Detail Information for IndEnz0002018699
IED ID IndEnz0002018699
Enzyme Type ID protease018699
Protein Name Dipeptidyl-peptidase 5
EC 3.4.14.-
Dipeptidyl-peptidase V
DPP V
DppV
Gene Name DPP5
Organism Trichophyton tonsurans (Scalp ringworm fungus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Trichophyton tonsurans (Scalp ringworm fungus)
Enzyme Sequence MAAAKWLIASLAFASSGLAFTPEDFISAPRRGEAIPDPKGELAVFHVSKYNFDKKDRPSGWNLLNLKNGDISVLTTDSDISEITWLGDGTKIVYVNGTDSVKGGVGIWISDAKNFGNAYKAGSVNGAFSGLKLAKSGDKINFVGYGQSTTKGDLYNEAAAKEAVSSARIYDSLFVRHWDTYVGTQFNAVFSGALTKSGDKYSFDGKLKNLVHPVKYAESPYPPFGGSGDYDLSSDGKTVAFMSKAPELPKANLTTTYIFVVPHDGSRVAEPINKRNGPRTPQGIEGASSSPVFSPDGKRIAYLQMATKNYESDRRVIHIAEVGSNKPVQRIASNWDRSPEVVKWSSDGRTLYVTAEDHATGKLFTLPADARDSHKPAVVKHDGSVSSFYFVGSSKSVLISGNSLWSNALFQVATPGRPNRKLFYANEHDPELKGLGPNDIEPLWVDGARTKIHSWIVKPTGFDKNKVYPLAFLIHGGPQGSWGDSWSTRWNPRVWADQGYVVVAPNPTGSTGFGQKLTDDITNDWGGAPYKDLVKIWEHVRDHIKYIDTDNGIAAGASFGGFMVNWIQGHDLGRKFKALVSHDGTFVGSSKIGTDELFFIEHDFNGTFFEARQNYDRWDCSKPELVAKWSTPQLVIHNDFDFRLSVAEGVGLFNVLQEKGIPSRFLNFPDETHWVTKPENSLVWHQQVLGWINKWSGINKSNPKSIKLSDCPIEVVDHEAHSYFDY
Enzyme Length 726
Uniprot Accession Number B6V869
Absorption
Active Site ACT_SITE 558; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 641; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 673; /note=Charge relay system; /evidence=ECO:0000250
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity
DNA Binding
EC Number 3.4.14.-
Enzyme Function FUNCTION: Extracellular dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini. Contributes to pathogenicity (By similarity). {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (1); Glycosylation (4); Region (1); Signal peptide (1)
Keywords Aminopeptidase;Glycoprotein;Hydrolase;Protease;Secreted;Serine protease;Signal;Virulence
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
Modified Residue
Post Translational Modification
Signal Peptide SIGNAL 1..19; /evidence=ECO:0000255
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 80,059
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda