Detail Information for IndEnz0002005180
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