A0A4E9EIW8 · A0A4E9EIW8_GIBZA
- Proteintripeptidyl-peptidase II
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1577 (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 | 284 | Charge relay system | ||||
Sequence: E | ||||||
Active site | 288 | Charge relay system | ||||
Sequence: D | ||||||
Active site | 505 | Charge relay system | ||||
Sequence: S | ||||||
Binding site | 548 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 549 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: V | ||||||
Binding site | 573 | Ca2+ (UniProtKB | ChEBI) | ||||
Sequence: G | ||||||
Binding site | 575 | 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
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Hypocreomycetidae > Hypocreales > Nectriaceae > Fusarium
Accessions
- Primary accessionA0A4E9EIW8
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-18 | |||||
Sequence: MISPILFTTLALAGLGAA | ||||||
Chain | PRO_5041086280 | 19-1577 | tripeptidyl-peptidase II | |||
Sequence: KNIKVEETPVLPNGWEKVNQAVDPSHVLRLSIAMRQPDIENLKTGLRKRDATSGQYIQRHLCQQEALALRTPDKKDVDKVLAWLKSKGAAAKATPDKDWIHVKTTVKDAQDLLDAKIGFYQFADQEPVLRTRDYSLPESLVNSISFIHPIANFMRPVKELTTPDPDFTPSMLKSLQLDKRASIPCGQAIKPDCLREQFNITYPAYNGTSPIRFGIAGFLEEYANYEDAQDFLRIYAKPLYEARYNFSVQLINGANNSQDLFDSGNEAALDVQYAMALGYPTNITYYLADGRGPTLDDDGEQVSEEYNDNEPYLEFLDYLLDLSDDEVPHVLSVSYGDNEVSVPRKYAERVCSMFGLLTARGTTILAASGDGGAKGSSNSTCRTNDGSHKDVTMAVFPATCPWVTSVGGVAAGAAPFEGAEFSGGGFSQYFPREKWQESSIKSYVKTLDGHLDGNYNASNRGVPDISMPATSYITRLKGQQVALRGTSASTPVMAAMIALINDARVRKGKNVLGWINEVLYSDKVQAALSDVTAGESRPCDFQKGHSPAGWPAAKGWDAITGLGVPSDFQKLCRLHAIAAYNRPLQYRDAADFPSSFSSTMPTTHVAPESQDELRDIANGLLKARKVIVVTGAGISTNSGIPDFRSENGLYSLISTQLDAAQQARLQENTANDEPSDSDSRPAPKRRKILRDECLKLEQDSGETKDEIEVQLEDPDPVEEKVADSIQVEGDHEDEDQPEDPDAVPSINPRTTRSTIAVAQPPTSPLSSPPPEDFRITPPSVFRRARRSHLHDSEIPPSSSPLSSPPPVLFEPFSSHASEEDGPGSRSSTSPSEVDDTPPSLPPNLSQTNLGTGKNTLPNMKGKDMFDASIWADPLRTSVFYTFATTLRQKVRDVEPTSSHRFISHLRDRGKLVRCYTQNIDQIEEKVGLSTCLTDGPGSRGRFSRKSTANLNQLNRMVDEANAMTEANSDRSQPPSDNEASQQSQPSQSRPDIMMASQAESDTGAPEDAMTAVENLRRDLPKSGVECVFLHGSLELLRCFLCGRVCSWDDNGRQLETMSGQQPECPHCVGATVAREERGKRPLGVGKLRPDIVLYGEEHPNAHLISPIVTHDLALCPDLLLILGTSLRVHGLKVMVREFAKAVHAKGGKVVFVNYTKPPESSWGDVIDYWVEWDCDAWVSDLQEKIPKLWQTPDPPKLKKKRDSGGVGEEGEKMDAKRCTAANPIALRDTKATGAYWVSKIMRELHRITGHGPLDPREIVTPVIVAAPIEIPTVPAEPEPVEVLQNKPIAIPKRSKRSRKSAPSTLERCKKPPSTLNPNHGRTLRSTETAEPPKVEEAEIPFSHILRPERFIKESSIIDSVKGRVRKRRRIDGEEVELPSVGRRQSSQKPPEIDNSLRLPPMKPQPPTPHNSPPFERLAPMEPPHCETPPKYFINAQLQPVSPVAAPNPGPLKQVSHNTSRRVTRSQRSSMGLEEAPAPFVAGCPPPETALEWCYSHQGSYSLVRKTDYSPAETGAIAALSMLKQGEARNFVLSPQSRLSLSFDSLDAKTLLEKKYIRED |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 206-595 | Peptidase S53 | ||||
Sequence: AIKPDCLREQFNITYPAYNGTSPIRFGIAGFLEEYANYEDAQDFLRIYAKPLYEARYNFSVQLINGANNSQDLFDSGNEAALDVQYAMALGYPTNITYYLADGRGPTLDDDGEQVSEEYNDNEPYLEFLDYLLDLSDDEVPHVLSVSYGDNEVSVPRKYAERVCSMFGLLTARGTTILAASGDGGAKGSSNSTCRTNDGSHKDVTMAVFPATCPWVTSVGGVAAGAAPFEGAEFSGGGFSQYFPREKWQESSIKSYVKTLDGHLDGNYNASNRGVPDISMPATSYITRLKGQQVALRGTSASTPVMAAMIALINDARVRKGKNVLGWINEVLYSDKVQAALSDVTAGESRPCDFQKGHSPAGWPAAKGWDAITGLGVPSDFQKLCRLHAI | ||||||
Domain | 624-1218 | Deacetylase sirtuin-type | ||||
Sequence: APESQDELRDIANGLLKARKVIVVTGAGISTNSGIPDFRSENGLYSLISTQLDAAQQARLQENTANDEPSDSDSRPAPKRRKILRDECLKLEQDSGETKDEIEVQLEDPDPVEEKVADSIQVEGDHEDEDQPEDPDAVPSINPRTTRSTIAVAQPPTSPLSSPPPEDFRITPPSVFRRARRSHLHDSEIPPSSSPLSSPPPVLFEPFSSHASEEDGPGSRSSTSPSEVDDTPPSLPPNLSQTNLGTGKNTLPNMKGKDMFDASIWADPLRTSVFYTFATTLRQKVRDVEPTSSHRFISHLRDRGKLVRCYTQNIDQIEEKVGLSTCLTDGPGSRGRFSRKSTANLNQLNRMVDEANAMTEANSDRSQPPSDNEASQQSQPSQSRPDIMMASQAESDTGAPEDAMTAVENLRRDLPKSGVECVFLHGSLELLRCFLCGRVCSWDDNGRQLETMSGQQPECPHCVGATVAREERGKRPLGVGKLRPDIVLYGEEHPNAHLISPIVTHDLALCPDLLLILGTSLRVHGLKVMVREFAKAVHAKGGKVVFVNYTKPPESSWGDVIDYWVEWDCDAWVSDLQEKIPKLWQTPDPPKLKKK | ||||||
Region | 683-876 | Disordered | ||||
Sequence: LQENTANDEPSDSDSRPAPKRRKILRDECLKLEQDSGETKDEIEVQLEDPDPVEEKVADSIQVEGDHEDEDQPEDPDAVPSINPRTTRSTIAVAQPPTSPLSSPPPEDFRITPPSVFRRARRSHLHDSEIPPSSSPLSSPPPVLFEPFSSHASEEDGPGSRSSTSPSEVDDTPPSLPPNLSQTNLGTGKNTLPN | ||||||
Compositional bias | 689-725 | Basic and acidic residues | ||||
Sequence: NDEPSDSDSRPAPKRRKILRDECLKLEQDSGETKDEI | ||||||
Compositional bias | 764-779 | Polar residues | ||||
Sequence: INPRTTRSTIAVAQPP | ||||||
Compositional bias | 837-873 | Polar residues | ||||
Sequence: EDGPGSRSSTSPSEVDDTPPSLPPNLSQTNLGTGKNT | ||||||
Region | 982-1009 | Disordered | ||||
Sequence: TEANSDRSQPPSDNEASQQSQPSQSRPD | ||||||
Region | 1207-1232 | Disordered | ||||
Sequence: WQTPDPPKLKKKRDSGGVGEEGEKMD | ||||||
Compositional bias | 1211-1232 | Basic and acidic residues | ||||
Sequence: DPPKLKKKRDSGGVGEEGEKMD | ||||||
Region | 1304-1358 | Disordered | ||||
Sequence: KPIAIPKRSKRSRKSAPSTLERCKKPPSTLNPNHGRTLRSTETAEPPKVEEAEIP | ||||||
Compositional bias | 1325-1343 | Polar residues | ||||
Sequence: RCKKPPSTLNPNHGRTLRS | ||||||
Compositional bias | 1344-1358 | Basic and acidic residues | ||||
Sequence: TETAEPPKVEEAEIP | ||||||
Region | 1393-1432 | Disordered | ||||
Sequence: VELPSVGRRQSSQKPPEIDNSLRLPPMKPQPPTPHNSPPF | ||||||
Compositional bias | 1417-1432 | Pro residues | ||||
Sequence: PPMKPQPPTPHNSPPF |
Sequence similarities
Belongs to the sirtuin family. Class I subfamily.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,577
- Mass (Da)173,513
- Last updated2020-08-12 v1
- Checksum25A4BF05D16D9D9A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 689-725 | Basic and acidic residues | ||||
Sequence: NDEPSDSDSRPAPKRRKILRDECLKLEQDSGETKDEI | ||||||
Compositional bias | 764-779 | Polar residues | ||||
Sequence: INPRTTRSTIAVAQPP | ||||||
Compositional bias | 837-873 | Polar residues | ||||
Sequence: EDGPGSRSSTSPSEVDDTPPSLPPNLSQTNLGTGKNT | ||||||
Compositional bias | 1211-1232 | Basic and acidic residues | ||||
Sequence: DPPKLKKKRDSGGVGEEGEKMD | ||||||
Compositional bias | 1325-1343 | Polar residues | ||||
Sequence: RCKKPPSTLNPNHGRTLRS | ||||||
Compositional bias | 1344-1358 | Basic and acidic residues | ||||
Sequence: TETAEPPKVEEAEIP | ||||||
Compositional bias | 1417-1432 | Pro residues | ||||
Sequence: PPMKPQPPTPHNSPPF |