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 |