A0A2J5HJV0 · A0A2J5HJV0_9EURO
- Proteintripeptidyl-peptidase II
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids786 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
function
Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence.
Catalytic activity
Cofactor
Features
Showing features for active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Active site | 287 | Charge relay system | |||
Active site | 291 | Charge relay system | |||
Active site | 502 | Charge relay system | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Cellular Component | membrane | |
Molecular Function | metal ion binding | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | tripeptidyl-peptidase activity | |
Biological Process | phosphoenolpyruvate-dependent sugar phosphotransferase system | |
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 > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA0A2J5HJV0
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Signal | 1-23 | ||||
Chain | PRO_5014400108 | 24-786 | tripeptidyl-peptidase II | ||
Keywords
- PTM
Structure
Sequence
- Sequence statusComplete
- Length786
- Mass (Da)86,166
- Last updated2018-03-28 v1
- MD5 Checksum3F1BC60B0BC2A35DC428F8BDCEF92B2A
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KZ559597 EMBL· GenBank· DDBJ | PLN77352.1 EMBL· GenBank· DDBJ | Genomic DNA |