Mercurial > repos > devteam > ncbi_blast_plus
diff test-data/cd00008.smp @ 0:432ea9614cc9 draft
Uploaded v0.1.02 preview 1, using tool_data_table_conf.xml for loc files, etc
| author | peterjc |
|---|---|
| date | Fri, 30 Jan 2015 08:27:28 -0500 |
| parents | |
| children |
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--- /dev/null Thu Jan 01 00:00:00 1970 +0000 +++ b/test-data/cd00008.smp Fri Jan 30 08:27:28 2015 -0500 @@ -0,0 +1,13679 @@ +PssmWithParameters ::= { + pssm { + isProtein TRUE, + numRows 28, + numColumns 160, + byRow FALSE, + query seq { + id { + general { + db "CDD", + tag id 189019 + } + }, + descr { + title "cd00008, PIN_53EXO-like, PIN domains of the 5'-3' exonucleases + of DNA polymerase I, bacteriophage T4 RNase H and T5-5' nucleases, and + homologs. PIN (PilT N terminus) domains of the 5'-3' exonucleases (53EXO) of + mutli-domain DNA polymerase I and single domain protein homologs, as well as, + the PIN domains of bacteriophage T5-5'nuclease (T5FEN or 5'-3'exonuclease), + bacteriophage T4 RNase H (T4FEN), bacteriophage T3 (T3 phage + exodeoxyribonuclease) and other similar nucleases are included in this + family. The 53EXO of DNA polymerase I recognizes and endonucleolytically + cleaves a structure-specific DNA substrate that has a bifurcated downstream + duplex and an upstream template-primer duplex that overlaps the downstream + duplex by 1 bp. The T5-5'nuclease is a 5'-3'exodeoxyribonuclease that also + exhibits endonucleolytic activity on flap structures (branched duplex DNA + containing a free single-stranded 5'end). T4 RNase H, which removes the RNA + primers that initiate lagging strand fragments, has 5'- 3'exonuclease + activity on DNA/DNA and RNA/DNA duplexes and has endonuclease activity on + flap or forked DNA structures. These nucleases are members of the + structure-specific, 5' nuclease family that catalyzes hydrolysis of DNA + duplex-containing nucleic acid structures during DNA replication, repair, and + recombination. They contain a PIN domain with a helical arch/clamp region (I + domain) of variable length (approximately 16 to 30 residues in 53EXO-like PIN + domains) and a H3TH (helix-3-turn-helix) domain, an atypical + helix-hairpin-helix-2-like region. Both the H3TH domain (not included here) + and the helical arch/clamp region are involved in DNA binding. The active + site of the 53EXO of Taq DNA polymerase I includes a set of conserved acidic + residues that are essential for binding three divalent metal ions (two Mn2+ + ions and one Zn2+ ion) required for nuclease activity. T5-5'nuclease requires + at least two bound divalent metal ions for nuclease activity and is reported + to be able to use Mg2+, Mn2+ or Co2+ as co-factors." + }, + inst { + repr raw, + mol aa, + length 160, + seq-data ncbieaa "LMLVDGTNLAFRTKHNNSKKKEKINLSPFASSYVSSIQSLAKSYSARTTIVL +GDKGKSVFRLEHLPEYKGNRDEKYAEEKALDEQFFEYLKDAFELCKATTFPTFTIRGYEADDMAAYLVKKIGHEGDHV +WIISTDGDWDQLLTDKVSRFSPTTRREYHL" + } + }, + intermediateData { + weightedResFreqsPerPos { + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 338020833333333, 10, -15 }, + { 0, 10, 0 }, + { 328645833333333, 10, -15 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 333333333333333, 10, -15 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 0, 10, 0 }, + { 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