A0A9P4XFP5 · A0A9P4XFP5_9HYPO
- Proteintripeptidyl-peptidase II
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1574 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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 | 275 | Charge relay system | ||||
Sequence: E | ||||||
Active site | 279 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 496 | Charge relay system | ||||
Sequence: S | ||||||
Binding site | 539 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 540 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: I | ||||||
Binding site | 564 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 566 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | extracellular region | |
Molecular Function | metal ion binding | |
Molecular Function | NAD+ binding | |
Molecular Function | serine-type endopeptidase activity | |
Molecular Function | transferase 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 > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Hypocreaceae > Trichoderma
Accessions
- Primary accessionA0A9P4XFP5
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-20 | |||||
Sequence: MKSALLWAVQLSLLAGLGAS | ||||||
Chain | PRO_5040357253 | 21-1574 | tripeptidyl-peptidase II | |||
Sequence: RRNVEQVLSIPTGWTKFQDVVNPARHMRLSIALRQPNIDQLETKMTENDNRLSLEEIQQLQAPDQKDVDAVLQWLSQNNLKGEVDNNFIHVTTTVAQAEPLLGMKVSRFAYKDKKPVLRTTKYTVPDSVAGSISFIHPLANFMTARHKPEVVSAPPKPASKAAAADEDNIIYCPGSVTPSCLAQLYNISSYKPADNKSPVIFGVAGFLEENANLLDLQQFLNSAAPNVAQAGKSITVELVNGGVNSQDLAESGHEAALDVDYAVSVGFPTNVTYYATGGRGVKLDDNGQPISGEDDDNEPYLEFFRYLLAKPDHQVPHVLSLSYSDDELSVPREYAKHVCSLFGLLTARGTSIIFSSGDGGARGGRDSSCLTNDGTKRPVAMATFPPTCPWVTSVGAVTNGAEPPSGASFSTGGFSQYFARPHWQDSSVKNYVQALNGRLDGLYDPSMRAIPDISAVGTSFMIIASGIPHFLQGTSASAPVFASMVALINDARLRAGKRSLGWLNQHLYSNKVKNVLQDITVGKSLSCVFNNTEVPGGWPAAPGWDAITGLGVPKEFDKFLQVLYDMPTQHVEPETHGLLQEVANSLLKARKVVVVTGAGISTNSGIPDFRSENGLYSLIQAQFDAASQPTRSTDRFKTDGDGNGNGDGGEEPRPTKRRKVSREPSPDLDEVDRQLNEDIKARAEAEMPAASSQAADTQQAVAASDPNASENGCLSTPRPKPALPSTPKPTTTSPLSSPPREEFMLPLPLASSSLRAEDRERIAGVSQNIVSSPLSSPPPVLFDPFHPSSPSDENMSRRSSTTPSEVDEMRDLPNAMPASQASNPGKTTLPNMKGKDLFDASIWSDPTRTSVFYQFATSLRQKVREAEPTSSHKFIGHLRDRGKLVRCYTQNIDQIEEKVGLSTSLLAGPGSRGRFSRKSTANAAQLNKMVEEVSSSGEGGNAGDVGDVGASSQSPTNGSSEQTPADQRQTSSQPNGKTEEDETTTSSTTTPPNQQPKPAPRKEVPPLRSGVECVFLHGSLQLLRCFLCGQVCSWDDDDREVETLSGQQPECPHCVGATEARQERGKRALGVGKLRPDIVLYGEEHPNAHLISPIVTHDLALYPDMLLILGTSLRVHGLKVMVREFAKTVHSKGGKVVFVNFTKPPESSWGDIIDYWIQWDCDAWVADLQVRIPKLWQEPEPPKPKKKRDSGGGAAEEGREEKKKPPAQNPVALRDTKVNGAYCTLKILKELRRITATSPPLPIILSLPPSLSTAPPLLERVSAAVTTEAKPNPDPPTPAEVAPRAAAVMDPPTRISTPRGKAKRPRKSAPGALERPKRTPSTLNPNHGRSKKPVEEVKEEEVLETPETPSQPPVSTVEEFSSILHSVKSNPRIRKRKMIDGEEFVFPTIGKKRGAVDSLYKGAEDDKKQLPPLRPVPDQATGVASLPAEAEAEDAIEEPLASISVNVRAATTFTRPEAFYIQDPLVTLLEKAPQWKAMEVNHGELRRNKRRISKRFLPVQVQMETKAQAEANAALALAGLRTNSHMVPQVAHAVPGNGYTELANWAATWSCKK |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 196-586 | Peptidase S53 | ||||
Sequence: SVTPSCLAQLYNISSYKPADNKSPVIFGVAGFLEENANLLDLQQFLNSAAPNVAQAGKSITVELVNGGVNSQDLAESGHEAALDVDYAVSVGFPTNVTYYATGGRGVKLDDNGQPISGEDDDNEPYLEFFRYLLAKPDHQVPHVLSLSYSDDELSVPREYAKHVCSLFGLLTARGTSIIFSSGDGGARGGRDSSCLTNDGTKRPVAMATFPPTCPWVTSVGAVTNGAEPPSGASFSTGGFSQYFARPHWQDSSVKNYVQALNGRLDGLYDPSMRAIPDISAVGTSFMIIASGIPHFLQGTSASAPVFASMVALINDARLRAGKRSLGWLNQHLYSNKVKNVLQDITVGKSLSCVFNNTEVPGGWPAAPGWDAITGLGVPKEFDKFLQVLYD | ||||||
Domain | 593-1199 | Deacetylase sirtuin-type | ||||
Sequence: EPETHGLLQEVANSLLKARKVVVVTGAGISTNSGIPDFRSENGLYSLIQAQFDAASQPTRSTDRFKTDGDGNGNGDGGEEPRPTKRRKVSREPSPDLDEVDRQLNEDIKARAEAEMPAASSQAADTQQAVAASDPNASENGCLSTPRPKPALPSTPKPTTTSPLSSPPREEFMLPLPLASSSLRAEDRERIAGVSQNIVSSPLSSPPPVLFDPFHPSSPSDENMSRRSSTTPSEVDEMRDLPNAMPASQASNPGKTTLPNMKGKDLFDASIWSDPTRTSVFYQFATSLRQKVREAEPTSSHKFIGHLRDRGKLVRCYTQNIDQIEEKVGLSTSLLAGPGSRGRFSRKSTANAAQLNKMVEEVSSSGEGGNAGDVGDVGASSQSPTNGSSEQTPADQRQTSSQPNGKTEEDETTTSSTTTPPNQQPKPAPRKEVPPLRSGVECVFLHGSLQLLRCFLCGQVCSWDDDDREVETLSGQQPECPHCVGATEARQERGKRALGVGKLRPDIVLYGEEHPNAHLISPIVTHDLALYPDMLLILGTSLRVHGLKVMVREFAKTVHSKGGKVVFVNFTKPPESSWGDIIDYWIQWDCDAWVADLQVRIPKLWQE | ||||||
Region | 647-773 | Disordered | ||||
Sequence: ASQPTRSTDRFKTDGDGNGNGDGGEEPRPTKRRKVSREPSPDLDEVDRQLNEDIKARAEAEMPAASSQAADTQQAVAASDPNASENGCLSTPRPKPALPSTPKPTTTSPLSSPPREEFMLPLPLASS | ||||||
Compositional bias | 655-705 | Basic and acidic residues | ||||
Sequence: DRFKTDGDGNGNGDGGEEPRPTKRRKVSREPSPDLDEVDRQLNEDIKARAE | ||||||
Compositional bias | 712-735 | Polar residues | ||||
Sequence: SSQAADTQQAVAASDPNASENGCL | ||||||
Compositional bias | 741-755 | Pro residues | ||||
Sequence: KPALPSTPKPTTTSP | ||||||
Region | 808-850 | Disordered | ||||
Sequence: PSSPSDENMSRRSSTTPSEVDEMRDLPNAMPASQASNPGKTTL | ||||||
Compositional bias | 969-1013 | Polar residues | ||||
Sequence: VGASSQSPTNGSSEQTPADQRQTSSQPNGKTEEDETTTSSTTTPP | ||||||
Region | 969-1026 | Disordered | ||||
Sequence: VGASSQSPTNGSSEQTPADQRQTSSQPNGKTEEDETTTSSTTTPPNQQPKPAPRKEVP | ||||||
Region | 1197-1236 | Disordered | ||||
Sequence: WQEPEPPKPKKKRDSGGGAAEEGREEKKKPPAQNPVALRD | ||||||
Compositional bias | 1199-1229 | Basic and acidic residues | ||||
Sequence: EPEPPKPKKKRDSGGGAAEEGREEKKKPPAQ | ||||||
Region | 1287-1380 | Disordered | ||||
Sequence: TTEAKPNPDPPTPAEVAPRAAAVMDPPTRISTPRGKAKRPRKSAPGALERPKRTPSTLNPNHGRSKKPVEEVKEEEVLETPETPSQPPVSTVEE | ||||||
Compositional bias | 1350-1366 | Basic and acidic residues | ||||
Sequence: RSKKPVEEVKEEEVLET |
Sequence similarities
Belongs to the sirtuin family. Class I subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,574
- Mass (Da)170,576
- Last updated2023-09-13 v1
- ChecksumC667035ECFC1B4A6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 655-705 | Basic and acidic residues | ||||
Sequence: DRFKTDGDGNGNGDGGEEPRPTKRRKVSREPSPDLDEVDRQLNEDIKARAE | ||||||
Compositional bias | 712-735 | Polar residues | ||||
Sequence: SSQAADTQQAVAASDPNASENGCL | ||||||
Compositional bias | 741-755 | Pro residues | ||||
Sequence: KPALPSTPKPTTTSP | ||||||
Compositional bias | 969-1013 | Polar residues | ||||
Sequence: VGASSQSPTNGSSEQTPADQRQTSSQPNGKTEEDETTTSSTTTPP | ||||||
Compositional bias | 1199-1229 | Basic and acidic residues | ||||
Sequence: EPEPPKPKKKRDSGGGAAEEGREEKKKPPAQ | ||||||
Compositional bias | 1350-1366 | Basic and acidic residues | ||||
Sequence: RSKKPVEEVKEEEVLET |