IED ID | IndEnz0002006992 |
Enzyme Type ID | protease006992 |
Protein Name |
Probable dipeptidyl-aminopeptidase B DPAP B EC 3.4.14.5 |
Gene Name | DAPB GLRG_06464 |
Organism | Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola) |
Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Hypocreomycetidae Glomerellales Glomerellaceae Colletotrichum Colletotrichum graminicola species complex Colletotrichum graminicola (Maize anthracnose fungus) (Glomerella graminicola) Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize anthracnose fungus) (Glomerella graminicola) |
Enzyme Sequence | MDAPATASRQPIAEEPRMSQESSLSTVSTTSLVFDRLHEHNEKSYHSSSQRRRAPSASRGGYADHPDDDDDDDESYKEADTNDLETGPFLAPASVMMRRVGVDRGLKKVILILAAAFLFAWGAALFVFLSNKSYKHASTIDHDPSATSRGSGKPVTLDQVISGFWYPTSHSISWIEGPNGEDGLLLEQGARGKDYLVVEDVRSGNKDSQVSANVVQSRTLMKNPWINVGGRQLAPSDTRPSKDMKKVLVSTDRQRNWRYSYTALYWIFDVETQTAEALDPEHPDGRVQLATWSPQSNAIVFTRDNNLFLRKLDGDKKVTQITNDGGPEYFYGIPDWVYEEEVFATNSATWYSEDGKYVAFLRTNETGVPEYPLQYFLSRPSGKEKPPGEETYPDEKRIKYPRAGSHNPVVDLLFFDVERGDVFSVDIDGGFADDDRLINMVLWANDKVLIKETNRVSDIMRVVLVDVVARTGKTVNTIDVGELDGGWFEISHTTQFIPADPANGRPQDGYIDTVVHGNGDHIAYFSPMDNAEPVYLTGGDWEVDDGPSAVDLKNNLVYFVATKESSIQRHVYSVHLNRSDLKPFTDTKFESYYDISFSSGAGYALLSYQGPKIPWQKVVSTPSSPVSYEHVVEKNEDLAENAKKYELPILNYGTLKVDGVELNYVERRPPHFDEKKKYPVLFQQYSGPGSQSVHKKFAVDFQSYVASALGYLVVTVDGRGTGFIGRKNRVLIRDHLGYWEAHDQIAAAQAWAAKKYVDPARIAIWGWSYGGFNTLKTLEMDAGRTFSYGMAVAPVTDWRFYDSIYTERYMRTPQLNPSGYDQTAVSNVSALAGNVRWLMMHGVGDDNVHYQNTLTLLDKLDLNGIENYDVHVFPDSDHGIYFHGANRIVYDKLSNWLINAFNGEWLKVAGAKPIVEPKARV |
Enzyme Length | 921 |
Uniprot Accession Number | E3QKD2 |
Absorption | |
Active Site | ACT_SITE 768; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 845; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 878; /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 (2); 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 | 103,378 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |