| IED ID | IndEnz0002018989 |
| Enzyme Type ID | protease018989 |
| Protein Name |
Probable dipeptidyl-aminopeptidase B DPAP B EC 3.4.14.5 |
| Gene Name | dapB ste13 AN2946 |
| Organism | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Nidulantes Emericella nidulans (Aspergillus nidulans) Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
| Enzyme Sequence | MRSSEDREDSELLPANRPRSPSRSSYDSDDSGLSVDSILEEQKYNAATNETLGLPQEMRYHDEEGGEAGSNEALHTKASSSRSRRLLWLVVLLCCGGWVVAFVLFITQGRADYRTATDELQSDNSGSFSDGTSSGKPLTLQQVLSGVFLPRGHAISWVAGPDGEDGLLIERGEDDEAGYLRINDIRQDGKVNRVLMQKPTVGVDGRTIKPSATRPSPDLKKVLIISNQEKNWRHSFTASYWIFDVETQTAEPLDPNNIDGRVQLALWSPKSDAIAFVRDNNLYLRKLSSERVVPITKDGGEQLFYGVPDWVYEEEVFSGNSVTWWSEDGSQIAFIRTNESAVPEFPVQYFLSRPSGKKPQPGLENYPEVREIKYPKAGAPNPFVNLQFYDVEQGEVFSVDTPDDFDDDDRLIIEVIWAAKGKVLVRTTNRESDILKVFLVDTESRESKLIRIQDISELDGGWVEPTQSVRFIPADPDKGRPFDGYLDTVVHEGYDHLAYFTPLDNPEPIMLTSGEWEVVDAPTAVDLTRGLVYFIATKEAPTERHLYRVRLDGSDLTPLTDTSQPGYYSVSFSDGAGYALLSYQGPSIPWQSIISTEGEKTTTLRIIEDNTDLSKLVAQYALPTENYQNITIDGFTLQVVERRPPHFNPARKYPVLFHLYGGPGSQTVDRRFNVDFQSYVAASLGYIVVTVDGRGTGFIGRAARCIIRGNIGHYEAIDQIATAKNWAQKPYVDESRMAIWGWSYGGFMTLKTLEQDAGETFQYGMAVAPVTDWRFYDSVYTERYMHTPQHNPTGYDNTSISDMAALHNNVRFLVIHGASDDNVHIQNTLTLIDKLDLASVQNYDVHFYPDSDHSIFFHNAHTMVYERLASWLVNAFNGEWHRTANPVPDESMLRRLAKRVWPGFAH |
| Enzyme Length | 906 |
| Uniprot Accession Number | Q5B934 |
| Absorption | |
| Active Site | ACT_SITE 743; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 820; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 853; /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); Erroneous gene model prediction (2); 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 | 101,960 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |