Protein: | gi|229267567, gi... |
Organism: | Bacillus anthracis str. A0248 |
Length: | 529 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|229267567, gi....
Description | E-value | Query Range |
Subject Range |
|
0.0 | [1..529] | [1..529] |
|
0.0 | [1..529] | [1..529] |
|
0.0 | [1..529] | [1..529] |
|
0.0 | [1..529] | [1..527] |
|
0.0 | [1..529] | [1..530] |
|
0.0 | [1..529] | [1..540] |
|
0.0 | [5..528] | [9..530] |
|
0.0 | [5..528] | [9..530] |
Region A: Residues: [1-193] |
1 11 21 31 41 51 | | | | | | 1 MKYRAVAAGI LAASLLSSPV SSFAAAKKFS DVPTWAQQSV DYLVGKKALD GKPDGTFSPS 60 61 EAVDRGSAAK ILAVVLGLPV DPKAKPSFKD AQNHWAAPYI AAVEKAGVIN GDGTGKFNPS 120 121 SQINRASMAS MLVQAYSLDK KIIGELPTQF KDLEPHWGKK QANILVALEI SKGTGNGWNP 180 181 EGTVTRAEAA QFI |
Shown below are all of our structure predictions for this domain.
Click here to view only most confident match.
Found no structure predictions for this domain.
Region A: Residues: [194-323] |
1 11 21 31 41 51 | | | | | | 1 AMADQNKTST SKRMYMNRNV ITYHQPSLSS GITDVQHKPQ MVEVTEQRAD GWLKIVTSKG 60 61 EKWTPLTEKT ETINEEFTTY ETASHSSKVL GTYNAQTVTV MEESGSWIRI RVGAGFQWVD 120 121 KNQLNPVKQE |
Shown below are all of our de novo (Rosetta) predictions for this domain.
Click here to view only most confident match.
MCM Score |
SCOP Match |
SCOP Description | ||
View | Download | 0.254 | c.37.1 | P-loop containing nucleoside triphosphate hydrolases |
View | Download | 0.213 | c.2.1 | NAD(P)-binding Rossmann-fold domains |
View | Download | 0.330 | c.52.1 | Restriction endonuclease-like |
View | Download | 0.220 | c.78.1 | Aspartate/ornithine carbamoyltransferase |
View | Download | 0.252 | d.110.2 | GAF domain-like |
Region A: Residues: [324-529] |
1 11 21 31 41 51 | | | | | | 1 NFLEGKAIII DPGHGGIDSG NVGYYEKESE TVLDVSLRLK KIFEQKAPFT VMFTRTDNTR 60 61 PGVNSTDSLK KRVEFAQEHN GDIFVSIHAN GSAEKNGQGT ETLYYQSARA KVTNPHVEDS 120 121 KLLAQKIQDR LVAALGTKDR GVKHQDLYVT RENTMPAVLT ELAFVDNKSD ADKIATPKQR 180 181 QAAAEAIYQG ILDYYEAKGN NVSSFR |
Detection Method: | ![]() |
Confidence: | 40.522879 |
Match: | 1jwqA |
Description: | Structure of the catalytic domain of CwlV, N-acetylmuramoyl-L-alanine amidase from Bacillus(Paenibacillus) polymyxa var.colistinus |
Matching Structure (courtesy of the PDB):![]() |
Term | Confidence | Notes |
N-acetylmuramoyl-L-alanine amidase activity | 3.05057546758914 | bayes_pls_golite062009 |
hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides | 2.6697110481986 | bayes_pls_golite062009 |
carboxypeptidase activity | 2.3176485329358 | bayes_pls_golite062009 |
hydrolase activity | 1.7824202462173 | bayes_pls_golite062009 |
catalytic activity | 1.76936806579991 | bayes_pls_golite062009 |
peptidase activity | 1.69812537802871 | bayes_pls_golite062009 |
peptidase activity, acting on L-amino acid peptides | 1.41029347724469 | bayes_pls_golite062009 |
exopeptidase activity | 0.82896398764377 | bayes_pls_golite062009 |
metallopeptidase activity | 0.1586028474273 | bayes_pls_golite062009 |