Alternative representations: 1 /
| Protein length | 518 aa |
|---|---|
| Source database | UniProt |
| Identifiers | G4ET11_BACIU, G4ET11, A0A164WYP7_BACIU, A0A164WYP7, A0A1B2BDK8_BACIU, A0A1B2BDK8, L8AP58_BACIU, L8AP58, A0A0T8Q1N3_STREE, A0A0T8Q1N3, H9TZX3_BACIU, H9TZX3, I0F716_9BACI, I0F716, YRVJ_BACSU, O32041 |
| Domain organisation | Proteins having all the domains as the query in the same order. Additional domains are allowed. |
|---|---|
| Domain composition | Proteins with the same domain composition have at least one copy of each of the domains of the query. |
This domain architecture was probably invented with the emergence of Bacillus subtilis subsp. subtilis str. 168
YRVJ_BACSU is shown as
yrvJ in the network
Click and drag to pan the network, and zoom by using your mouse wheel. Click the protein nodes for additional options.
The network on the left comes from STRING, a database of known and predicted protein interactions. Displayed here is the evidence view, where different line colors represent the types of evidence for the association.
Protein YRVJ_BACSU is possibly involved in these pathways, based on its similarity to the listed KEGG orthologous groups:
Orthology information is taken from eggNOG, a database of orthologous groups of genes. Orthologous groups containing this protein are listed below. This protein is named 224308.BSU27580 in eggNOG.
| OG | Taxonomic class | Description |
|---|---|---|
| LCOG3103 | All organisms (root) | SH3 domain protein,N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan DL-endopeptidase CwlO [EC:3.4.-.-] |
| B32PF | Bacillus subtilis group (species group) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28] |
| LCOG0860 | All organisms (root) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],bla regulator protein blaR1,stage II sporulation protein D |
| COG3103 | Bacteria (superkingdom) | SH3 domain protein,N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan DL-endopeptidase CwlO [EC:3.4.-.-] |
| COG0860 | Bacteria (superkingdom) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],bla regulator protein blaR1,stage II sporulation protein D |
| 9XIZK | Firmicutes (phylum) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28],peptidoglycan DL-endopeptidase CwlO [EC:3.4.-.-],stage II sporulation protein D |
| G62GK | Bacilli (class) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28] |
| F2X9S | Bacillales (order) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28] |
| F6EUP | Bacillaceae (family) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28] |
| AARII | Bacillus (genus) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28] |
| BAJ96 | Bacillus subtilis (species) | N-acetylmuramoyl-L-alanine amidase [EC:3.5.1.28] |
The SMART diagram above represents a summary of the results shown below. Domains with scores less significant than established cutoffs are not shown in the diagram. Features are also not shown when two or more occupy the same piece of sequence; the priority for display is given by SMART > PFAM > PROSPERO repeats > Signal peptide > Transmembrane > Coiled coil > Low complexity. In either case, features not shown in the above diagram are listed in the right side table below, and the reason for their omission is shown in the 'Reason' column.