| IED ID | IndEnz0002001350 |
| Enzyme Type ID | protease001350 |
| Protein Name |
Subtilisin-like protease 2 EC 3.4.21.- |
| Gene Name | SUB2 |
| Organism | Trichophyton verrucosum (Cattle ringworm fungus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton verrucosum (Cattle ringworm fungus) |
| Enzyme Sequence | MQLLNFGLLLLPFVAGDLAPQPEPLLAGPSDVVPGQYIVTLKEGLTSAQIRDHKKWVSSVHRANLDSFAAGASGVETEGIMKHFHIHDLNMYSGGFDEKTVEDLSRNPYVKSVHPDQHVYLAKTVTQRQARWGLGYMSSKGKPVPLHSTLVDYSYDDKAGEGVWAYVLDTGINVNHIEFEGRAILGHNAIPNKPHTDEFGHGTYVAGIIAGKTYGVAKKANVVSAKAFDTGSSTYNYILETYDWIVRNITDSNRKNKAVINLSISGAKYQPFDDAVEKAFKAGITTVVAAGNDGKDAKNNTPASSPNAITVGAVRWENTRPSFSNYGKLVDIWAPGELIKSCWKGGNNATSTQSGTSAASPHVAGLVAYLMSIENLPSPSAVTARVLNLTIPNLVKDAKDSPNRVAYNGIQERKFKLPK |
| Enzyme Length | 419 |
| Uniprot Accession Number | Q5VJ76 |
| Absorption | |
| Active Site | ACT_SITE 169; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 201; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU01240; ACT_SITE 357; /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); Domain (2); Erroneous gene model prediction (1); Glycosylation (4); Propeptide (1); 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..16; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 45,337 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |