IED ID | IndEnz0002018474 |
Enzyme Type ID | protease018474 |
Protein Name |
Probable dipeptidyl-peptidase 5 EC 3.4.14.- Dipeptidyl-peptidase V DPP V DppV |
Gene Name | dpp5 AN2572 |
Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
Enzyme Sequence | MGALRWLSLAAAASSALALTPEQLISAPRRSEAIPNPSGNIAVFSSSQYSFDTHESSSAWNLLDLRSGKITPLTNDSNVSEIVWLNDSTLLYINGTNAQIPGGSELWVSGLSNFPSGYKAASLPASFSGLKAVTTKSGDIKFVAYAQSYRNGTAYNEELAETYLSSARIYDSIYVRHWDTYLTTTFNAVFSGTLKKTQHARYASAGSLKNLVAPIPNAESPYPPFGGSSDYDISADGKWVAYKSKAPDVPQANHTTAYIYLVPHDGSETPVPINGPGSAPEGIEGDSNNPVFSPDSKSLAYLQMKDPTYESDRRVIYIYDLASKKITPLATEWDRSPDSLKWTDKSTIVAGSEDEGSGNLFLIPVKKATGDFIPEKLTNGKYASAFYLASGNTLVVTGSTLYSSWYVDLVSLNPKRGTIKNLVSAHEIDPELSGLGPEDISDIWFAGNWTDIHAWVIYPEGFDKSKTYPLAFLIHGGPQGAWYNSWSSRWNPKVFADQGYVVVAPNPTGSTGYGDELTDAIQNNWGGAPYEDLVKAWEYVRDNLDYVDTDRGVAAGASYGGFMVNWIQGSDLGREFKALVTHDGTFVADAKISTEELWFMEREFNGTFWDVRDNYRRFDPSAPERILRFATPHLIIHNDLDYRLPVAEGLSLFNVLQERGVPSRFLNFPDENHWVTSPENSLVWHQQVLGWLNKYSGIAEDNEDAVTLEDTVVPVVNINPPA |
Enzyme Length | 722 |
Uniprot Accession Number | Q5BA58 |
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. {ECO:0000250}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (1); Glycosylation (8); Signal peptide (1) |
Keywords | Aminopeptidase;Glycoprotein;Hydrolase;Protease;Reference proteome;Secreted;Serine protease;Signal |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: 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 | 79,446 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |