A0A0J8QR40 · A0A0J8QR40_COCIT
- Proteintripeptidyl-peptidase II
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids595 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
Function
function
Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
Catalytic activity
Cofactor
Note: Binds 1 Ca2+ ion per subunit.
Features
Showing features for active site, binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 290 | Charge relay system | |||
Active site | 294 | Charge relay system | |||
Active site | 505 | Charge relay system | |||
Binding site | 547 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 548 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 575 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 577 | Ca2+ (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | metal ion binding | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | tripeptidyl-peptidase activity | |
Biological Process | proteolysis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nametripeptidyl-peptidase II
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Onygenales > Onygenaceae > Coccidioides
Accessions
- Primary accessionA0A0J8QR40
Proteomes
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Protein-protein interaction databases
Structure
Sequence
- Sequence statusComplete
- Length595
- Mass (Da)65,330
- Last updated2015-10-14 v1
- ChecksumEC9DAC894306CFCC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
DS268137 EMBL· GenBank· DDBJ | KMU75114.1 EMBL· GenBank· DDBJ | Genomic DNA |