| IED ID | IndEnz0002018949 |
| Enzyme Type ID | protease018949 |
| Protein Name |
Probable dipeptidyl-aminopeptidase B DPAP B EC 3.4.14.5 |
| Gene Name | DAPB SMAC_05958 |
| Organism | Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Sordaria Sordaria macrospora Sordaria macrospora (strain ATCC MYA-333 / DSM 997 / K(L3346) / K-hell) |
| Enzyme Sequence | MPPFTYSDDTLRSGRDRFRDHSPSQHRRSMSQETDSSASTTSIVFDRIQERLDTKEFTPRGTDGDDDGSLKDELNNDDLETGPFLGNADSSSRSDQRSPGDGQRMDRSLRRWLFIVSGVLVATWVIGLFVFVSSKAYKPSSSFAHDPQATVTHGTGKKVTLDQVLNNQWRAKSHSISWIAGANGEDGLLLEKEGVGKDYLVVEDVRAQNPSSVQASKSKALIKEKLFEFANKTYWPSITVPSRDLKKVLLATDVKNNWRHSYYAVYWIFDVETQQVEPLVPYDVEARLQLASWSPTSDAIVYTRDNNMFLRKLGSDKIVQITRDGSADVFNGVPDWVYEEEVLASGVATWWSEDGQYVAFLRTNETGVPEYPIQYFVSRPSGEEPKPGEENYPEVRQIKYPKAGAHNPIVDLKFYDVKRGDVFSVDISGRFADDDRLITEVVWAGKQVLIKETNRVSDVMRVVLVDVGSRTGKAVRTVDVNAIDGGWFEISHKTKFIPADPVNGRPDDGYVDTIIHDNGDHLAYFTPLDNPEPIMLTSGDYEVVDAPSAVDLQRNLVYFVSTKESSIQRHVYQVKLTGEDMTPVTDTSKEGYYAISFSTGAGYAMVSYQGPDIPWQKVISTPSNPDKYEYVVEENKDLAEAAKKHELPINIYGTINVDGVDLNYVERRPPHFDKNKKYPVLFQQYSGPVSQTVKKTFAVDFQSFVAAGLGYICVTVDGRGTGFIGRKNRVIIRGDLGHWESHDQIAAAKHWAQKDYIDEDRLAIWGWSYGGYMTLKTLEQDAGQTFKYGMAVAPVTDWRFYDSIYTERYMRTPQTNLEGYDSAAVTNATALSQNVRFLLMHGVADDNVHMQNSLTLLDALDQRSVENYDVHVFPDSDHGIYFHNANRIVFDKLTNWLVNAFNGEWLKIANAQPNGMKKRAAPTA |
| Enzyme Length | 924 |
| Uniprot Accession Number | D1Z9B4 |
| Absorption | |
| Active Site | ACT_SITE 768; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 845; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 878; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084 |
| 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; Evidence={ECO:0000255|PROSITE-ProRule:PRU10084}; |
| 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 (3); Glycosylation (3); 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 | 104,058 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |