IED ID | IndEnz0002005180 |
Enzyme Type ID | protease005180 |
Protein Name |
Probable vacuolar protease A EC 3.4.23.25 Aspartic endopeptidase PEP2 Aspartic protease PEP2 |
Gene Name | PEP2 TRV_05606 |
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 | MKGSLLLAGATLLGCTSAKLHSLKLKKVSLKEQLEHADIDVQIKSLGQKYMGIRPEQHEQQMFKEQTPIEAESGHNVLIDNFLNAQYFSEISIGTPPQTFKVVLDTGSSNLWVPGKDCSSIACFLHSTYDSSASSTYSKNGTKFAIRYGSGSLEGFVSQDSVKIGDMTIKNQLFAEATSEPGLAFAFGRFDGIMGMGFSSISVNGITPPFYNMIDQGLIDEPVFSFYLGDTNKEGDQSVVTFGGSDTKHFTGDMTTIPLRRKAYWEVDFDAISLGEDTAALENTGIILDTGTSLIALPTTLAEMINTQIGATKSWNGQYTLDCAKRDSLPDVTFTVSGHNFTIGPHDYTLEVSGTCISSFMGMDFPEPVGPLAILGDSFLRRYYSVYDLGKGTVGLAKAK |
Enzyme Length | 400 |
Uniprot Accession Number | D4DEN7 |
Absorption | |
Active Site | ACT_SITE 105; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094; ACT_SITE 289; /evidence=ECO:0000255|PROSITE-ProRule:PRU10094 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.; EC=3.4.23.25; |
DNA Binding | |
EC Number | 3.4.23.25 |
Enzyme Function | FUNCTION: Vacuolar aspartic endopeptidase which is probably also secreted and contributes to virulence. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (2); Chain (1); Disulfide bond (2); Domain (1); Glycosylation (2); Propeptide (1); Signal peptide (1) |
Keywords | Aspartyl protease;Disulfide bond;Glycoprotein;Hydrolase;Protease;Secreted;Signal;Vacuole;Virulence;Zymogen |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Vacuole lumen {ECO:0000250}. Secreted {ECO:0000250}. |
Modified Residue | |
Post Translational Modification | |
Signal Peptide | SIGNAL 1..18; /evidence=ECO:0000255 |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 43,361 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |