| IED ID | IndEnz0002019327 |
| Enzyme Type ID | protease019327 |
| Protein Name |
Probable dipeptidyl-peptidase 5 EC 3.4.14.- Dipeptidyl-peptidase V DPP V DppV |
| Gene Name | dpp5 ACLA_080850 |
| Organism | Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus clavatus Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) |
| Enzyme Sequence | MGALTWLSVVAAAASTALAMTPEKMISAPRRSEVIPNPSGEIGVFSTSQYSFEKHKRSSWWSLLDLKTGQSKILTNDSSVSEILWLGTDDSTLLYVNGTNADVPGGVELWVTQVSSFTNGYKAASLPAAFSGFKTVTTKSGDIRFVAYAQSYANGTAYNEELVEKPLSSARIYDSIYVRHWDSYLTTTFNAVFSGTLKKGNNKKGYTLDGAVKNLVSPVRNAESPYPPFGGASDYDLSPNGKWVAFKSKAPELPKANFTTAYIYLVPHDGSEKAFAINGPDSPGTPKGIKGDANSPVFSPNSEKLAYLQMKDETYEADRRVLYVYSIGSKKTIPSVAGNWDRSPDSIKWTPDGKTLIVGSEDKGRSRLFAIPATARDDFKPKNFTDGGAVSAYYFLPDRSLLVTGTAIWTNWNVYTASPAKGVIKTLASANEIDPELKGLGPSDVSEIYFKGNWTDIHAWVVYPENFDKSKKYPLAFLIHGGPQGSWADSWSSRWNPKTFADQGYVVVAPNPTGSTGFGQKLTDEIQNNWGGAPYDDLVKCWEYVNKNLPFVDTEHGIAAGASYGGFMVNWIQGNDLGRRFKALVSHDGTFVADAKISTDELWFMQREFNGTFWDARDNYRRFDPSAPEHIRQFGTPQLVIHNDKDYRLAVAEGLSLFNVLQERGVPSRFLNFPDENHWVVNPENSLVWHQQVLGWINKYSGIEKSNPGAVSLDDTIVPVVNYN |
| Enzyme Length | 724 |
| Uniprot Accession Number | A1CSW4 |
| Absorption | |
| Active Site | ACT_SITE 563; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 646; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 678; /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 (7); 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..19; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 79,926 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |