Protein: | gi|30262986, gi|... |
Organism: | Bacillus anthracis str. Ames |
Length: | 584 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|30262986, gi|....
Description | E-value | Query Range |
Subject Range |
|
0.0 | [1..584] | [6..589] |
|
0.0 | [1..584] | [1..584] |
|
0.0 | [6..584] | [11..589] |
|
0.0 | [6..584] | [11..589] |
|
0.0 | [1..584] | [6..589] |
|
0.0 | [5..576] | [4..593] |
|
0.0 | [1..578] | [1..578] |
|
0.0 | [11..579] | [6..580] |
|
0.0 | [11..579] | [5..579] |
|
0.0 | [11..579] | [5..579] |
Region A: Residues: [1-423] |
1 11 21 31 41 51 | | | | | | 1 MGQNQFRWSN EQLREHVEII DGTRSPHKLL KNATYLNSYI REWMQANIWI YDDRIIYVGE 60 61 KLPEQLHECE VIDCDGKYVV PSYIEPHAHP YQLYNPETLA NHAMQFGTTT FINDNLTLFF 120 121 TLKREESFHL LDEFTKIPAS MYWWCRFDGQ TELQNGESLF NSEEIIKWLQ HEAVLQGGEL 180 181 TAWPKLLHGD DEMLTWVQET KRLQKKVEGH FPGASEATLA KLKLLGTDCD HEAMTGQEAL 240 241 ARLMQGYTVS LRNSSIRPDL EVLLKELLEL GVKQFDRFIF TTDGSHPSFY ENGMTNIMIA 300 301 TAIKKGIPVI DAYQMASYNI ARYYNMEHIH GAIATGRIAN INILESKENP VPTSVIAKGQ 360 361 WVKRDGVNTH EALHIDWSKC KVTPLSLEWS IEKEDMLFSN KTGIHLLNNV ITKPYTSEIN 420 421 IDC |
Detection Method: | ![]() |
Confidence: | 47.69897 |
Match: | 1e9zB |
Description: | alpha-Subunit of urease; alpha-subunit of urease, catalytic domain |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | 2.09478447332528 | bayes_pls_golite062009 |
catalytic activity | 2.072432847481 | bayes_pls_golite062009 |
hydrolase activity | 2.06578679075873 | bayes_pls_golite062009 |
deaminase activity | 2.00485136695944 | bayes_pls_golite062009 |
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides | 1.2382202418205 | bayes_pls_golite062009 |
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amidines | 0.97576964967771 | bayes_pls_golite062009 |
adenine deaminase activity | 0.56372605168514 | bayes_pls_golite062009 |
dihydroorotase activity | 0.44266757158292 | bayes_pls_golite062009 |
guanine deaminase activity | 0.22133469174284 | bayes_pls_golite062009 |
Region A: Residues: [424-584] |
1 11 21 31 41 51 | | | | | | 1 DELSIDYDEC FLMMIARDGT WRVNTVVKGF AKEIGGLASS YSGTGDIILV GKRKEDMLTA 60 61 FHRIKELGGG MVIAEKNEVL HEIALPLLGI MSELKMSELI QKEKKMVNLL QERGYVYNDP 120 121 AFTILFFSAT HLPFIRVTFI GLYDVKSGKV VASPVNLIKQ Y |
Shown below are all of our de novo (Rosetta) predictions for this domain.
Click here to view only most confident match.
MCM Score |
GO Score |
GO Term |
SCOP Match |
SCOP Description | ||
View | Download | 0.587 | 0.812 | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | c.2.1 | NAD(P)-binding Rossmann-fold domains |
View | Download | 0.556 | 0.812 | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | c.55.3 | Ribonuclease H-like |
View | Download | 0.487 | 0.812 | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | c.3.1 | FAD/NAD(P)-binding domain |
View | Download | 0.512 | 0.812 | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | c.57.1 | Molybdenum cofactor biosynthesis proteins |
View | Download | 0.563 | 0.812 | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds | c.2.1 | NAD(P)-binding Rossmann-fold domains |