Q5J6J2 · SCPB_TRIRU
- ProteinCarboxypeptidase S1 homolog B
- GeneSCPB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids662 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Extracellular serine carboxypeptidase that contributes to pathogenicity.
Catalytic activity
pH Dependence
Optimum pH is 8.0.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 240 | ||||
Active site | 459 | ||||
Binding site | 462 | substrate | |||
Active site | 517 | ||||
Binding site | 518 | substrate | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | fungal-type vacuole | |
Cellular Component | plasma membrane | |
Cellular Component | side of membrane | |
Molecular Function | serine-type carboxypeptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameCarboxypeptidase S1 homolog B
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Arthrodermataceae > Trichophyton
Accessions
- Primary accessionQ5J6J2
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain, disulfide bond, glycosylation, lipidation, propeptide.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-21 | ||||
Chain | PRO_0000384123 | 22-633 | Carboxypeptidase S1 homolog B | ||
Disulfide bond | 51↔123 | ||||
Glycosylation | 130 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 163 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 186 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 200 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 262 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 302 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 311 | N-linked (GlcNAc...) asparagine | |||
Disulfide bond | 328↔364 | ||||
Disulfide bond | 335↔357 | ||||
Glycosylation | 350 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 414 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 475 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 493 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 506 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 598 | N-linked (GlcNAc...) asparagine | |||
Glycosylation | 612 | N-linked (GlcNAc...) asparagine | |||
Lipidation | 633 | GPI-anchor amidated glycine | |||
Propeptide | PRO_0000384124 | 634-662 | Removed in mature form | ||
Keywords
- PTM
PTM databases
Expression
Induction
Expression is strongly increased during growth on protein-rich medium.
Structure
Sequence
- Sequence statusComplete
- Sequence processingThe displayed sequence is further processed into a mature form.
- Length662
- Mass (Da)73,012
- Last updated2005-02-15 v1
- ChecksumB47308AB5BB82CCB
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AY497022 EMBL· GenBank· DDBJ | AAS76666.1 EMBL· GenBank· DDBJ | Genomic DNA |