view test-data/cd00008.smp @ 31:0e3cf9594bb7 draft

Update with window size fix

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"
      }
    },
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