IED ID | IndEnz0002019020 |
Enzyme Type ID | protease019020 |
Protein Name |
Probable dipeptidyl-peptidase 5 EC 3.4.14.- Dipeptidyl-peptidase V DPP V DppV |
Gene Name | DPP5 ARB_06651 |
Organism | Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Arthrodermataceae (dermatophytes) Trichophyton Arthroderma benhamiae (Trichophyton mentagrophytes) Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton mentagrophytes) |
Enzyme Sequence | MAAAKWLIASLAFASSGLAFTPEDFISAPRRGEAIPDPKGELAVFHVSKYNFDKKDRPSGWNLLNLKNGDISVLTTDSDVSEITWLGDGTKVVYVNGTDSVKGGVGIWISDAKNFGNAYKAGSVNGAFSGLKLAKSGDKINFVGYGQSTTKGDLYNEAAAKEAVSSARIYDSLFVRHWDTYVSTQFNAVFSGALTKNGDKYSFDGKLKNLVQPVKYAESPYPPFGGSGDYDLSSDGKTVAFMSKAPELPKANLTTSYIFLVPHDGSRVAEPINKRNGPRTPQGIEGASSSPVFSPDGKRIAYLQMATKNYESDRRVIHIAEVGSNKPVQRIASNWDRSPEAVKWSSDGRTLYVTAEDHATGKLFTLPADARDNHKPEVVKHDGSVSSFYFVGSSKSVLISGNSLWSNALYQVATPGRPNRKLFYANEHDPELKGLGPNDIEPLWVDGARTKIHSWIVKPTGFDKNKVYPLAFLIHGGPQGSWGDNWSTRWNPRVWADQGYVVVAPNPTGSTGFGQKLTDDITNDWGGAPYKDLVKIWEHVHNNIKYIDTDNGIAAGASFGGFMVNWIQGQDLGRKFKALVSHDGTFVGSSKIGTDELFFIEHDFNGTFFEARQNYDRWDCSKPELVAKWSTPQLVVHNDFDFRLSVAEGVGLFNVLQEKGVPSRFLNFPDETHWVTKPENSLVWHQQVLGWVNKWSGINKSNPKSIKLSDCPIEVVDHEAHSYFDY |
Enzyme Length | 726 |
Uniprot Accession Number | D4ARB1 |
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 (5); Region (1); Signal peptide (1) |
Keywords | Aminopeptidase;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal;Virulence |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21247460}. |
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 | 80,085 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |