IED ID | IndEnz0002001060 |
Enzyme Type ID | protease001060 |
Protein Name |
Subtilisin-like protease 1 EC 3.4.21.- |
Gene Name | SUB1 |
Organism | Trichophyton tonsurans (Scalp ringworm fungus) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton tonsurans (Scalp ringworm fungus) |
Enzyme Sequence | MGVFRFISISLAAVSAANAAQILSMPHAQTVPHSYIVMMKDDTSDDDFNHHQSWLQSTHTHNITRRATIQNAGMRHKYNFRKMKGYSGIFDEETIKDIAKDPKVMFVEPDTIISVNGKVEQSNVPSWGLARISNSQPGANSYVYDSSAGEGITVYSVDTGVDINHEDFEGRAIWGSNQVNDGDDRDGSGHGTHTSGTMVGKEFGIAKKAKLVAVKVLGNDGSGPTSGIVAGINWCVEHARQNGGTDKAVMNMSLGGSSSSALNRAAAQAVEQGMFLSVAAGNENQDARSSSPASEPSVCTVGSSAEDDSRSSFSNWGPALDLFAPGSNIISARPGGGSQSMSGTSMAAPHVAGLAAYLMALEGISGGAVCDRLKELGSSSITDVGPGTPTNVLISNGGAKGGNPKPAPGPSPNPSQPSEPQQPAPSQPGEPGESFPGEPFPGEPFPGEPFPGESSPGESAPAPAPMPPSPQHPHTPYPGGDNFDFDGYWKKYFGGEHWRKMFGSFWN |
Enzyme Length | 507 |
Uniprot Accession Number | B8XGQ4 |
Absorption | |
Active Site | ACT_SITE 158; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 190; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 345; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | |
DNA Binding | |
EC Number | 3.4.21.- |
Enzyme Function | FUNCTION: Secreted subtilisin-like serine protease with keratinolytic activity that contributes to pathogenicity. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Compositional bias (2); Domain (2); Glycosylation (1); Propeptide (1); Region (3); Signal peptide (1) |
Keywords | Glycoprotein;Hydrolase;Protease;Secreted;Serine protease;Signal;Virulence;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..19; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 53,080 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |