| IED ID | IndEnz0002003787 |
| Enzyme Type ID | protease003787 |
| Protein Name |
Probable dipeptidyl-aminopeptidase B DPAP B EC 3.4.14.5 |
| Gene Name | dapB AFUA_3G07850 |
| Organism | Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Neosartorya fumigata (Aspergillus fumigatus) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) |
| Enzyme Sequence | MRRSDGHEETSEFLPMTHSRSVSAASQTSTDSSLSTESLFPREQKPFPNAMGGMALADDDKYRDLEDGEAEQSEPFLSSSKKAATGGGRARRIFWILVLLCLGGWLLAFVLFLTGGRANYQTASDALQAHGADSALGSTSTSSGKPVTLHQVLGGQWNPRYHAIGWVAGPNNEDGLLVEKGGDEKQGYLRVDDIRSRKGNNTGRESRVLMRKPIVHVDGQAIVPSNVWPSPDLKKVLLISEQQKNWRHSFTGKYWVLDVDSQTAQPLDPSAPDGRVQLALWSPASDAVVFVRDNNLYLRRLSSDSVVAITKDGGENLFYGVPDWVYEEEVISGNSVTWWSNDAKYIAFFRTNETSVPEFPVQYYISRPSGKKPLPGLENYPDVREIKYPKPGAPNPVVDLQFYDVEKNEVFSVQVADDFADDDRIIIEVLWASEGKILVRSTNRESDILKVYLIDTQSRTGKLVRSEDVAGLDGGWVEPSQSTRFVPADPNNGRPHDGYIDTVPYNGYDHLAYFSPLDNPNALMLTSGEWEVVDAPAAVDLQRGLVYFVGTKEAPTQRHVYRVQLDGSNLNPLTDTSKPGYYDVSFSHGTGYALLTYKGPSIPWQAIINTHGDEITYEDRIEDNAQLTKMVEAYALPTEVYQNVTVDGYTLQVVERRPPHFNPAKKYPVLFYLYGGPGSQTVDRKFTVDFQSYVASSLGYIVVTVDGRGTGFIGRKARCIVRGNLGFYEAHDQIATAKMWAAKSYVDETRMAIWGWSFGGFMTLKTLEQDAGRTFQYGMAVAPVTDWRFYDSIYTERYMHTPQHNPNGYDNSTITDMAALSESVRFLVMHGASDDNVHLQNTLVLIDKLDLSNVENYDVQFYPDSDHSIYFHNAHMMVYHRLSDWLVNAFNGEWHLIAKPVPDESMWERMKRSLRLLSP |
| Enzyme Length | 919 |
| Uniprot Accession Number | Q4WX13 |
| Absorption | |
| Active Site | ACT_SITE 757; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 834; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 867; /note=Charge relay system; /evidence=ECO:0000250 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.; EC=3.4.14.5; |
| DNA Binding | |
| EC Number | 3.4.14.5 |
| Enzyme Function | FUNCTION: Type IV dipeptidyl-peptidase which removes N-terminal dipeptides sequentially from polypeptides having unsubstituted N-termini provided that the penultimate residue is proline. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (3); Chain (1); Compositional bias (1); Glycosylation (4); Region (1); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Glycoprotein;Hydrolase;Membrane;Protease;Reference proteome;Serine protease;Signal-anchor;Transmembrane;Transmembrane helix;Vacuole |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Lysosome-like vacuoles. {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 103,079 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |