D4B1S6 · MCPB_ARTBC
- ProteinProbable carboxypeptidase 2
- GeneMCPB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids526 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
Function
function
Extracellular metalloprotease that contributes to pathogenicity.
Cofactor
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 136 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 139 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Binding site | 224 | Zn2+ (UniProtKB | ChEBI); catalytic | |||
Active site | 322 | Proton donor/acceptor | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular space | |
Molecular Function | metallocarboxypeptidase activity | |
Molecular Function | zinc ion binding | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProbable carboxypeptidase 2
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Arthrodermataceae > Trichophyton
Accessions
- Primary accessionD4B1S6
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, glycosylation.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-21 | ||||
Chain | PRO_0000397762 | 22-526 | Probable carboxypeptidase 2 | ||
Glycosylation | 46 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 116 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 393 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 459 | N-linked (GlcNAc...) asparagine | |||
Keywords
- PTM
PTM databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 53-73 | Polar residues | |||
Region | 53-76 | Disordered | |||
Domain | 71-351 | Peptidase M14 | |||
Sequence similarities
Belongs to the peptidase M14 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length526
- Mass (Da)58,561
- Last updated2010-05-18 v1
- Checksum601707DDD7794495
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 53-73 | Polar residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
ABSU01000027 EMBL· GenBank· DDBJ | EFE30708.1 EMBL· GenBank· DDBJ | Genomic DNA |