YRC Public Data Repository - Protein Structure Prediction

Protein:	ASTB_ECOLI
Organism:	Escherichia coli
Length:	447 amino acids
Reference:	Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16

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Top Sequence Alignment Hits

Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for ASTB_ECOLI.

Description	E-value	Query Range	Subject Range
ASTB_SHELP - N-succinylarginine dihydrolase OS=Shewanella loihica (strain ATCC BAA-1088 / PV-4) GN=astB PE=3 SV=1	850.0	[0..1]	[441..1]
SO2706 - succinylarginine dihydrolase ASTB_SHEON - N-succinylarginine dihydrolase OS=Shewanella oneidensis (strain MR-1) GN=astB PE=3 SV=1	847.0	[0..1]	[441..1]
ASTB_SHESW - N-succinylarginine dihydrolase OS=Shewanella sp. (strain W3-18-1) GN=astB PE=3 SV=1 gi\|124547576, gi... - gi\|124547576\|ref\|ZP_01706445.1\| Succinylarginine dihydrolase [Shewanella putrefaciens 200], gi\|12450...	846.0	[0..1]	[441..1]
gi\|82406014, gi\|... - gi\|82495973\|ref\|ZP_00881545.1\| succinylarginine dihydrolase [Shewanella sp. MR-4], gi\|82406014\|gb\|EA...	846.0	[0..1]	[441..1]
ASTB_SHEPC - N-succinylarginine dihydrolase OS=Shewanella putrefaciens (strain CN-32 / ATCC BAA-453) GN=astB PE=3...	845.0	[0..1]	[441..1]
gi\|78691713, gi\|... - gi\|78691713\|ref\|ZP_00856313.1\| succinylarginine dihydrolase [Shewanella sp. MR-7], gi\|78508891\|gb\|EA...	845.0	[0..1]	[441..1]
ASTB_SHEFN - N-succinylarginine dihydrolase OS=Shewanella frigidimarina (strain NCIMB 400) GN=astB PE=3 SV=1	844.0	[0..1]	[441..1]
ASTB_SHEAM - N-succinylarginine dihydrolase OS=Shewanella amazonensis (strain ATCC BAA-1098 / SB2B) GN=astB PE=3 ...	843.0	[0..1]	[441..1]
ASTB_SHEB5 - N-succinylarginine dihydrolase OS=Shewanella baltica (strain OS155 / ATCC BAA-1091) GN=astB PE=3 SV=...	842.0	[0..1]	[441..1]
ASTB_SHEDO - N-succinylarginine dihydrolase OS=Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013...	842.0	[0..1]	[441..1]

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Predicted Domain #1

Region A:
Residues: [1-447]

      1          11         21         31         41         51         
      |          |          |          |          |          |          
    1 MNAWEVNFDG LVGLTHHYAG LSFGNEASTR HRFQVSNPRL AAKQGLLKMK ALADAGFPQA  60
   61 VIPPHERPFI PVLRQLGFSG SDEQVLEKVA RQAPHWLSSV SSASPMWVAN AATIAPSADT 120
  121 LDGKVHLTVA NLNNKFHRSL EAPVTESLLK AIFNDEEKFS VHSALPQVAL LGDEGAANHN 180
  181 RLGGHYGEPG MQLFVYGREE GNDTRPSRYP ARQTREASEA VARLNQVNPQ QVIFAQQNPD 240
  241 VIDQGVFHND VIAVSNRQVL FCHQQAFARQ SQLLANLRAR VNGFMAIEVP ATQVSVSDTV 300
  301 STYLFNSQLL SRDDGSMMLV LPQECREHAG VWGYLNELLA ADNPISELKV FDLRESMANG 360
  361 GGPACLRLRV VLTEEERRAV NPAVMMNDTL FNALNDWVDR YYRDRLTAAD LADPQLLREG 420
  421 REALDVLSQL LNLGSVYPFQ REGGGNG

[Run NCBI BLAST on this sequence.]

Detection Method:	PSI-BLAST
Confidence:	1000.0
Match:	1ynfA
Description:	Crystal Structure of N-Succinylarginine Dihydrolase, AstB, bound to Substrate and Product, an Enzyme from the Arginine Catabolic Pathway of Escherichia coli
Matching Structure (courtesy of the PDB):

Predicted functions:

Term	Confidence	Notes
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines	1.80356530015579	bayes_pls_golite062009
N-succinylarginine dihydrolase activity	1.79190392361658	bayes_pls_golite062009
catalytic activity	1.2603605268935	bayes_pls_golite062009
protein-arginine deiminase activity	1.23765841785254	bayes_pls_golite062009
arginine deiminase activity	1.06118411192651	bayes_pls_golite062009
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds	0.89634749643842	bayes_pls_golite062009
hydrolase activity	0.79014898516962	bayes_pls_golite062009

TMHMM	2.0c	PSIPRED	v2.61
SignalP	3.0	COILS	1999
DISOPRED	v0.1	NCBI nr	06/2007
PSI-BLAST	2.2.18	FFAS	ffas03
PDB	06/2007	Pfam	22
HMMER	2.3.2

View Structure Prediction Details

Top Sequence Alignment Hits

Predicted functions: