Mercurial > repos > devteam > ncbi_blast_plus
view test-data/cd00008.smp @ 33:d999e774072a draft
Fix for get_species_taxids
author | peterjc |
---|---|
date | Sun, 19 Nov 2023 22:57:39 +0000 |
parents | 2fe07f50a41e |
children |
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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 }, { 338020833333333, 10, -15 }, { 0, 10, 0 }, { 0, 10, 0 }, { 0, 10, 0 }, { 0, 10, 0 }, { 0, 10, 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