Protein: | gi|30253920, gi|... |
Organism: | Bacillus anthracis str. Ames |
Length: | 674 amino acids |
Reference: | Drew K, et al. (2011) The proteome folding project: Proteome-scale prediction of structure and function. Genome Res. 2011 Sep 16 |
Listed below are up to the top 10 sequence alignment matches, by species, for the PSI-BLAST search against the protein sequence for gi|30253920, gi|....
Description | E-value | Query Range |
Subject Range |
|
0.0 | [1..674] | [15..688] |
|
0.0 | [1..674] | [1..674] |
|
0.0 | [1..674] | [1..674] |
|
0.0 | [1..674] | [1..674] |
|
0.0 | [1..674] | [15..688] |
|
0.0 | [1..674] | [1..674] |
|
0.0 | [1..674] | [15..688] |
|
0.0 | [1..674] | [15..688] |
|
0.0 | [1..674] | [1..674] |
|
0.0 | [1..674] | [15..688] |
Region A: Residues: [1-86] |
1 11 21 31 41 51 | | | | | | 1 MKSKKFTLLL LSLLLFLPLF LTNFITPNVV LADSQKQDQK IVGYFPSWGI YGRNYQVADI 60 61 DASKLTHLNY AFADICWNGK HGNPST |
Detection Method: | ![]() |
Confidence: | 78.0 |
Match: | 1itxA |
Description: | Chitinase A1 |
Matching Structure (courtesy of the PDB):![]() |
Region A: Residues: [87-576] |
1 11 21 31 41 51 | | | | | | 1 HPDNPNKQTW NCKESGVPLQ NKEVPNGTLV LGEPWADVTK SYPGSGTTWE DCDKYARCGN 60 61 FGELKRLKAK YPHLKTIISV GGWTWSNRFS DMAADEKTRK VFADSTVDFL REYGFDGVDL 120 121 DWEYPGVETI PGGSYRPEDK QNFTLLLQDV RNALTKAGAE DGKQYLLTIA SGASQRYADH 180 181 TELKKISQIL DWINIMTYDF HGGWEATSNH NAALYKDPND PAADTKFYVD GAIDIYTNEG 240 241 VPADKLVLGV PFYGRGWKSC GKENNGQYQP CKPGSDGKLA SKGTWDDYST GDTGVYDYGD 300 301 LAANYVNKNG FVRGWNDVAK VPYLYNATTG TFISYDDNES MKYKTDYIKT KGLSGAMFWE 360 361 LSGDCRTSPK YSCSGPKLLD TLVKELLGGP ITQKDIEPPT NVKNIAVTNK NSNSVQLNWT 420 421 ASTDNVGVTE YEITAGEEKW STTTNSIAIK NLKPNTEYTF SILAKDAAGN KSQPTSILVK 480 481 TDDANTTPPG |
Detection Method: | ![]() |
Confidence: | 46.09691 |
Match: | 1e6nA |
Description: | Chitinase B, C-terminal domain; Chitinase B, catalytic domain; Chitinase B |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
chitinase activity | 6.40555694403866 | bayes_pls_golite062009 |
receptor binding | 2.49274459751868 | bayes_pls_golite062009 |
growth factor activity | 2.4208679297225 | bayes_pls_golite062009 |
hydrolase activity, hydrolyzing O-glycosyl compounds | 1.91170236789651 | bayes_pls_golite062009 |
amylase activity | 1.38959979746158 | bayes_pls_golite062009 |
hydrolase activity, acting on glycosyl bonds | 1.34796838721403 | bayes_pls_golite062009 |
chitin binding | 1.29046765706168 | bayes_pls_golite062009 |
binding | 0.931465888895274 | bayes_pls_golite062009 |
carbohydrate binding | 0.83219070974164 | bayes_pls_golite062009 |
glucosidase activity | 0.766503513427695 | bayes_pls_golite062009 |
pattern binding | 0.629401292223251 | bayes_pls_golite062009 |
catalytic activity | 0.534516847146079 | bayes_pls_golite062009 |
protein binding | 0.41522498233974 | bayes_pls_golite062009 |
transferase activity, transferring hexosyl groups | 0.266938437560648 | bayes_pls_golite062009 |
hexosaminidase activity | 0.21148675734804 | bayes_pls_golite062009 |
hydrolase activity | 0.178746202646272 | bayes_pls_golite062009 |
Region A: Residues: [577-674] |
1 11 21 31 41 51 | | | | | | 1 GNSNATFSVT SNWGSGYNFS IVIKNSGTTP IKNWKLEFDY NGNLTQVWDS KISSKINNHY 60 61 VITNAGWNGE IPPGGSITIG GAGTGTPAEL VNASISEN |
Detection Method: | ![]() |
Confidence: | 12.0 |
Match: | 1exgA |
Description: | SOLUTION STRUCTURE OF A CELLULOSE BINDING DOMAIN FROM CELLULOMONAS FIMI BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
pattern binding | 2.27215563583973 | bayes_pls_golite062009 |
binding | 1.34949978791263 | bayes_pls_golite062009 |
polysaccharide binding | 1.30518726696745 | bayes_pls_golite062009 |
carbohydrate binding | 1.22734683278419 | bayes_pls_golite062009 |
protein binding | 0.382621269105676 | bayes_pls_golite062009 |