transposon Ty1-LR3 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0CX75-1</id>
+<name>Transposon Ty1-LR3 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-LR3 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YLR227W-A ORF.</text>
+</comment>
+<dbReference type="EC" id="3.4.23.-"/>
+<dbReference type="EC" id="2.7.7.49"/>
+<dbReference type="EC" id="2.7.7.7"/>
+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="U19027">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09544.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69963">
+<property type="entry name" value="S69963"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058171.1">
+<molecule id="P0C2I6-1"/>
+<property type="nucleotide sequence ID" value="NM_001184408.2"/>
+</dbReference>
+<dbReference type="BioGRID" id="31497">
+<property type="interactions" value="7"/>
+</dbReference>
+<dbReference type="iPTMnet" id="P0C2I6"/>
+<dbReference type="PaxDb" id="P0C2I6"/>
+<dbReference type="PRIDE" id="P0C2I6"/>
+<dbReference type="GeneID" id="850927"/>
+<dbReference type="KEGG" id="sce:YLR227W-B"/>
+<dbReference type="SGD" id="S000007376">
+<property type="gene designation" value="YLR227W-B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YLR227W-B"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="P0C2I6"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XII"/>
+</dbReference>
+<dbReference type="RNAct" id="P0C2I6">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
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+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-LR3 Gag-Pol polyprotein" id="PRO_0000279104">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279105" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279106" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279107" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279108" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="829"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<sequence length="1755" mass="198405" checksum="7F70DDBF158564C0" modified="2007-03-06" version="1">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSASQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKPISEINLRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSNNETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDPPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAAKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMNTWDTDKYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="86">
+<accession>P0C2I8</accession>
+<accession>D6VYQ3</accession>
+<name>YL14A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-LR4 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-LR4</name>
+<name type="synonym">YLRWTy1-4 GAG</name>
+<name type="ordered locus">YLR256W-A</name>
+<name type="ORF">L9672.1</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Louis E.J."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Scholler P."/>
+<person name="Schwager C."/>
+<person name="Schwarz S."/>
+<person name="Underwood A.P."/>
+<person name="Urrestarazu L.A."/>
+<person name="Vandenbol M."/>
+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
+<person name="Zollner A."/>
+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0C2I8-1</id>
+<name>Transposon Ty1-LR4 Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0C2I7-1</id>
+<name>Transposon Ty1-LR4 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-LR4 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-LR4 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="U20865">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09569.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69964">
+<property type="entry name" value="S69964"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058173.1">
+<molecule id="P0C2I8-1"/>
+<property type="nucleotide sequence ID" value="NM_001184409.1"/>
+</dbReference>
+<dbReference type="SMR" id="P0C2I8"/>
+<dbReference type="BioGRID" id="31523">
+<property type="interactions" value="4"/>
+</dbReference>
+<dbReference type="IntAct" id="P0C2I8">
+<property type="interactions" value="3"/>
+</dbReference>
+<dbReference type="MINT" id="P0C2I8"/>
+<dbReference type="STRING" id="4932.YLR256W-A"/>
+<dbReference type="iPTMnet" id="P0C2I8"/>
+<dbReference type="PaxDb" id="P0C2I8"/>
+<dbReference type="PRIDE" id="P0C2I8"/>
+<dbReference type="GeneID" id="850959"/>
+<dbReference type="KEGG" id="sce:YLR256W-A"/>
+<dbReference type="SGD" id="S000007377">
+<property type="gene designation" value="YLR256W-A"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YLR256W-A"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="OMA" id="SHKANNI"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XII"/>
+</dbReference>
+<dbReference type="RNAct" id="P0C2I8">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-LR4 Gag polyprotein" id="PRO_0000279114">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279115" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000279116" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
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+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
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+</source>
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+<sequence length="440" mass="49003" checksum="4124EDE383E8D539" modified="2007-03-06" version="1">MESQQLSQHPHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1994-06-01" modified="2020-02-26" version="80">
+<accession>P36072</accession>
+<name>YKL8_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Putative uncharacterized protein YKL118W</fullName>
+</recommendedName>
+</protein>
+<gene>
+<name type="ordered locus">YKL118W</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1992" name="Yeast" volume="8" first="121" last="132">
+<title>Sequence of a 10.7 kb segment of yeast chromosome XI identifies the APN1 and the BAF1 loci and reveals one tRNA gene and several new open reading frames including homologs to RAD2 and kinases.</title>
+<authorList>
+<person name="Jacquier A."/>
+<person name="Legrain P."/>
+<person name="Dujon B."/>
+</authorList>
+<dbReference type="PubMed" id="1561835"/>
+<dbReference type="DOI" id="10.1002/yea.320080207"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1994" name="Nature" volume="369" first="371" last="378">
+<title>Complete DNA sequence of yeast chromosome XI.</title>
+<authorList>
+<person name="Dujon B."/>
+<person name="Alexandraki D."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Baladron V."/>
+<person name="Ballesta J.P.G."/>
+<person name="Banrevi A."/>
+<person name="Bolle P.-A."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Bossier P."/>
+<person name="Bou G."/>
+<person name="Boyer J."/>
+<person name="Buitrago M.J."/>
+<person name="Cheret G."/>
+<person name="Colleaux L."/>
+<person name="Daignan-Fornier B."/>
+<person name="del Rey F."/>
+<person name="Dion C."/>
+<person name="Domdey H."/>
+<person name="Duesterhoeft A."/>
+<person name="Duesterhus S."/>
+<person name="Entian K.-D."/>
+<person name="Erfle H."/>
+<person name="Esteban P.F."/>
+<person name="Feldmann H."/>
+<person name="Fernandes L."/>
+<person name="Fobo G.M."/>
+<person name="Fritz C."/>
+<person name="Fukuhara H."/>
+<person name="Gabel C."/>
+<person name="Gaillon L."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Garcia-Ramirez J.J."/>
+<person name="Gent M.E."/>
+<person name="Ghazvini M."/>
+<person name="Goffeau A."/>
+<person name="Gonzalez A."/>
+<person name="Grothues D."/>
+<person name="Guerreiro P."/>
+<person name="Hegemann J.H."/>
+<person name="Hewitt N."/>
+<person name="Hilger F."/>
+<person name="Hollenberg C.P."/>
+<person name="Horaitis O."/>
+<person name="Indge K.J."/>
+<person name="Jacquier A."/>
+<person name="James C.M."/>
+<person name="Jauniaux J.-C."/>
+<person name="Jimenez A."/>
+<person name="Keuchel H."/>
+<person name="Kirchrath L."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Legrain P."/>
+<person name="Liebl S."/>
+<person name="Louis E.J."/>
+<person name="Maia e Silva A."/>
+<person name="Marck C."/>
+<person name="Monnier A.-L."/>
+<person name="Moestl D."/>
+<person name="Mueller S."/>
+<person name="Obermaier B."/>
+<person name="Oliver S.G."/>
+<person name="Pallier C."/>
+<person name="Pascolo S."/>
+<person name="Pfeiffer F."/>
+<person name="Philippsen P."/>
+<person name="Planta R.J."/>
+<person name="Pohl F.M."/>
+<person name="Pohl T.M."/>
+<person name="Poehlmann R."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Puzos V."/>
+<person name="Ramezani Rad M."/>
+<person name="Rasmussen S.W."/>
+<person name="Remacha M.A."/>
+<person name="Revuelta J.L."/>
+<person name="Richard G.-F."/>
+<person name="Rieger M."/>
+<person name="Rodrigues-Pousada C."/>
+<person name="Rose M."/>
+<person name="Rupp T."/>
+<person name="Santos M.A."/>
+<person name="Schwager C."/>
+<person name="Sensen C."/>
+<person name="Skala J."/>
+<person name="Soares H."/>
+<person name="Sor F."/>
+<person name="Stegemann J."/>
+<person name="Tettelin H."/>
+<person name="Thierry A."/>
+<person name="Tzermia M."/>
+<person name="Urrestarazu L.A."/>
+<person name="van Dyck L."/>
+<person name="van Vliet-Reedijk J.C."/>
+<person name="Valens M."/>
+<person name="Vandenbol M."/>
+<person name="Vilela C."/>
+<person name="Vissers S."/>
+<person name="von Wettstein D."/>
+<person name="Voss H."/>
+<person name="Wiemann S."/>
+<person name="Xu G."/>
+<person name="Zimmermann J."/>
+<person name="Haasemann M."/>
+<person name="Becker I."/>
+<person name="Mewes H.-W."/>
+</authorList>
+<dbReference type="PubMed" id="8196765"/>
+<dbReference type="DOI" id="10.1038/369371a0"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
+<person name="Rolfs A."/>
+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
+<person name="Zhu C."/>
+<person name="Berger M.F."/>
+<person name="Camargo A.A."/>
+<person name="Kelley F."/>
+<person name="McCarron S."/>
+<person name="Jepson D."/>
+<person name="Richardson A."/>
+<person name="Raphael J."/>
+<person name="Moreira D."/>
+<person name="Taycher E."/>
+<person name="Zuo D."/>
+<person name="Mohr S."/>
+<person name="Kane M.F."/>
+<person name="Williamson J."/>
+<person name="Simpson A.J.G."/>
+<person name="Bulyk M.L."/>
+<person name="Harlow E."/>
+<person name="Marsischky G."/>
+<person name="Kolodner R.D."/>
+<person name="LaBaer J."/>
+</authorList>
+<dbReference type="PubMed" id="17322287"/>
+<dbReference type="DOI" id="10.1101/gr.6037607"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<comment type="miscellaneous">
+<text evidence="1">Partially overlaps VPH2.</text>
+</comment>
+<comment type="caution">
+<text evidence="2">Product of a dubious gene prediction unlikely to encode a functional protein. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.</text>
+</comment>
+<dbReference type="EMBL" id="S93804">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z28118">
+<property type="protein sequence ID" value="CAA81959.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z28117">
+<property type="protein sequence ID" value="CAA81958.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY693342">
+<property type="protein sequence ID" value="AAT93361.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S37946">
+<property type="entry name" value="S37946"/>
+</dbReference>
+<dbReference type="SMR" id="P36072"/>
+<dbReference type="STRING" id="4932.YKL118W"/>
+<dbReference type="PaxDb" id="P36072"/>
+<dbReference type="EnsemblFungi" id="YKL118W_mRNA">
+<property type="protein sequence ID" value="YKL118W"/>
+<property type="gene ID" value="YKL118W"/>
+</dbReference>
+<dbReference type="SGD" id="S000001601">
+<property type="gene designation" value="YKL118W"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_2265808_0_0_1"/>
+<proteinExistence type="uncertain"/>
+<feature type="chain" description="Putative uncharacterized protein YKL118W" id="PRO_0000203155">
+<location>
+<begin position="1"/>
+<end position="103"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000305"/>
+<evidence key="2" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="24374639"/>
+</source>
+</evidence>
+<sequence length="103" mass="11761" checksum="FC0AA42E6E9C18EF" modified="1994-06-01" version="1">MSSSIPSFDFALFLNFRRNSVILSFSLISNIRVLLCDANRQLSYLTFSSFLSAFSCEICFIFASSFLILNIHTSVMSTLSQLNTQDFCKTEYFVNNIIVRIQS</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="108">
+<accession>P0C2I5</accession>
+<accession>D6VYF8</accession>
+<name>YL12B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-LR2 Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-LR2</name>
+<name type="synonym">YLRCTy1-2 POL</name>
+<name type="ordered locus">YLR157C-B</name>
+<name type="ORF">L9632.7</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Louis E.J."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Scholler P."/>
+<person name="Schwager C."/>
+<person name="Schwarz S."/>
+<person name="Underwood A.P."/>
+<person name="Urrestarazu L.A."/>
+<person name="Vandenbol M."/>
+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
+<person name="Zollner A."/>
+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0C2I5-1</id>
+<name>Transposon Ty1-LR2 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0CX72-1</id>
+<name>Transposon Ty1-LR2 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-LR2 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YLR157C-A ORF.</text>
+</comment>
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+<dbReference type="EC" id="2.7.7.7"/>
+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="U51921">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09474.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69960">
+<property type="entry name" value="S69960"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058169.1">
+<molecule id="P0C2I5-1"/>
+<property type="nucleotide sequence ID" value="NM_001184406.2"/>
+</dbReference>
+<dbReference type="BioGRID" id="31429">
+<property type="interactions" value="8"/>
+</dbReference>
+<dbReference type="IntAct" id="P0C2I5">
+<property type="interactions" value="10"/>
+</dbReference>
+<dbReference type="iPTMnet" id="P0C2I5"/>
+<dbReference type="PaxDb" id="P0C2I5"/>
+<dbReference type="PRIDE" id="P0C2I5"/>
+<dbReference type="GeneID" id="850853"/>
+<dbReference type="KEGG" id="sce:YLR157C-B"/>
+<dbReference type="SGD" id="S000007374">
+<property type="gene designation" value="YLR157C-B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YLR157C-B"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="P0C2I5"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XII"/>
+</dbReference>
+<dbReference type="RNAct" id="P0C2I5">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
+<property type="term" value="F:RNA-DNA hybrid ribonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-LR2 Gag-Pol polyprotein" id="PRO_0000279099">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279100" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279101" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279102" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279103" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<sequence length="1755" mass="198545" checksum="2916CADCA298D8A7" modified="2007-03-06" version="1">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAPTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2020-12-02" version="54">
+<accession>P0CX73</accession>
+<accession>D3DM44</accession>
+<accession>Q12162</accession>
+<name>YP11A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-PL Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-PL</name>
+<name type="synonym">YPLWTy1-1 GAG</name>
+<name type="ordered locus">YPL257W-A</name>
+<name type="ORF">P0725</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
+<person name="Albermann K."/>
+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
+<person name="Brueckner M."/>
+<person name="Carpenter J."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Churcher C.M."/>
+<person name="Coster F."/>
+<person name="Davis K."/>
+<person name="Davis R.W."/>
+<person name="Dietrich F.S."/>
+<person name="Delius H."/>
+<person name="DiPaolo T."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Duncan M."/>
+<person name="Floeth M."/>
+<person name="Fortin N."/>
+<person name="Friesen J.D."/>
+<person name="Fritz C."/>
+<person name="Goffeau A."/>
+<person name="Hall J."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Hilbert H."/>
+<person name="Hillier L.W."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Johnston M."/>
+<person name="Kalman S."/>
+<person name="Kleine K."/>
+<person name="Komp C."/>
+<person name="Kurdi O."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin A."/>
+<person name="Lin D."/>
+<person name="Louis E.J."/>
+<person name="Marathe R."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
+<person name="Nentwich U."/>
+<person name="Oefner P."/>
+<person name="Pearson D."/>
+<person name="Petel F.X."/>
+<person name="Pohl T.M."/>
+<person name="Purnelle B."/>
+<person name="Rajandream M.A."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Roberts D."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
+<person name="Ushinsky S."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Voss H."/>
+<person name="Walsh S.V."/>
+<person name="Wambutt R."/>
+<person name="Wang Y."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Winnett E."/>
+<person name="Zhong W.-W."/>
+<person name="Zollner A."/>
+<person name="Vo D.H."/>
+<person name="Hani J."/>
+</authorList>
+<dbReference type="PubMed" id="9169875"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0CX73-1</id>
+<name>Transposon Ty1-PL Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>Q12414-1</id>
+<name>Transposon Ty1-PL Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-PL is a highly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-PL Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="Z73613">
+<property type="protein sequence ID" value="CAA97983.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z73614">
+<property type="protein sequence ID" value="CAA97987.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11179.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S53553">
+<property type="entry name" value="S53553"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058153.3">
+<molecule id="P0CX73-1"/>
+<property type="nucleotide sequence ID" value="NM_001184426.3"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058155.1">
+<molecule id="P0CX73-1"/>
+<property type="nucleotide sequence ID" value="NM_001184428.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058170.1">
+<molecule id="P0CX73-1"/>
+<property type="nucleotide sequence ID" value="NM_001184405.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058190.1">
+<molecule id="P0CX73-1"/>
+<property type="nucleotide sequence ID" value="NM_001184391.1"/>
+</dbReference>
+<dbReference type="SMR" id="P0CX73"/>
+<dbReference type="BioGRID" id="31430">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="BioGRID" id="32423">
+<property type="interactions" value="5"/>
+</dbReference>
+<dbReference type="BioGRID" id="35904">
+<property type="interactions" value="19"/>
+</dbReference>
+<dbReference type="BioGRID" id="36886">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="IntAct" id="P0CX73">
+<property type="interactions" value="1"/>
+</dbReference>
+<dbReference type="iPTMnet" id="P0CX73"/>
+<dbReference type="GeneID" id="850854"/>
+<dbReference type="GeneID" id="851970"/>
+<dbReference type="GeneID" id="855816"/>
+<dbReference type="GeneID" id="856880"/>
+<dbReference type="KEGG" id="sce:YDR365W-A"/>
+<dbReference type="KEGG" id="sce:YER137C-A"/>
+<dbReference type="KEGG" id="sce:YLR157C-A"/>
+<dbReference type="KEGG" id="sce:YPL257W-A"/>
+<dbReference type="SGD" id="S000007357">
+<property type="gene designation" value="YPL257W-A"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="InParanoid" id="P0CX73"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XVI"/>
+</dbReference>
+<dbReference type="RNAct" id="P0CX73">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-PL Gag polyprotein" id="PRO_0000409797">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000409798" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000409799" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11884596"/>
+</source>
+</evidence>
+<sequence length="440" mass="48953" checksum="B3C484A9901A8296" modified="2011-06-28" version="1">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-02-10" version="149">
+<accession>Q12273</accession>
+<accession>D6W1W3</accession>
+<name>YO11B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-OL Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<shortName>RT-RH</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-OL</name>
+<name type="synonym">YOLWTy1-1 POL</name>
+<name type="ordered locus">YOL103W-B</name>
+<name type="ORF">O0770</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="1069" last="1075">
+<title>Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.</title>
+<authorList>
+<person name="Vandenbol M."/>
+<person name="Durand P."/>
+<person name="Portetelle D."/>
+<person name="Hilger F."/>
+</authorList>
+<dbReference type="PubMed" id="7502582"/>
+<dbReference type="DOI" id="10.1002/yea.320111108"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="98" last="102">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.</title>
+<authorList>
+<person name="Dujon B."/>
+<person name="Albermann K."/>
+<person name="Aldea M."/>
+<person name="Alexandraki D."/>
+<person name="Ansorge W."/>
+<person name="Arino J."/>
+<person name="Benes V."/>
+<person name="Bohn C."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Bordonne R."/>
+<person name="Boyer J."/>
+<person name="Camasses A."/>
+<person name="Casamayor A."/>
+<person name="Casas C."/>
+<person name="Cheret G."/>
+<person name="Cziepluch C."/>
+<person name="Daignan-Fornier B."/>
+<person name="Dang V.-D."/>
+<person name="de Haan M."/>
+<person name="Delius H."/>
+<person name="Durand P."/>
+<person name="Fairhead C."/>
+<person name="Feldmann H."/>
+<person name="Gaillon L."/>
+<person name="Galisson F."/>
+<person name="Gamo F.-J."/>
+<person name="Gancedo C."/>
+<person name="Goffeau A."/>
+<person name="Goulding S.E."/>
+<person name="Grivell L.A."/>
+<person name="Habbig B."/>
+<person name="Hand N.J."/>
+<person name="Hani J."/>
+<person name="Hattenhorst U."/>
+<person name="Hebling U."/>
+<person name="Hernando Y."/>
+<person name="Herrero E."/>
+<person name="Heumann K."/>
+<person name="Hiesel R."/>
+<person name="Hilger F."/>
+<person name="Hofmann B."/>
+<person name="Hollenberg C.P."/>
+<person name="Hughes B."/>
+<person name="Jauniaux J.-C."/>
+<person name="Kalogeropoulos A."/>
+<person name="Katsoulou C."/>
+<person name="Kordes E."/>
+<person name="Lafuente M.J."/>
+<person name="Landt O."/>
+<person name="Louis E.J."/>
+<person name="Maarse A.C."/>
+<person name="Madania A."/>
+<person name="Mannhaupt G."/>
+<person name="Marck C."/>
+<person name="Martin R.P."/>
+<person name="Mewes H.-W."/>
+<person name="Michaux G."/>
+<person name="Paces V."/>
+<person name="Parle-McDermott A.G."/>
+<person name="Pearson B.M."/>
+<person name="Perrin A."/>
+<person name="Pettersson B."/>
+<person name="Poch O."/>
+<person name="Pohl T.M."/>
+<person name="Poirey R."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rechmann S."/>
+<person name="Schwager C."/>
+<person name="Schweizer M."/>
+<person name="Sor F."/>
+<person name="Sterky F."/>
+<person name="Tarassov I.A."/>
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+<person name="Tettelin H."/>
+<person name="Thierry A."/>
+<person name="Tobiasch E."/>
+<person name="Tzermia M."/>
+<person name="Uhlen M."/>
+<person name="Unseld M."/>
+<person name="Valens M."/>
+<person name="Vandenbol M."/>
+<person name="Vetter I."/>
+<person name="Vlcek C."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler H."/>
+<person name="Wiemann S."/>
+<person name="Winsor B."/>
+<person name="Wolfe K.H."/>
+<person name="Zollner A."/>
+<person name="Zumstein E."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="9169874"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>Q12273-1</id>
+<name>Transposon Ty1-OL Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>Q92392-1</id>
+<name>Transposon Ty1-OL Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-OL Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YOL103W-A ORF.</text>
+</comment>
+<comment type="sequence caution" evidence="5">
+<conflict type="erroneous gene model prediction">
+<sequence resource="EMBL-CDS" id="CAA88158" version="1"/>
+</conflict>
+</comment>
+<dbReference type="EC" id="3.4.23.-"/>
+<dbReference type="EC" id="2.7.7.49"/>
+<dbReference type="EC" id="2.7.7.7"/>
+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="Z48149">
+<property type="protein sequence ID" value="CAA88158.1"/>
+<property type="status" value="ALT_SEQ"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z74845">
+<property type="protein sequence ID" value="CAA99118.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z74846">
+<property type="protein sequence ID" value="CAA99122.1"/>
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+</dbReference>
+<dbReference type="EMBL" id="BK006948">
+<property type="protein sequence ID" value="DAA10679.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69975">
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+</dbReference>
+<dbReference type="RefSeq" id="NP_058181.1">
+<molecule id="Q12273-1"/>
+<property type="nucleotide sequence ID" value="NM_001184384.2"/>
+</dbReference>
+<dbReference type="SMR" id="Q12273"/>
+<dbReference type="BioGRID" id="34299">
+<property type="interactions" value="5"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-8936N"/>
+<dbReference type="IntAct" id="Q12273">
+<property type="interactions" value="1"/>
+</dbReference>
+<dbReference type="STRING" id="4932.YOL103W-B"/>
+<dbReference type="iPTMnet" id="Q12273"/>
+<dbReference type="PaxDb" id="Q12273"/>
+<dbReference type="PRIDE" id="Q12273"/>
+<dbReference type="GeneID" id="854049"/>
+<dbReference type="KEGG" id="sce:YOL103W-B"/>
+<dbReference type="SGD" id="S000007350">
+<property type="gene designation" value="YOL103W-B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YOL103W-B"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="Q12273"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XV"/>
+</dbReference>
+<dbReference type="RNAct" id="Q12273">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
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+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
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+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
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+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
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+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
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+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-OL Gag-Pol polyprotein" id="PRO_0000279153">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279154" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279155" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279156" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279157" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000305"/>
+<sequence length="1755" mass="198614" checksum="64062136832619DE" modified="1996-11-01" version="1">MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="160">
+<accession>Q03612</accession>
+<accession>D3DM43</accession>
+<name>YE11B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-ER1 Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-ER1</name>
+<name type="synonym">YERCTy1-1 POL</name>
+<name type="ordered locus">YER138C</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="78" last="81">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome V.</title>
+<authorList>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Hennessy K.M."/>
+<person name="Yelton M.A."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Brennan T."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Guzman E."/>
+<person name="Hartzell G."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Kayser A."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin D."/>
+<person name="Mosedale D."/>
+<person name="Nakahara K."/>
+<person name="Namath A."/>
+<person name="Norgren R."/>
+<person name="Oefner P."/>
+<person name="Oh C."/>
+<person name="Petel F.X."/>
+<person name="Roberts D."/>
+<person name="Sehl P."/>
+<person name="Schramm S."/>
+<person name="Shogren T."/>
+<person name="Smith V."/>
+<person name="Taylor P."/>
+<person name="Wei Y."/>
+<person name="Botstein D."/>
+<person name="Davis R.W."/>
+</authorList>
+<dbReference type="PubMed" id="9169868"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>Q03612-1</id>
+<name>Transposon Ty1-ER1 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0CX71-1</id>
+<name>Transposon Ty1-ER1 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-ER1 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YER137C-A ORF.</text>
+</comment>
+<dbReference type="EC" id="3.4.23.-"/>
+<dbReference type="EC" id="2.7.7.49"/>
+<dbReference type="EC" id="2.7.7.7"/>
+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="U18917">
+<property type="protein sequence ID" value="AAB64665.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006939">
+<property type="protein sequence ID" value="DAA07797.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S50641">
+<property type="entry name" value="S50641"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_011064.3">
+<molecule id="Q03612-1"/>
+<property type="nucleotide sequence ID" value="NM_001179028.4"/>
+</dbReference>
+<dbReference type="BioGRID" id="36885">
+<property type="interactions" value="17"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-8790N"/>
+<dbReference type="IntAct" id="Q03612">
+<property type="interactions" value="10"/>
+</dbReference>
+<dbReference type="MINT" id="Q03612"/>
+<dbReference type="STRING" id="4932.YER138C"/>
+<dbReference type="iPTMnet" id="Q03612"/>
+<dbReference type="MaxQB" id="Q03612"/>
+<dbReference type="PaxDb" id="Q03612"/>
+<dbReference type="GeneID" id="856879"/>
+<dbReference type="KEGG" id="sce:YER138C"/>
+<dbReference type="SGD" id="S000000940">
+<property type="gene designation" value="YER138C"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YER138C"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="Q03612"/>
+<dbReference type="ChiTaRS" id="YER138C">
+<property type="organism name" value="yeast"/>
+</dbReference>
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+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
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+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
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+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-ER1 Gag-Pol polyprotein" id="PRO_0000279043">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279044" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279045" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279046" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279047" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<sequence length="1755" mass="198562" checksum="6EB17ED89FF1F6FB" modified="1996-11-01" version="1">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="110">
+<accession>P0C2J1</accession>
+<accession>D6W4F7</accession>
+<name>YP14B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-PR3 Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<shortName>RT-RH</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-PR3</name>
+<name type="synonym">YPRCTy1-4 POL</name>
+<name type="ordered locus">YPR158C-D</name>
+<name type="ORF">P9584.3</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
+<person name="Albermann K."/>
+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
+<person name="Brueckner M."/>
+<person name="Carpenter J."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Churcher C.M."/>
+<person name="Coster F."/>
+<person name="Davis K."/>
+<person name="Davis R.W."/>
+<person name="Dietrich F.S."/>
+<person name="Delius H."/>
+<person name="DiPaolo T."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Duncan M."/>
+<person name="Floeth M."/>
+<person name="Fortin N."/>
+<person name="Friesen J.D."/>
+<person name="Fritz C."/>
+<person name="Goffeau A."/>
+<person name="Hall J."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Hilbert H."/>
+<person name="Hillier L.W."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Johnston M."/>
+<person name="Kalman S."/>
+<person name="Kleine K."/>
+<person name="Komp C."/>
+<person name="Kurdi O."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin A."/>
+<person name="Lin D."/>
+<person name="Louis E.J."/>
+<person name="Marathe R."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
+<person name="Nentwich U."/>
+<person name="Oefner P."/>
+<person name="Pearson D."/>
+<person name="Petel F.X."/>
+<person name="Pohl T.M."/>
+<person name="Purnelle B."/>
+<person name="Rajandream M.A."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Roberts D."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
+<person name="Ushinsky S."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Voss H."/>
+<person name="Walsh S.V."/>
+<person name="Wambutt R."/>
+<person name="Wang Y."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Winnett E."/>
+<person name="Zhong W.-W."/>
+<person name="Zollner A."/>
+<person name="Vo D.H."/>
+<person name="Hani J."/>
+</authorList>
+<dbReference type="PubMed" id="9169875"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0C2J1-1</id>
+<name>Transposon Ty1-PR3 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>Q6Q5H1-1</id>
+<name>Transposon Ty1-PR3 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-PR3 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YPR158C-C ORF.</text>
+</comment>
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+<dbReference type="EC" id="2.7.7.49"/>
+<dbReference type="EC" id="2.7.7.7"/>
+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="U28371">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11573.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69982">
+<property type="entry name" value="S69982"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058195.1">
+<molecule id="P0C2J1-1"/>
+<property type="nucleotide sequence ID" value="NM_001184396.2"/>
+</dbReference>
+<dbReference type="BioGRID" id="36328">
+<property type="interactions" value="4"/>
+</dbReference>
+<dbReference type="IntAct" id="P0C2J1">
+<property type="interactions" value="1"/>
+</dbReference>
+<dbReference type="STRING" id="4932.YPR158C-D"/>
+<dbReference type="iPTMnet" id="P0C2J1"/>
+<dbReference type="PaxDb" id="P0C2J1"/>
+<dbReference type="PRIDE" id="P0C2J1"/>
+<dbReference type="GeneID" id="856284"/>
+<dbReference type="KEGG" id="sce:YPR158C-D"/>
+<dbReference type="SGD" id="S000007362">
+<property type="gene designation" value="YPR158C-D"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YPR158C-D"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="P0C2J1"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XVI"/>
+</dbReference>
+<dbReference type="RNAct" id="P0C2J1">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
+<property type="term" value="F:RNA-DNA hybrid ribonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-PR3 Gag-Pol polyprotein" id="PRO_0000279184">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279185" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279186" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279187" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279188" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="829"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<sequence length="1755" mass="198374" checksum="3079CD1AA3977A78" modified="2007-03-06" version="1">MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSASQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKPISEINLRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSNNETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDPPPEPPTELSDSFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDRYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSHLVQELNKKPITKGLLTDSKSTISIIISNNEEKFRNRFFGTKAMRLRDEVSGNHLHVCYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2005-12-20" modified="2021-02-10" version="146">
+<accession>Q07589</accession>
+<accession>D6VRK4</accession>
+<name>YD144_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Uncharacterized protein YDL144C</fullName>
+</recommendedName>
+</protein>
+<gene>
+<name type="ordered locus">YDL144C</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="75" last="78">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
+<person name="Jacq C."/>
+<person name="Alt-Moerbe J."/>
+<person name="Andre B."/>
+<person name="Arnold W."/>
+<person name="Bahr A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Bargues M."/>
+<person name="Baron L."/>
+<person name="Becker A."/>
+<person name="Biteau N."/>
+<person name="Bloecker H."/>
+<person name="Blugeon C."/>
+<person name="Boskovic J."/>
+<person name="Brandt P."/>
+<person name="Brueckner M."/>
+<person name="Buitrago M.J."/>
+<person name="Coster F."/>
+<person name="Delaveau T."/>
+<person name="del Rey F."/>
+<person name="Dujon B."/>
+<person name="Eide L.G."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Goffeau A."/>
+<person name="Gomez-Peris A."/>
+<person name="Granotier C."/>
+<person name="Hanemann V."/>
+<person name="Hankeln T."/>
+<person name="Hoheisel J.D."/>
+<person name="Jaeger W."/>
+<person name="Jimenez A."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kraemer C."/>
+<person name="Kuester H."/>
+<person name="Laamanen P."/>
+<person name="Legros Y."/>
+<person name="Louis E.J."/>
+<person name="Moeller-Rieker S."/>
+<person name="Monnet A."/>
+<person name="Moro M."/>
+<person name="Mueller-Auer S."/>
+<person name="Nussbaumer B."/>
+<person name="Paricio N."/>
+<person name="Paulin L."/>
+<person name="Perea J."/>
+<person name="Perez-Alonso M."/>
+<person name="Perez-Ortin J.E."/>
+<person name="Pohl T.M."/>
+<person name="Prydz H."/>
+<person name="Purnelle B."/>
+<person name="Rasmussen S.W."/>
+<person name="Remacha M.A."/>
+<person name="Revuelta J.L."/>
+<person name="Rieger M."/>
+<person name="Salom D."/>
+<person name="Saluz H.P."/>
+<person name="Saiz J.E."/>
+<person name="Saren A.-M."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Schmidt E.R."/>
+<person name="Schneider C."/>
+<person name="Scholler P."/>
+<person name="Schwarz S."/>
+<person name="Soler-Mira A."/>
+<person name="Urrestarazu L.A."/>
+<person name="Verhasselt P."/>
+<person name="Vissers S."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Wagner G."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Woelfl S."/>
+<person name="Harris D.E."/>
+<person name="Bowman S."/>
+<person name="Brown D."/>
+<person name="Churcher C.M."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jones L."/>
+<person name="McDonald S."/>
+<person name="Murphy L.D."/>
+<person name="Niblett D."/>
+<person name="Odell C."/>
+<person name="Oliver K."/>
+<person name="Rajandream M.A."/>
+<person name="Richards C."/>
+<person name="Shore L."/>
+<person name="Walsh S.V."/>
+<person name="Barrell B.G."/>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin D."/>
+<person name="Mosedale D."/>
+<person name="Nakahara K."/>
+<person name="Namath A."/>
+<person name="Oefner P."/>
+<person name="Oh C."/>
+<person name="Petel F.X."/>
+<person name="Roberts D."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Shogren T."/>
+<person name="Shroff N."/>
+<person name="Winant A."/>
+<person name="Yelton M.A."/>
+<person name="Botstein D."/>
+<person name="Davis R.W."/>
+<person name="Johnston M."/>
+<person name="Andrews S."/>
+<person name="Brinkman R."/>
+<person name="Cooper J."/>
+<person name="Ding H."/>
+<person name="Du Z."/>
+<person name="Favello A."/>
+<person name="Fulton L."/>
+<person name="Gattung S."/>
+<person name="Greco T."/>
+<person name="Hallsworth K."/>
+<person name="Hawkins J."/>
+<person name="Hillier L.W."/>
+<person name="Jier M."/>
+<person name="Johnson D."/>
+<person name="Johnston L."/>
+<person name="Kirsten J."/>
+<person name="Kucaba T."/>
+<person name="Langston Y."/>
+<person name="Latreille P."/>
+<person name="Le T."/>
+<person name="Mardis E."/>
+<person name="Menezes S."/>
+<person name="Miller N."/>
+<person name="Nhan M."/>
+<person name="Pauley A."/>
+<person name="Peluso D."/>
+<person name="Rifkin L."/>
+<person name="Riles L."/>
+<person name="Taich A."/>
+<person name="Trevaskis E."/>
+<person name="Vignati D."/>
+<person name="Wilcox L."/>
+<person name="Wohldman P."/>
+<person name="Vaudin M."/>
+<person name="Wilson R."/>
+<person name="Waterston R."/>
+<person name="Albermann K."/>
+<person name="Hani J."/>
+<person name="Heumann K."/>
+<person name="Kleine K."/>
+<person name="Mewes H.-W."/>
+<person name="Zollner A."/>
+<person name="Zaccaria P."/>
+</authorList>
+<dbReference type="PubMed" id="9169867"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2003" name="Nature" volume="423" first="241" last="254">
+<title>Sequencing and comparison of yeast species to identify genes and regulatory elements.</title>
+<authorList>
+<person name="Kellis M."/>
+<person name="Patterson N."/>
+<person name="Endrizzi M."/>
+<person name="Birren B.W."/>
+<person name="Lander E.S."/>
+</authorList>
+<dbReference type="PubMed" id="12748633"/>
+<dbReference type="DOI" id="10.1038/nature01644"/>
+</citation>
+<scope>IDENTIFICATION OF PROBABLE INITIATION SITE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="686" last="691">
+<title>Global analysis of protein localization in budding yeast.</title>
+<authorList>
+<person name="Huh W.-K."/>
+<person name="Falvo J.V."/>
+<person name="Gerke L.C."/>
+<person name="Carroll A.S."/>
+<person name="Howson R.W."/>
+<person name="Weissman J.S."/>
+<person name="O'Shea E.K."/>
+</authorList>
+<dbReference type="PubMed" id="14562095"/>
+<dbReference type="DOI" id="10.1038/nature02026"/>
+</citation>
+<scope>SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 5171 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="sequence caution" evidence="3">
+<conflict type="erroneous initiation">
+<sequence resource="EMBL-CDS" id="CAA98717" version="1"/>
+</conflict>
+</comment>
+<dbReference type="EMBL" id="Z74192">
+<property type="protein sequence ID" value="CAA98717.1"/>
+<property type="status" value="ALT_INIT"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006938">
+<property type="protein sequence ID" value="DAA11714.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S67691">
+<property type="entry name" value="S67691"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_010137.2">
+<property type="nucleotide sequence ID" value="NM_001180204.1"/>
+</dbReference>
+<dbReference type="BioGRID" id="31917">
+<property type="interactions" value="38"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-1632N"/>
+<dbReference type="IntAct" id="Q07589">
+<property type="interactions" value="5"/>
+</dbReference>
+<dbReference type="MINT" id="Q07589"/>
+<dbReference type="STRING" id="4932.YDL144C"/>
+<dbReference type="MaxQB" id="Q07589"/>
+<dbReference type="PaxDb" id="Q07589"/>
+<dbReference type="PRIDE" id="Q07589"/>
+<dbReference type="EnsemblFungi" id="YDL144C_mRNA">
+<property type="protein sequence ID" value="YDL144C"/>
+<property type="gene ID" value="YDL144C"/>
+</dbReference>
+<dbReference type="GeneID" id="851411"/>
+<dbReference type="KEGG" id="sce:YDL144C"/>
+<dbReference type="SGD" id="S000002303">
+<property type="gene designation" value="YDL144C"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YDL144C"/>
+<dbReference type="eggNOG" id="ENOG502QWBM">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="GeneTree" id="ENSGT00940000176320"/>
+<dbReference type="HOGENOM" id="CLU_031468_2_1_1"/>
+<dbReference type="InParanoid" id="Q07589"/>
+<dbReference type="OMA" id="FKPSMCV"/>
+<dbReference type="PRO" id="PR:Q07589"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome IV"/>
+</dbReference>
+<dbReference type="RNAct" id="Q07589">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0007005"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0016491">
+<property type="term" value="F:oxidoreductase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="InterPro"/>
+</dbReference>
+<dbReference type="Gene3D" id="1.10.1040.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR008927">
+<property type="entry name" value="6-PGluconate_DH-like_C_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013328">
+<property type="entry name" value="6PGD_dom2"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013752">
+<property type="entry name" value="KPA_reductase"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013332">
+<property type="entry name" value="KPR_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036291">
+<property type="entry name" value="NAD(P)-bd_dom_sf"/>
+</dbReference>
+<dbReference type="Pfam" id="PF02558">
+<property type="entry name" value="ApbA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF08546">
+<property type="entry name" value="ApbA_C"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF48179">
+<property type="entry name" value="SSF48179"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF51735">
+<property type="entry name" value="SSF51735"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<feature type="chain" description="Uncharacterized protein YDL144C" id="PRO_0000202587">
+<location>
+<begin position="1"/>
+<end position="356"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562095"/>
+</source>
+</evidence>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000305"/>
+<sequence length="356" mass="39783" checksum="12578C1253C1AA21" modified="2005-12-20" version="2">MSRILVIGAGGVGVITALSLWLKKESDVSLVVRSDYDRVLKHGYTIESCDYGRLEGWRPHHIYSSVEDAASAADNQGYNYIVVTTKNIIDGPVNSRVSNIIRPVLEKNKELHGPQLTTHILLVQNGIDIEKEIWAEFPREQYRYTVLSGIQLIGSTKIGSGHISQVGQDHLSCGAFDPQDAAAIQAANDFVRMYSNEGQNFVEFDPRVRYSRWKKLLYNAAINTSTALVGLDVPRCLEFGVNKKSTEIEVFHPAMREIIAIAASEGIIIEEEFITMFTEITRKKVFKPSMCVDCEKGQLMELEVILGNPIRIAKRNGVATPTLSILYNLLVLVQAKLKERKGLLKFDEKTATLVDE</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="102">
+<accession>Q6Q5H1</accession>
+<accession>D6W4F8</accession>
+<name>YP14A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-PR3 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-PR3</name>
+<name type="synonym">YPRCTy1-4 GAG</name>
+<name type="ordered locus">YPR158C-C</name>
+<name type="ORF">P9584.3</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
+<person name="Albermann K."/>
+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
+<person name="Brueckner M."/>
+<person name="Carpenter J."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Churcher C.M."/>
+<person name="Coster F."/>
+<person name="Davis K."/>
+<person name="Davis R.W."/>
+<person name="Dietrich F.S."/>
+<person name="Delius H."/>
+<person name="DiPaolo T."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Duncan M."/>
+<person name="Floeth M."/>
+<person name="Fortin N."/>
+<person name="Friesen J.D."/>
+<person name="Fritz C."/>
+<person name="Goffeau A."/>
+<person name="Hall J."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Hilbert H."/>
+<person name="Hillier L.W."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Johnston M."/>
+<person name="Kalman S."/>
+<person name="Kleine K."/>
+<person name="Komp C."/>
+<person name="Kurdi O."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin A."/>
+<person name="Lin D."/>
+<person name="Louis E.J."/>
+<person name="Marathe R."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
+<person name="Nentwich U."/>
+<person name="Oefner P."/>
+<person name="Pearson D."/>
+<person name="Petel F.X."/>
+<person name="Pohl T.M."/>
+<person name="Purnelle B."/>
+<person name="Rajandream M.A."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Roberts D."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
+<person name="Ushinsky S."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Voss H."/>
+<person name="Walsh S.V."/>
+<person name="Wambutt R."/>
+<person name="Wang Y."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Winnett E."/>
+<person name="Zhong W.-W."/>
+<person name="Zollner A."/>
+<person name="Vo D.H."/>
+<person name="Hani J."/>
+</authorList>
+<dbReference type="PubMed" id="9169875"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
+<person name="Rolfs A."/>
+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
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+<person name="Kolodner R.D."/>
+<person name="LaBaer J."/>
+</authorList>
+<dbReference type="PubMed" id="17322287"/>
+<dbReference type="DOI" id="10.1101/gr.6037607"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>Q6Q5H1-1</id>
+<name>Transposon Ty1-PR3 Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0C2J1-1</id>
+<name>Transposon Ty1-PR3 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-PR3 is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-PR3 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="U28371">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY558070">
+<property type="protein sequence ID" value="AAS56396.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11574.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69985">
+<property type="entry name" value="S69985"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058196.1">
+<molecule id="Q6Q5H1-1"/>
+<property type="nucleotide sequence ID" value="NM_001184395.1"/>
+</dbReference>
+<dbReference type="SMR" id="Q6Q5H1"/>
+<dbReference type="BioGRID" id="36329">
+<property type="interactions" value="10"/>
+</dbReference>
+<dbReference type="IntAct" id="Q6Q5H1">
+<property type="interactions" value="1"/>
+</dbReference>
+<dbReference type="STRING" id="4932.YPR158C-C"/>
+<dbReference type="iPTMnet" id="Q6Q5H1"/>
+<dbReference type="PaxDb" id="Q6Q5H1"/>
+<dbReference type="PRIDE" id="Q6Q5H1"/>
+<dbReference type="GeneID" id="856285"/>
+<dbReference type="KEGG" id="sce:YPR158C-C"/>
+<dbReference type="SGD" id="S000007361">
+<property type="gene designation" value="YPR158C-C"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YPR158C-C"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XVI"/>
+</dbReference>
+<dbReference type="RNAct" id="Q6Q5H1">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-PR3 Gag polyprotein" id="PRO_0000279189">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279190" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000279191" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; AAS56396." ref="3" evidence="4">
+<original>G</original>
+<variation>C</variation>
+<location>
+<position position="199"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11884596"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000305"/>
+<sequence length="440" mass="48965" checksum="8C2E419B10A9B7D0" modified="2007-03-06" version="2">MESQQLSNYSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="109">
+<accession>P0C2I3</accession>
+<accession>D6VSZ5</accession>
+<name>YD15B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-DR6 Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<shortName>RT-RH</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-DR6</name>
+<name type="synonym">YDRWTy1-5 POL</name>
+<name type="ordered locus">YDR365W-B</name>
+<name type="ORF">D9481.12</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="75" last="78">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.</title>
+<authorList>
+<person name="Jacq C."/>
+<person name="Alt-Moerbe J."/>
+<person name="Andre B."/>
+<person name="Arnold W."/>
+<person name="Bahr A."/>
+<person name="Ballesta J.P.G."/>
+<person name="Bargues M."/>
+<person name="Baron L."/>
+<person name="Becker A."/>
+<person name="Biteau N."/>
+<person name="Bloecker H."/>
+<person name="Blugeon C."/>
+<person name="Boskovic J."/>
+<person name="Brandt P."/>
+<person name="Brueckner M."/>
+<person name="Buitrago M.J."/>
+<person name="Coster F."/>
+<person name="Delaveau T."/>
+<person name="del Rey F."/>
+<person name="Dujon B."/>
+<person name="Eide L.G."/>
+<person name="Garcia-Cantalejo J.M."/>
+<person name="Goffeau A."/>
+<person name="Gomez-Peris A."/>
+<person name="Granotier C."/>
+<person name="Hanemann V."/>
+<person name="Hankeln T."/>
+<person name="Hoheisel J.D."/>
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+<person name="Jimenez A."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kraemer C."/>
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+<person name="Laamanen P."/>
+<person name="Legros Y."/>
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+<person name="Moeller-Rieker S."/>
+<person name="Monnet A."/>
+<person name="Moro M."/>
+<person name="Mueller-Auer S."/>
+<person name="Nussbaumer B."/>
+<person name="Paricio N."/>
+<person name="Paulin L."/>
+<person name="Perea J."/>
+<person name="Perez-Alonso M."/>
+<person name="Perez-Ortin J.E."/>
+<person name="Pohl T.M."/>
+<person name="Prydz H."/>
+<person name="Purnelle B."/>
+<person name="Rasmussen S.W."/>
+<person name="Remacha M.A."/>
+<person name="Revuelta J.L."/>
+<person name="Rieger M."/>
+<person name="Salom D."/>
+<person name="Saluz H.P."/>
+<person name="Saiz J.E."/>
+<person name="Saren A.-M."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
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+<person name="Schneider C."/>
+<person name="Scholler P."/>
+<person name="Schwarz S."/>
+<person name="Soler-Mira A."/>
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+<person name="Verhasselt P."/>
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+<person name="Brown D."/>
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+<person name="Connor R."/>
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+<person name="Shore L."/>
+<person name="Walsh S.V."/>
+<person name="Barrell B.G."/>
+<person name="Dietrich F.S."/>
+<person name="Mulligan J.T."/>
+<person name="Allen E."/>
+<person name="Araujo R."/>
+<person name="Aviles E."/>
+<person name="Berno A."/>
+<person name="Carpenter J."/>
+<person name="Chen E."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Duncan M."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Komp C."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin D."/>
+<person name="Mosedale D."/>
+<person name="Nakahara K."/>
+<person name="Namath A."/>
+<person name="Oefner P."/>
+<person name="Oh C."/>
+<person name="Petel F.X."/>
+<person name="Roberts D."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Shogren T."/>
+<person name="Shroff N."/>
+<person name="Winant A."/>
+<person name="Yelton M.A."/>
+<person name="Botstein D."/>
+<person name="Davis R.W."/>
+<person name="Johnston M."/>
+<person name="Andrews S."/>
+<person name="Brinkman R."/>
+<person name="Cooper J."/>
+<person name="Ding H."/>
+<person name="Du Z."/>
+<person name="Favello A."/>
+<person name="Fulton L."/>
+<person name="Gattung S."/>
+<person name="Greco T."/>
+<person name="Hallsworth K."/>
+<person name="Hawkins J."/>
+<person name="Hillier L.W."/>
+<person name="Jier M."/>
+<person name="Johnson D."/>
+<person name="Johnston L."/>
+<person name="Kirsten J."/>
+<person name="Kucaba T."/>
+<person name="Langston Y."/>
+<person name="Latreille P."/>
+<person name="Le T."/>
+<person name="Mardis E."/>
+<person name="Menezes S."/>
+<person name="Miller N."/>
+<person name="Nhan M."/>
+<person name="Pauley A."/>
+<person name="Peluso D."/>
+<person name="Rifkin L."/>
+<person name="Riles L."/>
+<person name="Taich A."/>
+<person name="Trevaskis E."/>
+<person name="Vignati D."/>
+<person name="Wilcox L."/>
+<person name="Wohldman P."/>
+<person name="Vaudin M."/>
+<person name="Wilson R."/>
+<person name="Waterston R."/>
+<person name="Albermann K."/>
+<person name="Hani J."/>
+<person name="Heumann K."/>
+<person name="Kleine K."/>
+<person name="Mewes H.-W."/>
+<person name="Zollner A."/>
+<person name="Zaccaria P."/>
+</authorList>
+<dbReference type="PubMed" id="9169867"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0C2I3-1</id>
+<name>Transposon Ty1-DR6 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0CX70-1</id>
+<name>Transposon Ty1-DR6 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-DR6 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YDR365W-A ORF.</text>
+</comment>
+<dbReference type="EC" id="3.4.23.-"/>
+<dbReference type="EC" id="2.7.7.49"/>
+<dbReference type="EC" id="2.7.7.7"/>
+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="U28373">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006938">
+<property type="protein sequence ID" value="DAA12205.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69957">
+<property type="entry name" value="S69957"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058152.1">
+<molecule id="P0C2I3-1"/>
+<property type="nucleotide sequence ID" value="NM_001184427.2"/>
+</dbReference>
+<dbReference type="BioGRID" id="32424">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="iPTMnet" id="P0C2I3"/>
+<dbReference type="PaxDb" id="P0C2I3"/>
+<dbReference type="PRIDE" id="P0C2I3"/>
+<dbReference type="GeneID" id="851971"/>
+<dbReference type="KEGG" id="sce:YDR365W-B"/>
+<dbReference type="SGD" id="S000007401">
+<property type="gene designation" value="YDR365W-B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YDR365W-B"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="P0C2I3"/>
+<dbReference type="ChiTaRS" id="YDR365W-B">
+<property type="organism name" value="yeast"/>
+</dbReference>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome IV"/>
+</dbReference>
+<dbReference type="RNAct" id="P0C2I3">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
+<property type="term" value="F:RNA-DNA hybrid ribonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-DR6 Gag-Pol polyprotein" id="PRO_0000279032">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279033" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279034" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279035" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279036" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<sequence length="1755" mass="198659" checksum="D8F43BA96B1C2760" modified="2007-03-06" version="1">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNYLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1996-02-01" modified="2021-02-10" version="158">
+<accession>P47098</accession>
+<accession>D6VWJ9</accession>
+<accession>P87194</accession>
+<name>YJ11B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-JR1 Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<shortName>RT-RH</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-JR1</name>
+<name type="synonym">YJRWTy1-1 POL</name>
+<name type="ordered locus">YJR027W</name>
+<name type="ORF">J1560</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="1179" last="1186">
+<title>The sequence of 24.3 kb from chromosome X reveals five complete open reading frames, all of which correspond to new genes, and a tandem insertion of a Ty1 transposon.</title>
+<authorList>
+<person name="Zagulski M."/>
+<person name="Babinska B."/>
+<person name="Gromadka R."/>
+<person name="Migdalski A."/>
+<person name="Rytka J."/>
+<person name="Sulicka J."/>
+<person name="Herbert C.J."/>
+</authorList>
+<dbReference type="PubMed" id="8619316"/>
+<dbReference type="DOI" id="10.1002/yea.320111208"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1996" name="EMBO J." volume="15" first="2031" last="2049">
+<title>Complete nucleotide sequence of Saccharomyces cerevisiae chromosome X.</title>
+<authorList>
+<person name="Galibert F."/>
+<person name="Alexandraki D."/>
+<person name="Baur A."/>
+<person name="Boles E."/>
+<person name="Chalwatzis N."/>
+<person name="Chuat J.-C."/>
+<person name="Coster F."/>
+<person name="Cziepluch C."/>
+<person name="de Haan M."/>
+<person name="Domdey H."/>
+<person name="Durand P."/>
+<person name="Entian K.-D."/>
+<person name="Gatius M."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="Hennemann A."/>
+<person name="Herbert C.J."/>
+<person name="Heumann K."/>
+<person name="Hilger F."/>
+<person name="Hollenberg C.P."/>
+<person name="Huang M.-E."/>
+<person name="Jacq C."/>
+<person name="Jauniaux J.-C."/>
+<person name="Katsoulou C."/>
+<person name="Kirchrath L."/>
+<person name="Kleine K."/>
+<person name="Kordes E."/>
+<person name="Koetter P."/>
+<person name="Liebl S."/>
+<person name="Louis E.J."/>
+<person name="Manus V."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Obermaier B."/>
+<person name="Perea J."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rasmussen S.W."/>
+<person name="Rose M."/>
+<person name="Rossau R."/>
+<person name="Schaaff-Gerstenschlaeger I."/>
+<person name="Smits P.H.M."/>
+<person name="Scarcez T."/>
+<person name="Soriano N."/>
+<person name="To Van D."/>
+<person name="Tzermia M."/>
+<person name="Van Broekhoven A."/>
+<person name="Vandenbol M."/>
+<person name="Wedler H."/>
+<person name="von Wettstein D."/>
+<person name="Wambutt R."/>
+<person name="Zagulski M."/>
+<person name="Zollner A."/>
+<person name="Karpfinger-Hartl L."/>
+</authorList>
+<dbReference type="PubMed" id="8641269"/>
+<dbReference type="DOI" id="10.1002/j.1460-2075.1996.tb00557.x"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P47098-1</id>
+<name>Transposon Ty1-JR1 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0CX74-1</id>
+<name>Transposon Ty1-JR1 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-JR1 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YJR026W ORF.</text>
+</comment>
+<comment type="sequence caution" evidence="5">
+<conflict type="erroneous gene model prediction">
+<sequence resource="EMBL-CDS" id="CAA89553" version="1"/>
+</conflict>
+</comment>
+<dbReference type="EC" id="3.4.23.-"/>
+<dbReference type="EC" id="2.7.7.49"/>
+<dbReference type="EC" id="2.7.7.7"/>
+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="X87297">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z49526">
+<property type="protein sequence ID" value="CAA89553.1"/>
+<property type="status" value="ALT_SEQ"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006943">
+<property type="protein sequence ID" value="DAA08815.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S57045">
+<property type="entry name" value="S57045"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_012560.1">
+<molecule id="P47098-1"/>
+<property type="nucleotide sequence ID" value="NM_001181685.2"/>
+</dbReference>
+<dbReference type="SMR" id="P47098"/>
+<dbReference type="BioGRID" id="33780">
+<property type="interactions" value="8"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-6367N"/>
+<dbReference type="IntAct" id="P47098">
+<property type="interactions" value="1"/>
+</dbReference>
+<dbReference type="STRING" id="4932.YJR027W"/>
+<dbReference type="iPTMnet" id="P47098"/>
+<dbReference type="PaxDb" id="P47098"/>
+<dbReference type="GeneID" id="853484"/>
+<dbReference type="KEGG" id="sce:YJR027W"/>
+<dbReference type="SGD" id="S000003788">
+<property type="gene designation" value="YJR027W"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YJR027W"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="P47098"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome X"/>
+</dbReference>
+<dbReference type="RNAct" id="P47098">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
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+</dbReference>
+<dbReference type="GO" id="GO:0003677">
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+</dbReference>
+<dbReference type="GO" id="GO:0003887">
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+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
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+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
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+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
+<property type="term" value="F:RNA-DNA hybrid ribonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-JR1 Gag-Pol polyprotein" id="PRO_0000199563">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279082" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279083" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279084" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279085" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000305"/>
+<sequence length="1755" mass="198652" checksum="88F0B33BB020E338" modified="2010-11-02" version="3">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVQYGDFYWVSKRYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDTGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSHYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2020-12-02" version="66">
+<accession>P0CX76</accession>
+<accession>D6VWK0</accession>
+<accession>P47097</accession>
+<accession>Q66R50</accession>
+<name>YM12A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-ML2 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-ML2</name>
+<name type="synonym">YMLWTy1-2 GAG</name>
+<name type="ordered locus">YML040W</name>
+<name type="ORF">YM8054.03</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="90" last="93">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.</title>
+<authorList>
+<person name="Bowman S."/>
+<person name="Churcher C.M."/>
+<person name="Badcock K."/>
+<person name="Brown D."/>
+<person name="Chillingworth T."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Devlin K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jagels K."/>
+<person name="Lye G."/>
+<person name="Moule S."/>
+<person name="Odell C."/>
+<person name="Pearson D."/>
+<person name="Rajandream M.A."/>
+<person name="Rice P."/>
+<person name="Skelton J."/>
+<person name="Walsh S.V."/>
+<person name="Whitehead S."/>
+<person name="Barrell B.G."/>
+</authorList>
+<dbReference type="PubMed" id="9169872"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0CX76-1</id>
+<name>Transposon Ty1-ML2 Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>Q03434-1</id>
+<name>Transposon Ty1-ML2 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-ML2 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-ML2 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="Z48430">
+<property type="protein sequence ID" value="CAA88329.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006946">
+<property type="protein sequence ID" value="DAA09860.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S57044">
+<property type="entry name" value="S57044"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_012561.3">
+<molecule id="P0CX76-1"/>
+<property type="nucleotide sequence ID" value="NM_001181684.3"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013673.1">
+<molecule id="P0CX76-1"/>
+<property type="nucleotide sequence ID" value="NM_001182398.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058172.1">
+<molecule id="P0CX76-1"/>
+<property type="nucleotide sequence ID" value="NM_001184407.1"/>
+</dbReference>
+<dbReference type="SMR" id="P0CX76"/>
+<dbReference type="BioGRID" id="31496">
+<property type="interactions" value="3"/>
+</dbReference>
+<dbReference type="BioGRID" id="33779">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="BioGRID" id="35130">
+<property type="interactions" value="5"/>
+</dbReference>
+<dbReference type="iPTMnet" id="P0CX76"/>
+<dbReference type="GeneID" id="850926"/>
+<dbReference type="GeneID" id="853483"/>
+<dbReference type="GeneID" id="854968"/>
+<dbReference type="KEGG" id="sce:YJR026W"/>
+<dbReference type="KEGG" id="sce:YLR227W-A"/>
+<dbReference type="KEGG" id="sce:YML040W"/>
+<dbReference type="SGD" id="S000004504">
+<property type="gene designation" value="YML040W"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="InParanoid" id="P0CX76"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XIII"/>
+</dbReference>
+<dbReference type="RNAct" id="P0CX76">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-ML2 Gag polyprotein" id="PRO_0000409803">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000409804" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000409805" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11884596"/>
+</source>
+</evidence>
+<sequence length="440" mass="48993" checksum="ACC50DD2AC8F4781" modified="2011-06-28" version="1">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1997-11-01" modified="2021-02-10" version="144">
+<accession>Q03434</accession>
+<accession>D6VZD5</accession>
+<name>YM12B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-ML2 Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-ML2</name>
+<name type="synonym">YMLWTy1-2 POL</name>
+<name type="ordered locus">YML039W</name>
+<name type="ORF">YM8054.04</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="90" last="93">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.</title>
+<authorList>
+<person name="Bowman S."/>
+<person name="Churcher C.M."/>
+<person name="Badcock K."/>
+<person name="Brown D."/>
+<person name="Chillingworth T."/>
+<person name="Connor R."/>
+<person name="Dedman K."/>
+<person name="Devlin K."/>
+<person name="Gentles S."/>
+<person name="Hamlin N."/>
+<person name="Hunt S."/>
+<person name="Jagels K."/>
+<person name="Lye G."/>
+<person name="Moule S."/>
+<person name="Odell C."/>
+<person name="Pearson D."/>
+<person name="Rajandream M.A."/>
+<person name="Rice P."/>
+<person name="Skelton J."/>
+<person name="Walsh S.V."/>
+<person name="Whitehead S."/>
+<person name="Barrell B.G."/>
+</authorList>
+<dbReference type="PubMed" id="9169872"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>Q03434-1</id>
+<name>Transposon Ty1-ML2 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0CX76-1</id>
+<name>Transposon Ty1-ML2 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-ML2 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YML040W ORF.</text>
+</comment>
+<comment type="sequence caution" evidence="5">
+<conflict type="erroneous gene model prediction">
+<sequence resource="EMBL-CDS" id="CAA88330" version="1"/>
+</conflict>
+</comment>
+<dbReference type="EC" id="3.4.23.-"/>
+<dbReference type="EC" id="2.7.7.49"/>
+<dbReference type="EC" id="2.7.7.7"/>
+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="Z48430">
+<property type="protein sequence ID" value="CAA88330.1"/>
+<property type="status" value="ALT_SEQ"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006946">
+<property type="protein sequence ID" value="DAA09859.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S52481">
+<property type="entry name" value="S52481"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013672.1">
+<molecule id="Q03434-1"/>
+<property type="nucleotide sequence ID" value="NM_001182397.2"/>
+</dbReference>
+<dbReference type="SMR" id="Q03434"/>
+<dbReference type="BioGRID" id="35131">
+<property type="interactions" value="3"/>
+</dbReference>
+<dbReference type="iPTMnet" id="Q03434"/>
+<dbReference type="PaxDb" id="Q03434"/>
+<dbReference type="PRIDE" id="Q03434"/>
+<dbReference type="GeneID" id="854969"/>
+<dbReference type="KEGG" id="sce:YML039W"/>
+<dbReference type="SGD" id="S000004503">
+<property type="gene designation" value="YML039W"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YML039W"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="Q03434"/>
+<dbReference type="OMA" id="KKQDICR"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XIII"/>
+</dbReference>
+<dbReference type="RNAct" id="Q03434">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
+<property type="term" value="F:RNA-DNA hybrid ribonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-ML2 Gag-Pol polyprotein" id="PRO_0000199565">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279123" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279124" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279125" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279126" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000305"/>
+<sequence length="1755" mass="198572" checksum="5EC9D7C5C3192354" modified="2007-03-06" version="2">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDRSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPKSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYQSFIASNEIQQSDDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSHQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="75">
+<accession>P0C2I7</accession>
+<name>YL14B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-LR4 Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<shortName>RT-RH</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-LR4</name>
+<name type="synonym">YLRWTy1-4 POL</name>
+<name type="ordered locus">YLR256W-B/YLR256W-C</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
+<person name="Johnston M."/>
+<person name="Hillier L.W."/>
+<person name="Riles L."/>
+<person name="Albermann K."/>
+<person name="Andre B."/>
+<person name="Ansorge W."/>
+<person name="Benes V."/>
+<person name="Brueckner M."/>
+<person name="Delius H."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Entian K.-D."/>
+<person name="Floeth M."/>
+<person name="Goffeau A."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Heuss-Neitzel D."/>
+<person name="Hilbert H."/>
+<person name="Hilger F."/>
+<person name="Kleine K."/>
+<person name="Koetter P."/>
+<person name="Louis E.J."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Miosga T."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Nentwich U."/>
+<person name="Obermaier B."/>
+<person name="Piravandi E."/>
+<person name="Pohl T.M."/>
+<person name="Portetelle D."/>
+<person name="Purnelle B."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Rinke M."/>
+<person name="Rose M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Scholler P."/>
+<person name="Schwager C."/>
+<person name="Schwarz S."/>
+<person name="Underwood A.P."/>
+<person name="Urrestarazu L.A."/>
+<person name="Vandenbol M."/>
+<person name="Verhasselt P."/>
+<person name="Vierendeels F."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Zimmermann F.K."/>
+<person name="Zollner A."/>
+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+<scope>IDENTIFICATION OF FRAMESHIFT</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0C2I7-1</id>
+<name>Transposon Ty1-LR4 Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0C2I8-1</id>
+<name>Transposon Ty1-LR4 Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-LR4 Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YLR256W-A ORF.</text>
+</comment>
+<comment type="caution">
+<text evidence="5 6">Could be the product of a pseudogene unlikely to encode a functional protein. Transposon Ty1-LR4 (YLRWTy1-4) contains a frameshift at position 753, which disrupts the ORF coding for protein TY1B. Because of that it is not part of the S.cerevisiae S288c complete/reference proteome set.</text>
+</comment>
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+<dbReference type="EC" id="3.1.26.4"/>
+<dbReference type="EMBL" id="U20865">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PeptideAtlas" id="P0C2I7"/>
+<dbReference type="PRIDE" id="P0C2I7"/>
+<dbReference type="InParanoid" id="P0C2I7"/>
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+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
+<property type="term" value="F:RNA-DNA hybrid ribonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032196">
+<property type="term" value="P:transposition"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="uncertain"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-LR4 Gag-Pol polyprotein" id="PRO_0000279109">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279110" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279111" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279112" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279113" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<evidence key="5" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="24374639"/>
+</source>
+</evidence>
+<evidence key="6" type="ECO:0000305">
+<source>
+<dbReference type="PubMed" id="9582191"/>
+</source>
+</evidence>
+<sequence length="1755" mass="198656" checksum="4CF7E58C3E27F89D" modified="2007-03-06" version="1">MESQQLSQHPHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIQQCGMEEVRGWSCVFKNSQVTICLFVDDMVLFSKNLNSNKRIIEKLKMQYDTKIINLGESDEEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTKPDNKLVAISDASYGNQPYYKSQIGNIFLLNGKVIGGKSTKASLTCTSTTEAEIHAVSEAIPLLNNLSHLVQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1994-10-01" modified="2021-04-07" version="153">
+<accession>P38079</accession>
+<accession>D6VQ53</accession>
+<name>YRO2_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Protein YRO2</fullName>
+</recommendedName>
+</protein>
+<gene>
+<name type="primary">YRO2</name>
+<name type="ordered locus">YBR054W</name>
+<name type="ORF">YBR0507</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="475" last="479">
+<title>Sequence and analysis of 24 kb on chromosome II of Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Aljinovic G."/>
+<person name="Pohl T.M."/>
+</authorList>
+<dbReference type="PubMed" id="7597852"/>
+<dbReference type="DOI" id="10.1002/yea.320110511"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1994" name="EMBO J." volume="13" first="5795" last="5809">
+<title>Complete DNA sequence of yeast chromosome II.</title>
+<authorList>
+<person name="Feldmann H."/>
+<person name="Aigle M."/>
+<person name="Aljinovic G."/>
+<person name="Andre B."/>
+<person name="Baclet M.C."/>
+<person name="Barthe C."/>
+<person name="Baur A."/>
+<person name="Becam A.-M."/>
+<person name="Biteau N."/>
+<person name="Boles E."/>
+<person name="Brandt T."/>
+<person name="Brendel M."/>
+<person name="Brueckner M."/>
+<person name="Bussereau F."/>
+<person name="Christiansen C."/>
+<person name="Contreras R."/>
+<person name="Crouzet M."/>
+<person name="Cziepluch C."/>
+<person name="Demolis N."/>
+<person name="Delaveau T."/>
+<person name="Doignon F."/>
+<person name="Domdey H."/>
+<person name="Duesterhus S."/>
+<person name="Dubois E."/>
+<person name="Dujon B."/>
+<person name="El Bakkoury M."/>
+<person name="Entian K.-D."/>
+<person name="Feuermann M."/>
+<person name="Fiers W."/>
+<person name="Fobo G.M."/>
+<person name="Fritz C."/>
+<person name="Gassenhuber J."/>
+<person name="Glansdorff N."/>
+<person name="Goffeau A."/>
+<person name="Grivell L.A."/>
+<person name="de Haan M."/>
+<person name="Hein C."/>
+<person name="Herbert C.J."/>
+<person name="Hollenberg C.P."/>
+<person name="Holmstroem K."/>
+<person name="Jacq C."/>
+<person name="Jacquet M."/>
+<person name="Jauniaux J.-C."/>
+<person name="Jonniaux J.-L."/>
+<person name="Kallesoee T."/>
+<person name="Kiesau P."/>
+<person name="Kirchrath L."/>
+<person name="Koetter P."/>
+<person name="Korol S."/>
+<person name="Liebl S."/>
+<person name="Logghe M."/>
+<person name="Lohan A.J.E."/>
+<person name="Louis E.J."/>
+<person name="Li Z.Y."/>
+<person name="Maat M.J."/>
+<person name="Mallet L."/>
+<person name="Mannhaupt G."/>
+<person name="Messenguy F."/>
+<person name="Miosga T."/>
+<person name="Molemans F."/>
+<person name="Mueller S."/>
+<person name="Nasr F."/>
+<person name="Obermaier B."/>
+<person name="Perea J."/>
+<person name="Pierard A."/>
+<person name="Piravandi E."/>
+<person name="Pohl F.M."/>
+<person name="Pohl T.M."/>
+<person name="Potier S."/>
+<person name="Proft M."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rieger M."/>
+<person name="Rose M."/>
+<person name="Schaaff-Gerstenschlaeger I."/>
+<person name="Scherens B."/>
+<person name="Schwarzlose C."/>
+<person name="Skala J."/>
+<person name="Slonimski P.P."/>
+<person name="Smits P.H.M."/>
+<person name="Souciet J.-L."/>
+<person name="Steensma H.Y."/>
+<person name="Stucka R."/>
+<person name="Urrestarazu L.A."/>
+<person name="van der Aart Q.J.M."/>
+<person name="Van Dyck L."/>
+<person name="Vassarotti A."/>
+<person name="Vetter I."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Wagner G."/>
+<person name="de Wergifosse P."/>
+<person name="Wolfe K.H."/>
+<person name="Zagulski M."/>
+<person name="Zimmermann F.K."/>
+<person name="Mewes H.-W."/>
+<person name="Kleine K."/>
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+<dbReference type="DOI" id="10.1002/j.1460-2075.1994.tb06923.x"/>
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+<source>
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+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
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+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2003" name="Nature" volume="425" first="737" last="741">
+<title>Global analysis of protein expression in yeast.</title>
+<authorList>
+<person name="Ghaemmaghami S."/>
+<person name="Huh W.-K."/>
+<person name="Bower K."/>
+<person name="Howson R.W."/>
+<person name="Belle A."/>
+<person name="Dephoure N."/>
+<person name="O'Shea E.K."/>
+<person name="Weissman J.S."/>
+</authorList>
+<dbReference type="PubMed" id="14562106"/>
+<dbReference type="DOI" id="10.1038/nature02046"/>
+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2003" name="Nat. Biotechnol." volume="21" first="921" last="926">
+<title>A proteomics approach to understanding protein ubiquitination.</title>
+<authorList>
+<person name="Peng J."/>
+<person name="Schwartz D."/>
+<person name="Elias J.E."/>
+<person name="Thoreen C.C."/>
+<person name="Cheng D."/>
+<person name="Marsischky G."/>
+<person name="Roelofs J."/>
+<person name="Finley D."/>
+<person name="Gygi S.P."/>
+</authorList>
+<dbReference type="PubMed" id="12872131"/>
+<dbReference type="DOI" id="10.1038/nbt849"/>
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+<scope>UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-286</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY</scope>
+<source>
+<strain>SUB592</strain>
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+</reference>
+<reference key="6">
+<citation type="journal article" date="2006" name="Proc. Natl. Acad. Sci. U.S.A." volume="103" first="11142" last="11147">
+<title>A global topology map of the Saccharomyces cerevisiae membrane proteome.</title>
+<authorList>
+<person name="Kim H."/>
+<person name="Melen K."/>
+<person name="Oesterberg M."/>
+<person name="von Heijne G."/>
+</authorList>
+<dbReference type="PubMed" id="16847258"/>
+<dbReference type="DOI" id="10.1073/pnas.0604075103"/>
+</citation>
+<scope>TOPOLOGY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ATCC 208353 / W303-1A</strain>
+</source>
+</reference>
+<reference key="7">
+<citation type="journal article" date="2007" name="Mol. Cell. Proteomics" volume="6" first="1896" last="1906">
+<title>Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase.</title>
+<authorList>
+<person name="Reinders J."/>
+<person name="Wagner K."/>
+<person name="Zahedi R.P."/>
+<person name="Stojanovski D."/>
+<person name="Eyrich B."/>
+<person name="van der Laan M."/>
+<person name="Rehling P."/>
+<person name="Sickmann A."/>
+<person name="Pfanner N."/>
+<person name="Meisinger C."/>
+</authorList>
+<dbReference type="PubMed" id="17761666"/>
+<dbReference type="DOI" id="10.1074/mcp.m700098-mcp200"/>
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+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341 AND SER-343</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+<source>
+<strain>ATCC 76625 / YPH499</strain>
+</source>
+</reference>
+<reference key="8">
+<citation type="journal article" date="2008" name="Mol. Cell. Proteomics" volume="7" first="1389" last="1396">
+<title>A multidimensional chromatography technology for in-depth phosphoproteome analysis.</title>
+<authorList>
+<person name="Albuquerque C.P."/>
+<person name="Smolka M.B."/>
+<person name="Payne S.H."/>
+<person name="Bafna V."/>
+<person name="Eng J."/>
+<person name="Zhou H."/>
+</authorList>
+<dbReference type="PubMed" id="18407956"/>
+<dbReference type="DOI" id="10.1074/mcp.m700468-mcp200"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293; THR-341 AND SER-343</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<reference key="9">
+<citation type="journal article" date="2009" name="Science" volume="325" first="1682" last="1686">
+<title>Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution.</title>
+<authorList>
+<person name="Holt L.J."/>
+<person name="Tuch B.B."/>
+<person name="Villen J."/>
+<person name="Johnson A.D."/>
+<person name="Gygi S.P."/>
+<person name="Morgan D.O."/>
+</authorList>
+<dbReference type="PubMed" id="19779198"/>
+<dbReference type="DOI" id="10.1126/science.1172867"/>
+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-341</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Membrane</location>
+<topology>Multi-pass membrane protein</topology>
+</subcellularLocation>
+</comment>
+<comment type="miscellaneous">
+<text evidence="3">Present with 1950 molecules/cell in log phase SD medium.</text>
+</comment>
+<comment type="similarity">
+<text evidence="4">Belongs to the archaeal/bacterial/fungal opsin family.</text>
+</comment>
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+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-02-10" version="120">
+<accession>Q92392</accession>
+<accession>D6W1W4</accession>
+<name>YO11A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-OL Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
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+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-OL</name>
+<name type="synonym">YOLWTy1-1 GAG</name>
+<name type="ordered locus">YOL103W-A</name>
+<name type="ORF">HRA440</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1995" name="Yeast" volume="11" first="1069" last="1075">
+<title>Sequence analysis of a 44 kb DNA fragment of yeast chromosome XV including the Ty1-H3 retrotransposon, the suf1(+) frameshift suppressor gene for tRNA-Gly, the yeast transfer RNA-Thr-1a and a delta element.</title>
+<authorList>
+<person name="Vandenbol M."/>
+<person name="Durand P."/>
+<person name="Portetelle D."/>
+<person name="Hilger F."/>
+</authorList>
+<dbReference type="PubMed" id="7502582"/>
+<dbReference type="DOI" id="10.1002/yea.320111108"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+</reference>
+<reference key="2">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="98" last="102">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.</title>
+<authorList>
+<person name="Dujon B."/>
+<person name="Albermann K."/>
+<person name="Aldea M."/>
+<person name="Alexandraki D."/>
+<person name="Ansorge W."/>
+<person name="Arino J."/>
+<person name="Benes V."/>
+<person name="Bohn C."/>
+<person name="Bolotin-Fukuhara M."/>
+<person name="Bordonne R."/>
+<person name="Boyer J."/>
+<person name="Camasses A."/>
+<person name="Casamayor A."/>
+<person name="Casas C."/>
+<person name="Cheret G."/>
+<person name="Cziepluch C."/>
+<person name="Daignan-Fornier B."/>
+<person name="Dang V.-D."/>
+<person name="de Haan M."/>
+<person name="Delius H."/>
+<person name="Durand P."/>
+<person name="Fairhead C."/>
+<person name="Feldmann H."/>
+<person name="Gaillon L."/>
+<person name="Galisson F."/>
+<person name="Gamo F.-J."/>
+<person name="Gancedo C."/>
+<person name="Goffeau A."/>
+<person name="Goulding S.E."/>
+<person name="Grivell L.A."/>
+<person name="Habbig B."/>
+<person name="Hand N.J."/>
+<person name="Hani J."/>
+<person name="Hattenhorst U."/>
+<person name="Hebling U."/>
+<person name="Hernando Y."/>
+<person name="Herrero E."/>
+<person name="Heumann K."/>
+<person name="Hiesel R."/>
+<person name="Hilger F."/>
+<person name="Hofmann B."/>
+<person name="Hollenberg C.P."/>
+<person name="Hughes B."/>
+<person name="Jauniaux J.-C."/>
+<person name="Kalogeropoulos A."/>
+<person name="Katsoulou C."/>
+<person name="Kordes E."/>
+<person name="Lafuente M.J."/>
+<person name="Landt O."/>
+<person name="Louis E.J."/>
+<person name="Maarse A.C."/>
+<person name="Madania A."/>
+<person name="Mannhaupt G."/>
+<person name="Marck C."/>
+<person name="Martin R.P."/>
+<person name="Mewes H.-W."/>
+<person name="Michaux G."/>
+<person name="Paces V."/>
+<person name="Parle-McDermott A.G."/>
+<person name="Pearson B.M."/>
+<person name="Perrin A."/>
+<person name="Pettersson B."/>
+<person name="Poch O."/>
+<person name="Pohl T.M."/>
+<person name="Poirey R."/>
+<person name="Portetelle D."/>
+<person name="Pujol A."/>
+<person name="Purnelle B."/>
+<person name="Ramezani Rad M."/>
+<person name="Rechmann S."/>
+<person name="Schwager C."/>
+<person name="Schweizer M."/>
+<person name="Sor F."/>
+<person name="Sterky F."/>
+<person name="Tarassov I.A."/>
+<person name="Teodoru C."/>
+<person name="Tettelin H."/>
+<person name="Thierry A."/>
+<person name="Tobiasch E."/>
+<person name="Tzermia M."/>
+<person name="Uhlen M."/>
+<person name="Unseld M."/>
+<person name="Valens M."/>
+<person name="Vandenbol M."/>
+<person name="Vetter I."/>
+<person name="Vlcek C."/>
+<person name="Voet M."/>
+<person name="Volckaert G."/>
+<person name="Voss H."/>
+<person name="Wambutt R."/>
+<person name="Wedler H."/>
+<person name="Wiemann S."/>
+<person name="Winsor B."/>
+<person name="Wolfe K.H."/>
+<person name="Zollner A."/>
+<person name="Zumstein E."/>
+<person name="Kleine K."/>
+</authorList>
+<dbReference type="PubMed" id="9169874"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>Q92392-1</id>
+<name>Transposon Ty1-OL Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>Q12273-1</id>
+<name>Transposon Ty1-OL Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-OL is a weakly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-OL Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="Z48149">
+<property type="protein sequence ID" value="CAA88157.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z74845">
+<property type="protein sequence ID" value="CAA99117.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="Z74846">
+<property type="protein sequence ID" value="CAA99121.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006948">
+<property type="protein sequence ID" value="DAA10680.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S51894">
+<property type="entry name" value="S51894"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058182.1">
+<molecule id="Q92392-1"/>
+<property type="nucleotide sequence ID" value="NM_001184383.1"/>
+</dbReference>
+<dbReference type="SMR" id="Q92392"/>
+<dbReference type="BioGRID" id="34298">
+<property type="interactions" value="12"/>
+</dbReference>
+<dbReference type="IntAct" id="Q92392">
+<property type="interactions" value="3"/>
+</dbReference>
+<dbReference type="CarbonylDB" id="Q92392"/>
+<dbReference type="iPTMnet" id="Q92392"/>
+<dbReference type="PaxDb" id="Q92392"/>
+<dbReference type="GeneID" id="854048"/>
+<dbReference type="KEGG" id="sce:YOL103W-A"/>
+<dbReference type="SGD" id="S000007349">
+<property type="gene designation" value="YOL103W-A"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YOL103W-A"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="InParanoid" id="Q92392"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XV"/>
+</dbReference>
+<dbReference type="RNAct" id="Q92392">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-OL Gag polyprotein" id="PRO_0000279158">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279159" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000279160" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11884596"/>
+</source>
+</evidence>
+<sequence length="440" mass="49005" checksum="4E3D83778FDFB2FB" modified="1997-02-01" version="1">MESQQLSNYPQISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIINRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2007-03-06" modified="2021-04-07" version="146">
+<accession>Q12414</accession>
+<accession>D6W3B2</accession>
+<name>YP11B_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-PL Gag-Pol polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-Pol-p199</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>TY1A-TY1B</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 TYA-TYB polyprotein</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p190</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Ty1 protease</fullName>
+<shortName>PR</shortName>
+<ecNumber>3.4.23.-</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p20</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p23</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Integrase</fullName>
+<shortName>IN</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p71</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p84</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p90</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Reverse transcriptase/ribonuclease H</fullName>
+<shortName>RT</shortName>
+<shortName>RT-RH</shortName>
+<ecNumber>2.7.7.49</ecNumber>
+<ecNumber>2.7.7.7</ecNumber>
+<ecNumber>3.1.26.4</ecNumber>
+</recommendedName>
+<alternativeName>
+<fullName>Pol-p63</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p60</fullName>
+</alternativeName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1B-PL</name>
+<name type="synonym">YPLWTy1-1 POL</name>
+<name type="ordered locus">YPL257W-B</name>
+<name type="ORF">P0729</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="103" last="105">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XVI.</title>
+<authorList>
+<person name="Bussey H."/>
+<person name="Storms R.K."/>
+<person name="Ahmed A."/>
+<person name="Albermann K."/>
+<person name="Allen E."/>
+<person name="Ansorge W."/>
+<person name="Araujo R."/>
+<person name="Aparicio A."/>
+<person name="Barrell B.G."/>
+<person name="Badcock K."/>
+<person name="Benes V."/>
+<person name="Botstein D."/>
+<person name="Bowman S."/>
+<person name="Brueckner M."/>
+<person name="Carpenter J."/>
+<person name="Cherry J.M."/>
+<person name="Chung E."/>
+<person name="Churcher C.M."/>
+<person name="Coster F."/>
+<person name="Davis K."/>
+<person name="Davis R.W."/>
+<person name="Dietrich F.S."/>
+<person name="Delius H."/>
+<person name="DiPaolo T."/>
+<person name="Dubois E."/>
+<person name="Duesterhoeft A."/>
+<person name="Duncan M."/>
+<person name="Floeth M."/>
+<person name="Fortin N."/>
+<person name="Friesen J.D."/>
+<person name="Fritz C."/>
+<person name="Goffeau A."/>
+<person name="Hall J."/>
+<person name="Hebling U."/>
+<person name="Heumann K."/>
+<person name="Hilbert H."/>
+<person name="Hillier L.W."/>
+<person name="Hunicke-Smith S."/>
+<person name="Hyman R.W."/>
+<person name="Johnston M."/>
+<person name="Kalman S."/>
+<person name="Kleine K."/>
+<person name="Komp C."/>
+<person name="Kurdi O."/>
+<person name="Lashkari D."/>
+<person name="Lew H."/>
+<person name="Lin A."/>
+<person name="Lin D."/>
+<person name="Louis E.J."/>
+<person name="Marathe R."/>
+<person name="Messenguy F."/>
+<person name="Mewes H.-W."/>
+<person name="Mirtipati S."/>
+<person name="Moestl D."/>
+<person name="Mueller-Auer S."/>
+<person name="Namath A."/>
+<person name="Nentwich U."/>
+<person name="Oefner P."/>
+<person name="Pearson D."/>
+<person name="Petel F.X."/>
+<person name="Pohl T.M."/>
+<person name="Purnelle B."/>
+<person name="Rajandream M.A."/>
+<person name="Rechmann S."/>
+<person name="Rieger M."/>
+<person name="Riles L."/>
+<person name="Roberts D."/>
+<person name="Schaefer M."/>
+<person name="Scharfe M."/>
+<person name="Scherens B."/>
+<person name="Schramm S."/>
+<person name="Schroeder M."/>
+<person name="Sdicu A.-M."/>
+<person name="Tettelin H."/>
+<person name="Urrestarazu L.A."/>
+<person name="Ushinsky S."/>
+<person name="Vierendeels F."/>
+<person name="Vissers S."/>
+<person name="Voss H."/>
+<person name="Walsh S.V."/>
+<person name="Wambutt R."/>
+<person name="Wang Y."/>
+<person name="Wedler E."/>
+<person name="Wedler H."/>
+<person name="Winnett E."/>
+<person name="Zhong W.-W."/>
+<person name="Zollner A."/>
+<person name="Vo D.H."/>
+<person name="Hani J."/>
+</authorList>
+<dbReference type="PubMed" id="9169875"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="4">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="269" last="287">
+<title>Reverse transcriptase and integrase of the Saccharomyces cerevisiae Ty1 element.</title>
+<authorList>
+<person name="Wilhelm F.-X."/>
+<person name="Wilhelm M."/>
+<person name="Gabriel A."/>
+</authorList>
+<dbReference type="PubMed" id="16093680"/>
+<dbReference type="DOI" id="10.1159/000084960"/>
+</citation>
+<scope>REVIEW</scope>
+<scope>DOMAINS</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">The aspartyl protease (PR) mediates the proteolytic cleavages of the Gag and Gag-Pol polyproteins after assembly of the VLP.</text>
+</comment>
+<comment type="function">
+<text evidence="1">Reverse transcriptase/ribonuclease H (RT) is a multifunctional enzyme that catalyzes the conversion of the retro-elements RNA genome into dsDNA within the VLP. The enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes during plus-strand synthesis and hydrolyzes RNA primers. The conversion leads to a linear dsDNA copy of the retrotransposon that includes long terminal repeats (LTRs) at both ends (By similarity).</text>
+</comment>
+<comment type="function">
+<text evidence="1">Integrase (IN) targets the VLP to the nucleus, where a subparticle preintegration complex (PIC) containing at least integrase and the newly synthesized dsDNA copy of the retrotransposon must transit the nuclear membrane. Once in the nucleus, integrase performs the integration of the dsDNA into the host genome (By similarity).</text>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.49"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)</text>
+<dbReference type="Rhea" id="RHEA:22508"/>
+<dbReference type="Rhea" id="RHEA-COMP:11130"/>
+<dbReference type="Rhea" id="RHEA-COMP:11131"/>
+<dbReference type="ChEBI" id="CHEBI:33019"/>
+<dbReference type="ChEBI" id="CHEBI:61560"/>
+<dbReference type="ChEBI" id="CHEBI:83828"/>
+<dbReference type="EC" id="2.7.7.7"/>
+</reaction>
+</comment>
+<comment type="catalytic activity">
+<reaction>
+<text>Endonucleolytic cleavage to 5'-phosphomonoester.</text>
+<dbReference type="EC" id="3.1.26.4"/>
+</reaction>
+</comment>
+<comment type="subunit">
+<text evidence="1">The capsid protein forms a homotrimer, from which the VLPs are assembled. The protease is a homodimer, whose active site consists of two apposed aspartic acid residues (By similarity).</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Cytoplasm</location>
+</subcellularLocation>
+<subcellularLocation>
+<location evidence="1">Nucleus</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>Q12414-1</id>
+<name>Transposon Ty1-PL Gag-Pol polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0CX73-1</id>
+<name>Transposon Ty1-PL Gag polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">Integrase core domain contains the D-x(n)-D-x(35)-E motif, named for the phylogenetically conserved glutamic acid and aspartic acid residues and the invariant 35 amino acid spacing between the second and third acidic residues. Each acidic residue of the D,D(35)E motif is independently essential for the 3'-processing and strand transfer activities of purified integrase protein (By similarity).</text>
+</comment>
+<comment type="PTM">
+<text evidence="1">Initially, virus-like particles (VLPs) are composed of the structural unprocessed proteins Gag and Gag-Pol, and contain also the host initiator methionine tRNA (tRNA(i)-Met) which serves as a primer for minus-strand DNA synthesis, and a dimer of genomic Ty RNA. Processing of the polyproteins occurs within the particle and proceeds by an ordered pathway, called maturation. First, the protease (PR) is released by autocatalytic cleavage of the Gag-Pol polyprotein yielding capsid protein p45 and a Pol-p154 precursor protein. This cleavage is a prerequisite for subsequent processing of Pol-p154 at the remaining sites to release the mature structural and catalytic proteins. Maturation takes place prior to the RT reaction and is required to produce transposition-competent VLPs (By similarity).</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-PL Gag-Pol polyprotein</molecule>
+<text>Produced by +1 ribosomal frameshifting between codon Leu-435 and Gly-436 of the YPL257W-A ORF.</text>
+</comment>
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+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
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+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006949">
+<property type="protein sequence ID" value="DAA11178.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S69979">
+<property type="entry name" value="S69979"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058189.1">
+<molecule id="Q12414-1"/>
+<property type="nucleotide sequence ID" value="NM_001184392.2"/>
+</dbReference>
+<dbReference type="SMR" id="Q12414"/>
+<dbReference type="BioGRID" id="35905">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-8957N"/>
+<dbReference type="IntAct" id="Q12414">
+<property type="interactions" value="1"/>
+</dbReference>
+<dbReference type="iPTMnet" id="Q12414"/>
+<dbReference type="MaxQB" id="Q12414"/>
+<dbReference type="PaxDb" id="Q12414"/>
+<dbReference type="PRIDE" id="Q12414"/>
+<dbReference type="GeneID" id="855817"/>
+<dbReference type="KEGG" id="sce:YPL257W-B"/>
+<dbReference type="SGD" id="S000007358">
+<property type="gene designation" value="YPL257W-B"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YPL257W-B"/>
+<dbReference type="eggNOG" id="KOG0017">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_244151_0_0_1"/>
+<dbReference type="InParanoid" id="Q12414"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XVI"/>
+</dbReference>
+<dbReference type="RNAct" id="Q12414">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005634">
+<property type="term" value="C:nucleus"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004190">
+<property type="term" value="F:aspartic-type endopeptidase activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005524">
+<property type="term" value="F:ATP binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003677">
+<property type="term" value="F:DNA binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003887">
+<property type="term" value="F:DNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0046872">
+<property type="term" value="F:metal ion binding"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0008233">
+<property type="term" value="F:peptidase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004540">
+<property type="term" value="F:ribonuclease activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003964">
+<property type="term" value="F:RNA-directed DNA polymerase activity"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0004523">
+<property type="term" value="F:RNA-DNA hybrid ribonuclease activity"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-EC"/>
+</dbReference>
+<dbReference type="GO" id="GO:0015074">
+<property type="term" value="P:DNA integration"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0006310">
+<property type="term" value="P:DNA recombination"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-KW"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="Gene3D" id="3.30.420.10">
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001969">
+<property type="entry name" value="Aspartic_peptidase_AS"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR043502">
+<property type="entry name" value="DNA/RNA_pol_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR001584">
+<property type="entry name" value="Integrase_cat-core"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR012337">
+<property type="entry name" value="RNaseH-like_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR036397">
+<property type="entry name" value="RNaseH_sf"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR013103">
+<property type="entry name" value="RVT_2"/>
+</dbReference>
+<dbReference type="Pfam" id="PF00665">
+<property type="entry name" value="rve"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF07727">
+<property type="entry name" value="RVT_2"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF53098">
+<property type="entry name" value="SSF53098"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="SUPFAM" id="SSF56672">
+<property type="entry name" value="SSF56672"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS00141">
+<property type="entry name" value="ASP_PROTEASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<dbReference type="PROSITE" id="PS50994">
+<property type="entry name" value="INTEGRASE"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="inferred from homology"/>
+<keyword id="KW-0064">Aspartyl protease</keyword>
+<keyword id="KW-0067">ATP-binding</keyword>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0229">DNA integration</keyword>
+<keyword id="KW-0233">DNA recombination</keyword>
+<keyword id="KW-0238">DNA-binding</keyword>
+<keyword id="KW-0239">DNA-directed DNA polymerase</keyword>
+<keyword id="KW-0255">Endonuclease</keyword>
+<keyword id="KW-0378">Hydrolase</keyword>
+<keyword id="KW-0460">Magnesium</keyword>
+<keyword id="KW-0479">Metal-binding</keyword>
+<keyword id="KW-0511">Multifunctional enzyme</keyword>
+<keyword id="KW-0540">Nuclease</keyword>
+<keyword id="KW-0547">Nucleotide-binding</keyword>
+<keyword id="KW-0548">Nucleotidyltransferase</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-0645">Protease</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0695">RNA-directed DNA polymerase</keyword>
+<keyword id="KW-0808">Transferase</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<keyword id="KW-0815">Transposition</keyword>
+<keyword id="KW-1188">Viral release from host cell</keyword>
+<keyword id="KW-0917">Virion maturation</keyword>
+<keyword id="KW-0862">Zinc</keyword>
+<keyword id="KW-0863">Zinc-finger</keyword>
+<feature type="chain" description="Transposon Ty1-PL Gag-Pol polyprotein" id="PRO_0000279169">
+<location>
+<begin position="1"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000279170" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="chain" description="Ty1 protease" id="PRO_0000279171" evidence="1">
+<location>
+<begin position="402"/>
+<end position="582"/>
+</location>
+</feature>
+<feature type="chain" description="Integrase" id="PRO_0000279172" evidence="1">
+<location>
+<begin position="583"/>
+<end position="1217"/>
+</location>
+</feature>
+<feature type="chain" description="Reverse transcriptase/ribonuclease H" id="PRO_0000279173" evidence="1">
+<location>
+<begin position="1218"/>
+<end position="1755"/>
+</location>
+</feature>
+<feature type="domain" description="Integrase catalytic" evidence="3">
+<location>
+<begin position="660"/>
+<end position="835"/>
+</location>
+</feature>
+<feature type="domain" description="Reverse transcriptase Ty1/copia-type">
+<location>
+<begin position="1338"/>
+<end position="1476"/>
+</location>
+</feature>
+<feature type="domain" description="RNase H Ty1/copia-type">
+<location>
+<begin position="1610"/>
+<end position="1752"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="region of interest" description="Integrase-type zinc finger-like">
+<location>
+<begin position="583"/>
+<end position="640"/>
+</location>
+</feature>
+<feature type="short sequence motif" description="Bipartite nuclear localization signal" evidence="1">
+<location>
+<begin position="1178"/>
+<end position="1212"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="active site" description="For protease activity; shared with dimeric partner" evidence="4">
+<location>
+<position position="461"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="671"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for integrase activity" evidence="3">
+<location>
+<position position="736"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1346"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1427"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for reverse transcriptase activity" evidence="3">
+<location>
+<position position="1428"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1610"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1652"/>
+</location>
+</feature>
+<feature type="metal ion-binding site" description="Magnesium; catalytic; for RNase H activity" evidence="3">
+<location>
+<position position="1685"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="582"/>
+<end position="583"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="1217"/>
+<end position="1218"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q99231"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU00457"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000255">
+<source>
+<dbReference type="PROSITE-ProRule" id="PRU10094"/>
+</source>
+</evidence>
+<sequence length="1755" mass="198576" checksum="C1D766C7C6070422" modified="1996-11-01" version="1">MESQQLSQHSPISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLGQELTESTVNHTNHSDDELPGHLLLDSGASRTLIRSAHHIHSASSNPDINVVDAQKRNIPINAIGDLQFHFQDNTKTSIKVLHTPNIAYDLLSLNELAAVDITACFTKNVLERSDGTVLAPIVKYGDFYWVSKKYLLPSNISVPTINNVHTSESTRKYPYPFIHRMLAHANAQTIRYSLKNNTITYFNESDVDWSSAIDYQCPDCLIGKSTKHRHIKGSRLKYQNSYEPFQYLHTDIFGPVHNLPNSAPSYFISFTDETTKFRWVYPLHDRREDSILDVFTTILAFIKNQFQASVLVIQMDRGSEYTNRTLHKFLEKNGITPCYTTTADSRAHGVAERLNRTLLDDCRTQLQCSGLPNHLWFSAIEFSTIVRNSLASPKSKKSARQHAGLAGLDISTLLPFGQPVIVNDHNPNSKIHPRGIPGYALHPSRNSYGYIIYLPSLKKTVDTTNYVILQGKESRLDQFNYDALTFDEDLNRLTASYHSFIASNEIQESNDLNIESDHDFQSDIELHPEQPRNVLSKAVSPTDSTPPSTHTEDSKRVSKTNIRAPREVDPNISESNILPSKKRSSTPQISNIESTGSGGMHKLNVPLLAPMSQSNTHESSHASKSKDFRHSDSYSENETNHTNVPISSTGGTNNKTVPQISDQETEKRIIHRSPSIDASPPENNSSHNIVPIKTPTTVSEQNTEESIIADLPLPDLPPESPTEFPDPFKELPPINSRQTNSSLGGIGDSNAYTTINSKKRSLEDNETEIKVSRDTWNTKNMRSLEPPRSKKRIHLIAAVKAVKSIKPIRTTLRYDEAITYNKDIKEKEKYIEAYHKEVNQLLKMKTWDTDEYYDRKEIDPKRVINSMFIFNKKRDGTHKARFVARGDIQHPDTYDSGMQSNTVHHYALMTSLSLALDNNYYITQLDISSAYLYADIKEELYIRPPPHLGMNDKLIRLKKSLYGLKQSGANWYETIKSYLIKQCGMEEVRGWSCVFKNSQVTICLFVDDMILFSKDLNANKKIITTLKKQYDTKIINLGESDNEIQYDILGLEIKYQRGKYMKLGMENSLTEKIPKLNVPLNPKGRKLSAPGQPGLYIDQDELEIDEDEYKEKVHEMQKLIGLASYVGYKFRFDLLYYINTLAQHILFPSRQVLDMTYELIQFMWDTRDKQLIWHKNKPTEPDNKLVAISDASYGNQPYYKSQIGNIYLLNGKVIGGKSTKASLTCTSTTEAEIHAISESVPLLNNLSYLIQELNKKPIIKGLLTDSRSTISIIKSTNEEKFRNRFFGTKAMRLRDEVSGNNLYVYYIETKKNIADVMTKPLPIKTFKLLTNKWIH</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="1993-07-01" modified="2021-04-07" version="163">
+<accession>P31111</accession>
+<accession>D6VSR5</accession>
+<name>ZIP1_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Synaptonemal complex protein ZIP1</fullName>
+</recommendedName>
+</protein>
+<gene>
+<name type="primary">ZIP1</name>
+<name type="ordered locus">YDR285W</name>
+<name type="ORF">D9819.9</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1993" name="Cell" volume="72" first="365" last="378">
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+<authorList>
+<person name="Sym M."/>
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+</authorList>
+<dbReference type="PubMed" id="7916652"/>
+<dbReference type="DOI" id="10.1016/0092-8674(93)90114-6"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>BR1824-3B</strain>
+</source>
+</reference>
+<reference key="2">
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+</authorList>
+<dbReference type="PubMed" id="9169867"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
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+<dbReference type="PubMed" id="24374639"/>
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+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
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+<dbReference type="PubMed" id="14562106"/>
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+</citation>
+<scope>LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS]</scope>
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+<reference key="5">
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+<dbReference type="PubMed" id="18407956"/>
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+</citation>
+<scope>PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-481</scope>
+<scope>IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]</scope>
+</reference>
+<comment type="function">
+<text>Required for meiotic chromosome synapsis and cell cycle progression. May act as a molecular zipper to bring homologous chromosomes in close apposition. ZIP1 may encode the transverse filaments of the synaptonemal complex.</text>
+</comment>
+<comment type="interaction">
+<interactant intactId="EBI-29645">
+<id>P31111</id>
+</interactant>
+<interactant intactId="EBI-30044">
+<id>Q06032</id>
+<label>CST9</label>
+</interactant>
+<organismsDiffer>false</organismsDiffer>
+<experiments>3</experiments>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location>Nucleus</location>
+</subcellularLocation>
+<subcellularLocation>
+<location>Chromosome</location>
+</subcellularLocation>
+<text>Synapsed meiotic chromosomes.</text>
+</comment>
+<comment type="miscellaneous">
+<text evidence="2">Present with 391 molecules/cell in log phase SD medium.</text>
+</comment>
+<dbReference type="EMBL" id="L06487">
+<property type="protein sequence ID" value="AAA35239.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="U51031">
+<property type="protein sequence ID" value="AAB64474.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006938">
+<property type="protein sequence ID" value="DAA12125.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S70115">
+<property type="entry name" value="S70115"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_010571.1">
+<property type="nucleotide sequence ID" value="NM_001180593.1"/>
+</dbReference>
+<dbReference type="SMR" id="P31111"/>
+<dbReference type="BioGRID" id="32338">
+<property type="interactions" value="97"/>
+</dbReference>
+<dbReference type="ComplexPortal" id="CPX-1387">
+<property type="entry name" value="Synaptonemal complex"/>
+</dbReference>
+<dbReference type="DIP" id="DIP-1240N"/>
+<dbReference type="IntAct" id="P31111">
+<property type="interactions" value="4"/>
+</dbReference>
+<dbReference type="MINT" id="P31111"/>
+<dbReference type="STRING" id="4932.YDR285W"/>
+<dbReference type="iPTMnet" id="P31111"/>
+<dbReference type="PaxDb" id="P31111"/>
+<dbReference type="PRIDE" id="P31111"/>
+<dbReference type="EnsemblFungi" id="YDR285W_mRNA">
+<property type="protein sequence ID" value="YDR285W"/>
+<property type="gene ID" value="YDR285W"/>
+</dbReference>
+<dbReference type="GeneID" id="851879"/>
+<dbReference type="KEGG" id="sce:YDR285W"/>
+<dbReference type="SGD" id="S000002693">
+<property type="gene designation" value="ZIP1"/>
+</dbReference>
+<dbReference type="VEuPathDB" id="FungiDB:YDR285W"/>
+<dbReference type="eggNOG" id="ENOG502R6M6">
+<property type="taxonomic scope" value="Eukaryota"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_341332_0_0_1"/>
+<dbReference type="InParanoid" id="P31111"/>
+<dbReference type="OMA" id="WKNENEE"/>
+<dbReference type="PRO" id="PR:P31111"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome IV"/>
+</dbReference>
+<dbReference type="RNAct" id="P31111">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000775">
+<property type="term" value="C:chromosome, centromeric region"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000795">
+<property type="term" value="C:synaptonemal complex"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000802">
+<property type="term" value="C:transverse filament"/>
+<property type="evidence" value="ECO:0000314"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032184">
+<property type="term" value="F:SUMO polymer binding"/>
+<property type="evidence" value="ECO:0000353"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0007129">
+<property type="term" value="P:homologous chromosome pairing at meiosis"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0045128">
+<property type="term" value="P:negative regulation of reciprocal meiotic recombination"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0033235">
+<property type="term" value="P:positive regulation of protein sumoylation"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:1990166">
+<property type="term" value="P:protein localization to site of double-strand break"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0007131">
+<property type="term" value="P:reciprocal meiotic recombination"/>
+<property type="evidence" value="ECO:0000315"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<proteinExistence type="evidence at protein level"/>
+<keyword id="KW-0158">Chromosome</keyword>
+<keyword id="KW-0175">Coiled coil</keyword>
+<keyword id="KW-0469">Meiosis</keyword>
+<keyword id="KW-0539">Nucleus</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<feature type="chain" description="Synaptonemal complex protein ZIP1" id="PRO_0000066584">
+<location>
+<begin position="1"/>
+<end position="875"/>
+</location>
+</feature>
+<feature type="coiled-coil region" evidence="1">
+<location>
+<begin position="177"/>
+<end position="333"/>
+</location>
+</feature>
+<feature type="coiled-coil region" evidence="1">
+<location>
+<begin position="397"/>
+<end position="438"/>
+</location>
+</feature>
+<feature type="coiled-coil region" evidence="1">
+<location>
+<begin position="456"/>
+<end position="752"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="4">
+<location>
+<position position="481"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 1; AAA35239." ref="1" evidence="3">
+<original>T</original>
+<variation>A</variation>
+<location>
+<position position="55"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000255"/>
+<evidence key="2" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="14562106"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000305"/>
+<evidence key="4" type="ECO:0007744">
+<source>
+<dbReference type="PubMed" id="18407956"/>
+</source>
+</evidence>
+<sequence length="875" mass="100035" checksum="674F12625CD9DDFD" modified="1996-10-01" version="2">MSNFFRDSSMGFKPRPNIFAKLRVRDVDSDSSANTVVENSSNCLDVGSSIEGDDTFKKPHKTSTEQELITSMSLSQRNHGYSDDMEIGSPKKTTSTDQYNRILKNDVAAIENDTDEDFEITEVREVSEGVAKETKESHGDPNDSETTLKDSKMHEYTMTNGKAPLHTSINNSSTSSNDVLLEAFTNTQRICSNLKQELQKQQQDNAKLKVRLQSYASNSDKINEKVGKYKSCLETLQERIATLTSHKNNQETKLKDLRQNHQLYQRRISGFKTSIENLNKTINDLGKNKKEADAELMKKGKEIEYLKRELDDCSGQLSEEKIKNSSLIQEMGKNREEMIKSIENFFSEDKAHHLLQFNKFEERVHDLFEKKLQKHFDVAKDTLNVGLRNTTVELSSNTETMLKQQYEDIKENLEQKMSSSKDEMAKTINELSVTQKGLIMGVQEELLTSSGNIQTALVSEMNNTRQELLDDASQTAKNYASLENLVKAYKAEIVQSNEYEERIKHLESERSTLSSQKNQIISSLGTKEAQYEDLVKKLEAKNIEISQISGKEQSLTEKNENLSNELKKVQDQLEKLNNLNITTKSNYENKISSQNEIVKALVSENDTLKQRIQQLVEIKENEQKDHTTKLEAFQKNNEQLQKLNVEVVQLKAHELELEEQNRHLKNCLEKKETGVEESLSDVKTLKQQVIVLKSEKQDITAEKLELQDNLESLEEVTKNLQQKVQSQKRELEQKIKELEEIKNHKRNEPSKKGTQNFTKPSDSPKKNATTSNLFPNNSAAIHSPMKKCPKVDHISKSRINSSKETSKFNDEFDLSSSSNDDLELTNPSPIQIKPVRGKIKKGSNCMKPPISSRKKLLLVEDEDQSLKISKKRRRK</sequence>
+</entry>
+<entry dataset="Swiss-Prot" created="2011-06-28" modified="2020-12-02" version="60">
+<accession>P0CX75</accession>
+<accession>D6VWK0</accession>
+<accession>P47097</accession>
+<accession>Q66R50</accession>
+<name>YL13A_YEAST</name>
+<protein>
+<recommendedName>
+<fullName>Transposon Ty1-LR3 Gag polyprotein</fullName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p49</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>Transposon Ty1 protein A</fullName>
+<shortName>TY1A</shortName>
+<shortName>TYA</shortName>
+</alternativeName>
+<alternativeName>
+<fullName>p58</fullName>
+</alternativeName>
+<component>
+<recommendedName>
+<fullName>Capsid protein</fullName>
+<shortName>CA</shortName>
+</recommendedName>
+<alternativeName>
+<fullName>Gag-p45</fullName>
+</alternativeName>
+<alternativeName>
+<fullName>p54</fullName>
+</alternativeName>
+</component>
+<component>
+<recommendedName>
+<fullName>Gag-p4</fullName>
+</recommendedName>
+</component>
+</protein>
+<gene>
+<name type="primary">TY1A-LR3</name>
+<name type="synonym">YLRWTy1-3 GAG</name>
+<name type="ordered locus">YLR227W-A</name>
+<name type="ORF">L8083.11</name>
+</gene>
+<organism>
+<name type="scientific">Saccharomyces cerevisiae (strain ATCC 204508 / S288c)</name>
+<name type="common">Baker's yeast</name>
+<dbReference type="NCBI Taxonomy" id="559292"/>
+<lineage>
+<taxon>Eukaryota</taxon>
+<taxon>Fungi</taxon>
+<taxon>Dikarya</taxon>
+<taxon>Ascomycota</taxon>
+<taxon>Saccharomycotina</taxon>
+<taxon>Saccharomycetes</taxon>
+<taxon>Saccharomycetales</taxon>
+<taxon>Saccharomycetaceae</taxon>
+<taxon>Saccharomyces</taxon>
+</lineage>
+</organism>
+<reference key="1">
+<citation type="journal article" date="1997" name="Nature" volume="387" first="87" last="90">
+<title>The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.</title>
+<authorList>
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+<person name="Hani J."/>
+<person name="Hoheisel J.D."/>
+</authorList>
+<dbReference type="PubMed" id="9169871"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="2">
+<citation type="journal article" date="2014" name="G3 (Bethesda)" volume="4" first="389" last="398">
+<title>The reference genome sequence of Saccharomyces cerevisiae: Then and now.</title>
+<authorList>
+<person name="Engel S.R."/>
+<person name="Dietrich F.S."/>
+<person name="Fisk D.G."/>
+<person name="Binkley G."/>
+<person name="Balakrishnan R."/>
+<person name="Costanzo M.C."/>
+<person name="Dwight S.S."/>
+<person name="Hitz B.C."/>
+<person name="Karra K."/>
+<person name="Nash R.S."/>
+<person name="Weng S."/>
+<person name="Wong E.D."/>
+<person name="Lloyd P."/>
+<person name="Skrzypek M.S."/>
+<person name="Miyasato S.R."/>
+<person name="Simison M."/>
+<person name="Cherry J.M."/>
+</authorList>
+<dbReference type="PubMed" id="24374639"/>
+<dbReference type="DOI" id="10.1534/g3.113.008995"/>
+</citation>
+<scope>GENOME REANNOTATION</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="3">
+<citation type="journal article" date="2007" name="Genome Res." volume="17" first="536" last="543">
+<title>Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.</title>
+<authorList>
+<person name="Hu Y."/>
+<person name="Rolfs A."/>
+<person name="Bhullar B."/>
+<person name="Murthy T.V.S."/>
+<person name="Zhu C."/>
+<person name="Berger M.F."/>
+<person name="Camargo A.A."/>
+<person name="Kelley F."/>
+<person name="McCarron S."/>
+<person name="Jepson D."/>
+<person name="Richardson A."/>
+<person name="Raphael J."/>
+<person name="Moreira D."/>
+<person name="Taycher E."/>
+<person name="Zuo D."/>
+<person name="Mohr S."/>
+<person name="Kane M.F."/>
+<person name="Williamson J."/>
+<person name="Simpson A.J.G."/>
+<person name="Bulyk M.L."/>
+<person name="Harlow E."/>
+<person name="Marsischky G."/>
+<person name="Kolodner R.D."/>
+<person name="LaBaer J."/>
+</authorList>
+<dbReference type="PubMed" id="17322287"/>
+<dbReference type="DOI" id="10.1101/gr.6037607"/>
+</citation>
+<scope>NUCLEOTIDE SEQUENCE [GENOMIC DNA]</scope>
+<source>
+<strain>ATCC 204508 / S288c</strain>
+</source>
+</reference>
+<reference key="4">
+<citation type="journal article" date="1998" name="Genome Res." volume="8" first="464" last="478">
+<title>Transposable elements and genome organization: a comprehensive survey of retrotransposons revealed by the complete Saccharomyces cerevisiae genome sequence.</title>
+<authorList>
+<person name="Kim J.M."/>
+<person name="Vanguri S."/>
+<person name="Boeke J.D."/>
+<person name="Gabriel A."/>
+<person name="Voytas D.F."/>
+</authorList>
+<dbReference type="PubMed" id="9582191"/>
+<dbReference type="DOI" id="10.1101/gr.8.5.464"/>
+</citation>
+<scope>NOMENCLATURE</scope>
+</reference>
+<reference key="5">
+<citation type="journal article" date="2002" name="Mol. Cell. Biol." volume="22" first="2078" last="2088">
+<title>Differential effects of chromatin and Gcn4 on the 50-fold range of expression among individual yeast Ty1 retrotransposons.</title>
+<authorList>
+<person name="Morillon A."/>
+<person name="Benard L."/>
+<person name="Springer M."/>
+<person name="Lesage P."/>
+</authorList>
+<dbReference type="PubMed" id="11884596"/>
+<dbReference type="DOI" id="10.1128/mcb.22.7.2078-2088.2002"/>
+</citation>
+<scope>INDUCTION</scope>
+</reference>
+<reference key="6">
+<citation type="journal article" date="2005" name="Cytogenet. Genome Res." volume="110" first="70" last="90">
+<title>Happy together: the life and times of Ty retrotransposons and their hosts.</title>
+<authorList>
+<person name="Lesage P."/>
+<person name="Todeschini A.L."/>
+</authorList>
+<dbReference type="PubMed" id="16093660"/>
+<dbReference type="DOI" id="10.1159/000084940"/>
+</citation>
+<scope>REVIEW</scope>
+</reference>
+<comment type="function">
+<text evidence="1">Capsid protein (CA) is the structural component of the virus-like particle (VLP), forming the shell that encapsulates the retrotransposons dimeric RNA genome. The particles are assembled from trimer-clustered units and there are holes in the capsid shells that allow for the diffusion of macromolecules. CA has also nucleocapsid-like chaperone activity, promoting primer tRNA(i)-Met annealing to the multipartite primer-binding site (PBS), dimerization of Ty1 RNA and initiation of reverse transcription (By similarity).</text>
+</comment>
+<comment type="subunit">
+<text evidence="1">Homotrimer.</text>
+</comment>
+<comment type="subcellular location">
+<subcellularLocation>
+<location evidence="1">Cytoplasm</location>
+</subcellularLocation>
+</comment>
+<comment type="alternative products">
+<event type="ribosomal frameshifting"/>
+<isoform>
+<id>P0CX75-1</id>
+<name>Transposon Ty1-LR3 Gag polyprotein</name>
+<sequence type="displayed"/>
+</isoform>
+<isoform>
+<id>P0C2I6-1</id>
+<name>Transposon Ty1-LR3 Gag-Pol polyprotein</name>
+<sequence type="external"/>
+</isoform>
+<text evidence="1">The Gag-Pol polyprotein is generated by a +1 ribosomal frameshift. The ratio of Gag:Gag-Pol varies between 20:1 and 5:1 (By similarity).</text>
+</comment>
+<comment type="induction">
+<text evidence="3">Ty1-LR3 is a highly expressed element. Induced under amino acid starvation conditions by GCN4.</text>
+</comment>
+<comment type="domain">
+<text evidence="1">The C-terminal RNA-binding region of CA is sufficient for all its nucleocapsid-like chaperone activities.</text>
+</comment>
+<comment type="miscellaneous">
+<text>Retrotransposons are mobile genetic entities that are able to replicate via an RNA intermediate and a reverse transcription step. In contrast to retroviruses, retrotransposons are non-infectious, lack an envelope and remain intracellular. Ty1 retrotransposons belong to the copia elements (pseudoviridae).</text>
+</comment>
+<comment type="miscellaneous">
+<molecule>Isoform Transposon Ty1-LR3 Gag polyprotein</molecule>
+<text>Produced by conventional translation.</text>
+</comment>
+<dbReference type="EMBL" id="U19027">
+<property type="status" value="NOT_ANNOTATED_CDS"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="AY723845">
+<property type="protein sequence ID" value="AAU09762.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="EMBL" id="BK006945">
+<property type="protein sequence ID" value="DAA09545.1"/>
+<property type="molecule type" value="Genomic_DNA"/>
+</dbReference>
+<dbReference type="PIR" id="S57044">
+<property type="entry name" value="S57044"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_012561.3">
+<molecule id="P0CX75-1"/>
+<property type="nucleotide sequence ID" value="NM_001181684.3"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_013673.1">
+<molecule id="P0CX75-1"/>
+<property type="nucleotide sequence ID" value="NM_001182398.1"/>
+</dbReference>
+<dbReference type="RefSeq" id="NP_058172.1">
+<molecule id="P0CX75-1"/>
+<property type="nucleotide sequence ID" value="NM_001184407.1"/>
+</dbReference>
+<dbReference type="SMR" id="P0CX75"/>
+<dbReference type="BioGRID" id="31496">
+<property type="interactions" value="3"/>
+</dbReference>
+<dbReference type="BioGRID" id="33779">
+<property type="interactions" value="6"/>
+</dbReference>
+<dbReference type="BioGRID" id="35130">
+<property type="interactions" value="5"/>
+</dbReference>
+<dbReference type="iPTMnet" id="P0CX75"/>
+<dbReference type="GeneID" id="850926"/>
+<dbReference type="GeneID" id="853483"/>
+<dbReference type="GeneID" id="854968"/>
+<dbReference type="KEGG" id="sce:YJR026W"/>
+<dbReference type="KEGG" id="sce:YLR227W-A"/>
+<dbReference type="KEGG" id="sce:YML040W"/>
+<dbReference type="SGD" id="S000007375">
+<property type="gene designation" value="YLR227W-A"/>
+</dbReference>
+<dbReference type="HOGENOM" id="CLU_045291_1_0_1"/>
+<dbReference type="Proteomes" id="UP000002311">
+<property type="component" value="Chromosome XII"/>
+</dbReference>
+<dbReference type="RNAct" id="P0CX75">
+<property type="molecule type" value="protein"/>
+</dbReference>
+<dbReference type="GO" id="GO:0005737">
+<property type="term" value="C:cytoplasm"/>
+<property type="evidence" value="ECO:0000501"/>
+<property type="project" value="UniProtKB-SubCell"/>
+</dbReference>
+<dbReference type="GO" id="GO:0000943">
+<property type="term" value="C:retrotransposon nucleocapsid"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0003723">
+<property type="term" value="F:RNA binding"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="GO" id="GO:0032197">
+<property type="term" value="P:transposition, RNA-mediated"/>
+<property type="evidence" value="ECO:0000250"/>
+<property type="project" value="SGD"/>
+</dbReference>
+<dbReference type="InterPro" id="IPR015820">
+<property type="entry name" value="Retrotransposon_Ty1A_N"/>
+</dbReference>
+<dbReference type="Pfam" id="PF01021">
+<property type="entry name" value="TYA"/>
+<property type="match status" value="1"/>
+</dbReference>
+<proteinExistence type="evidence at transcript level"/>
+<keyword id="KW-0963">Cytoplasm</keyword>
+<keyword id="KW-0597">Phosphoprotein</keyword>
+<keyword id="KW-1185">Reference proteome</keyword>
+<keyword id="KW-0688">Ribosomal frameshifting</keyword>
+<keyword id="KW-0694">RNA-binding</keyword>
+<keyword id="KW-0814">Transposable element</keyword>
+<feature type="chain" description="Transposon Ty1-LR3 Gag polyprotein" id="PRO_0000409800">
+<location>
+<begin position="1"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="chain" description="Capsid protein" id="PRO_0000409801" evidence="1">
+<location>
+<begin position="1"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="peptide" description="Gag-p4" id="PRO_0000409802" evidence="1">
+<location>
+<begin position="402"/>
+<end position="440"/>
+</location>
+</feature>
+<feature type="region of interest" description="RNA-binding" evidence="1">
+<location>
+<begin position="299"/>
+<end position="401"/>
+</location>
+</feature>
+<feature type="compositionally biased region" description="Pro-rich">
+<location>
+<begin position="64"/>
+<end position="146"/>
+</location>
+</feature>
+<feature type="site" description="Cleavage; by Ty1 protease" evidence="1">
+<location>
+<begin position="401"/>
+<end position="402"/>
+</location>
+</feature>
+<feature type="modified residue" description="Phosphoserine" evidence="2">
+<location>
+<position position="416"/>
+</location>
+</feature>
+<feature type="sequence conflict" description="In Ref. 3; AAU09762." ref="3" evidence="4">
+<original>S</original>
+<variation>G</variation>
+<location>
+<position position="255"/>
+</location>
+</feature>
+<evidence key="1" type="ECO:0000250"/>
+<evidence key="2" type="ECO:0000250">
+<source>
+<dbReference type="UniProtKB" id="Q12441"/>
+</source>
+</evidence>
+<evidence key="3" type="ECO:0000269">
+<source>
+<dbReference type="PubMed" id="11884596"/>
+</source>
+</evidence>
+<evidence key="4" type="ECO:0000305"/>
+<sequence length="440" mass="48993" checksum="ACC50DD2AC8F4781" modified="2011-06-28" version="1">MESQQLSQHSHISHGSACASVTSKEVHTNQDPLDVSASKTEECEKASTKANSQQTTTPASSAVPENPHHASPQPASVPPPQNGPYPQQCMMTQNQANPSGWSFYGHPSMIPYTPYQMSPMYFPPGPQSQFPQYPSSVGTPLSTPSPESGNTFTDSSSADSDMTSTKKYVRPPPMLTSPNDFPNWVKTYIKFLQNSNLGGIIPTVNGKPVRQITDDELTFLYNTFQIFAPSQFLPTWVKDILSVDYTDIMKILSKSIEKMQSDTQEANDIVTLANLQYNGSTPADAFETKVTNIIDRLNNNGIHINNKVACQLIMRGLSGEYKFLRYTRHRHLNMTVAELFLDIHAIYEEQQGSRNSKPNYRRNLSDEKNDSRSYTNTTKPKVIARNPQKTNNSKSKTARAHNVSTSNNSPSTDNDSISKSTTEPIQLNNKHDLHLRPGTY</sequence>
+</entry>
+<copyright>
+Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
+Distributed under the Creative Commons Attribution (CC BY 4.0) License
+</copyright>
+</uniprot>