| IED ID | IndEnz0002009178 |
| Enzyme Type ID | protease009178 |
| Protein Name |
Tripeptidyl-peptidase sed5 EC 3.4.14.10 Sedolisin-E |
| Gene Name | sed5 sedE AFUA_7G06220 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MYPLDGSARPHPPGTTRLNSVEPDKQIGFTVLVRPQTGAPRLPDLAQWQAIPIAERQFLSTAGFERTYGSSEDDIVSVASFLEKAGMTIRSRHAGAGTVEVQAKTCQIHSVFAVQLLYYRGQLRPAARKRRDDKQPAEETYIGFEGCISLPAALHDKVIHIFGLDTRTFGASGGYSGDPPRAQRLIVAELAALYGFPAGVDASQQTIGIFSGEGNDDKGQSLSNYRPADVAAYFNNQTVGYNRAPTVVPVSLTVADQTYRNDPDHPTQELSQDIMTAATIAQGCTVNVYFSDLTEQGWLAFLTRVLFPQGEEKRPTIVSISWTMYDEQTYRDRLSFLFQRLAVVGTSVFAIAGDWGANNNIIDGQPHVGWPGSDPWVTCVGGTVVGNVRSSGAFTEHAWSDRDNPDSQFTIDGHLGVTGGGMSRVFATPPYQLSSGISAVTDCNGERWTGGRFIPDITGMVGFRGFIVNGKRNYFIGTSCSTPLYAGLFAALASALGGGGEGGVLFGPLNTVLYQIDRGVYRDITFGHNDSGDMPACAYFAAGEGYDTVSGLGSVDGRRTLEELRRIYWPKTKGFGCFRN |
| Enzyme Length | 580 |
| Uniprot Accession Number | Q4WGU1 |
| Absorption | |
| Active Site | ACT_SITE 269; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 273; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 479; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal tripeptide from a polypeptide.; EC=3.4.14.10; |
| DNA Binding | |
| EC Number | 3.4.14.10 |
| Enzyme Function | FUNCTION: Secreted tripeptidyl-peptidase which degrades proteins at acidic pHs and is involved in virulence. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Domain (1); Glycosylation (2); Metal binding (5); Propeptide (1); Region (1); Signal peptide (1) |
| Keywords | Calcium;Glycoprotein;Hydrolase;Metal-binding;Protease;Reference proteome;Secreted;Serine protease;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..?; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 62,768 |
| Kinetics | |
| Metal Binding | METAL 523; /note=Calcium; /evidence=ECO:0000250; METAL 524; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 543; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 545; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 547; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |