A0AAD4L8X0 · A0AAD4L8X0_9AGAM
- Proteintripeptidyl-peptidase II
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids550 (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 binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 509 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 510 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 528 | Ca2+ (UniProtKB | ChEBI) | |||
Binding site | 530 | 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
- 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 > Basidiomycota > Agaricomycotina > Agaricomycetes > Russulales > Russulaceae > Lactarius
Accessions
- Primary accessionA0AAD4L8X0
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length550
- Mass (Da)59,761
- Last updated2024-05-29 v1
- Checksum530935A68F71A2F2
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
JAKELL010000070 EMBL· GenBank· DDBJ | KAH8984902.1 EMBL· GenBank· DDBJ | Genomic DNA |