| IED ID | IndEnz0002000084 |
| Enzyme Type ID | protease000084 |
| Protein Name |
Aspartic endopeptidase PEP1 EC 3.4.23.18 Aspergillopepsin I |
| Gene Name | PEP1 TRV_03007 |
| Organism | Trichophyton verrucosum (strain HKI 0517) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton verrucosum (Cattle ringworm fungus) Trichophyton verrucosum (strain HKI 0517) |
| Enzyme Sequence | MVQISQIGAVLAVCSTLTVAAPTKGKARFNVPQVAVPMKAVHHPAVAYARALHKFGMKVPKAVSDAARGSVPTTPTKDDEQYVTQVTVGQGKLNLDLDTGSGDLWVFSTETPKDQSQGHNLYMPTSKSKRLDGYSWEITYGDMSSAGGDVFLDTVSIGNVTASSQAVESAKKVSDQFAKDKATDGLMGLSFSVLNTVQPKPQTTFFDTVLKQLEKPLFTCTLKHGQPGSYDFGYIDDSKHSGEIAYTNVDNSQGWWGFTAESYSIGGGSNSTHSFHGAQHHGARGSSIDGIADTGTTLMLLSDDVVQEYYKQVQGAKNDQQQGGWVFPCDAKLPDFTLSISGYNAVVPGKFMNYQAVGSVCFGGLQSVGSSGGVPNIFGDVFLKSQFVVWDTEGPRIGFAPQA |
| Enzyme Length | 403 |
| Uniprot Accession Number | D4D7C5 |
| Absorption | |
| Active Site | ACT_SITE 98; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 293; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity. Generally favors hydrophobic residues in P1 and P1', but also accepts Lys in P1, which leads to activation of trypsinogen. Does not clot milk.; EC=3.4.23.18; |
| DNA Binding | |
| EC Number | 3.4.23.18 |
| Enzyme Function | FUNCTION: Secreted aspartic endopeptidase that allows assimilation of proteinaceous substrates. Can catalyze hydrolysis of the major structural proteins of basement membrane, elastin, collagen, and laminin. Thought to play a significant role in virulence (By similarity). {ECO:0000250}.; FUNCTION: Can catalyze hydrolysis of the major structural proteins of basement membrane, elastin, collagen, and laminin. Thought to play a significant role in virulence (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Chain (1); Disulfide bond (1); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1) |
| Keywords | Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Signal;Virulence;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {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 | 43,002 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |