| IED ID | IndEnz0002003781 |
| Enzyme Type ID | protease003781 |
| Protein Name |
Probable dipeptidyl-aminopeptidase B DPAP B EC 3.4.14.5 |
| Gene Name | dapB BC1G_13641 |
| Organism | Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Leotiomycetes Helotiales Sclerotiniaceae Botrytis Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea) Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis cinerea) |
| Enzyme Sequence | MAGHPEENAQLLSTEQESMSRNSSDSVASTASTTSLVFDRIGERVAANGSEKPTMVTPKFPPRGERAYADDEHTQIHLEEEEEKDYDMEDGAFLTNGATNKSVDKKLRRLIWIIGGVFIGAWVLALFIFLGKQAYKHSSESPHDPQATSSRGSGKKVTMDQVMGGQWRATKHSISWIEGANGEDGLLLEQGSVGKDYLIVEDVRTQSPSAVGTLDTMTLMKNGYFEVAGRSLTPSKVYPSKDLKKVLVATDVQSNWRHSFYAKYWIFDVETQTAEPLDPVDLDGRVQLASWSPKSDAIVFTRDNNMYLRKLASPTVVQITVDGGPEFFYGVPDWVYEEEVFAGASATWWDDSGKYIAFLRTNESEVPEYPVQYFVSRPSGKDPLPGEENYPEVREIKYPKAGAPNPTVDLLFYDISKAEVFEVKIAGGFEPKDLLITEVVWAGSTGKALIRETNRESDVLRVVLVDVVAREGKTVRFTDIAKLDGGWFEVSEDTRYIPADPANGRPHDGYIDTIIHENYDHLGYFTPMDNSEPILLTSGDWEVVKAPSAVDLKNNIVYFISTKESPITRQLYSVKLDGTDLKAITDTSTEGYYGASFSKGAGYVLLNYNGPNIPWQKVISTPSNDNQYTHIIEENKGLADMAKKHELPILIYQTVTVDGFELQVVERRPPHFNPKKKYPVLFYLYGGPGSQTVSKSFGVDFQSYIASNLGYIVVTVDGRGTGFIGRKARTIIRGNIGHYEARDQIETAKIWASKKYVDESRMAIWGWSYGGFMTLKTLEQDAGETFSYGMAVAPVTDWRFYDSIYTERYMHTPQHNPGGYDNTSISDVKSLAKNVRFLVMHGVADDNVHMQNTLTLLDKLDLAGVENYDVHVFPDSDHSIYFHNANRIVYDKLNNWLINAFNGEWLRTANAVPLEIDAAKV |
| Enzyme Length | 921 |
| Uniprot Accession Number | A6SL49 |
| 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 (2); Region (3); Topological domain (2); Transmembrane (1) |
| Keywords | Aminopeptidase;Glycoprotein;Hydrolase;Membrane;Protease;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 | 103,088 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |