| IED ID | IndEnz0002001634 |
| Enzyme Type ID | protease001634 |
| Protein Name |
Tripeptidyl-peptidase SED1 EC 3.4.14.10 Sedolisin-A |
| Gene Name | SED1 MCYG_01559 |
| Organism | Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Microsporum Arthroderma otae (Microsporum canis) Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) (Microsporum canis) |
| Enzyme Sequence | MSTMIFMYFIYIVLYASGIAANLSYHVHEKRSIPVWWQRVSRIDPHAFLPLTIALAQQNLEHAEDYLLSVSDPSSPQYAQYWTAEAVAAKFAPSEPTARKVMSWLNQSGIAPAGVRRSKSGGELYMNITAQEAEKLLHTTFYIYKHQLTNKTLAICEKYSVATFVEKYVDFITTTEQFHHGLRRRSFQDPEPRMPSGKSPGHYVELADDSFPFPYLSFGSSVGLLKNKILSDSLPSNCDKLITPDCLRALYHIPVRNTSHPDNSLGIIEFTWVGYLESDLDKFFNIFQPSMVGNRPKFESIDGGFIQTLVPSFAFNGEADLDIEYAMALTHPLNITNYQVGDIWSLGNMNNFLASLDSTYCSAVDPVYDPIYPDPTPANPPLPSGYNSSDCGTHKPTKVISISYAYEEGEFSPAYERRQCLEYLKLGLQGVTVVFASGDHGTATRDGMCGNTVIDSNQISDHEPSYVPTFPSTCPYVTSVGGTQVPANGSVLDAEVAFDTIITSSDGNVSSRLTSAGGFSNVFAVPGYQATATRDYLQRLQNKYTLPVNLNVTGFGSGRGFPDVAANAAAYATAVNGKLVKVYGTSASAPVFASVIAWINDARLNMGKQPVGFVNPVLYANPQVLNDVAKGSNYDCANLPAYHASSGWDPVTGLGTPNFDRMLDLFLQLS |
| Enzyme Length | 670 |
| Uniprot Accession Number | C5FHK0 |
| Absorption | |
| Active Site | ACT_SITE 318; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 322; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 586; /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 (5); Metal binding (4); Propeptide (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..20; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 73,464 |
| Kinetics | |
| Metal Binding | METAL 627; /note=Calcium; /evidence=ECO:0000250; METAL 628; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 647; /note=Calcium; via carbonyl oxygen; /evidence=ECO:0000250; METAL 649; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |