Mercurial > repos > devteam > ncbi_blast_plus

diff test-data/cd00008.smp @ 14:2fe07f50a41e draft

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Uploaded v0.1.01 - Requires blastdbd datatype (blast_datatypes v0.0.19). Support for makeprofiledb to create protein domain databases and use them in RPS-BLAST and RPS-TBLASTN. Tools now support GI and SeqID filters, and embed the citations.
author peterjc
date Mon, 01 Dec 2014 05:59:16 -0500
parents
children
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--- /dev/null	Thu Jan 01 00:00:00 1970 +0000
+++ b/test-data/cd00008.smp	Mon Dec 01 05:59:16 2014 -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 {
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+      h { 14, 10, -2 },
+      scalingFactor 100,
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+    }
+  }
+}