Detail Information for IndEnz0002018906
IED ID IndEnz0002018906
Enzyme Type ID protease018906
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name dapB NFIA_069310
Organism Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Aspergillaceae Aspergillus Aspergillus subgen. Fumigati Aspergillus fischeri Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus)
Enzyme Sequence MRPSDDHGETSEFLPITRSRSVSAASQTSTDSSLSTESLFPGEQKPFPNVNGTMALADDDQYRDLEDGEVEQTEPFLASSKKAATGGGRARRIFWILVLLCLGGWLLAFALFLTGGRANYQTASDALQAHGADSALGSTSTSSGKPVTLQQVLAGQWNPRYHAIGWVAGPNNEDGLLVEKGGDEKQGYLRVDDIRSRKGNDTGRESRVLMWKPIVHVDGKAIVPSNVWPSPDLKKVLLISEQQKNWRHSFTGKYWVLDVDSQTAQPLDPSAPDGRVQLALWSPASDAVVFVRDNNLYLRRLSSDSVVVITKDGGENLFYGVPDWVYEEEVISGNSVTWWSNDAKYIAFFRTNETSVPEFPVQYYISRPSGKKPLPGLENYPDVREIKYPKPGAPNPVVDLQFYDVDKNEVFSVEVADDFADDDRIIIEVLWASEGKVLVRSTNRESDILKVYLIDTKSRTGKLVRSEDVAGLDGGWVEPSQSTRFIPADPNNGRPHDGYIDTVPYNGYDHLAYFSPLDSPNALMLTSGEWEVVDAPAAVDLQRGLVYFVGTREAPTQRHVYRVQLDGSNLKPLTDTSKPGYYDVSFSHGTGYALLTYKGPSIPWQAIIKTQGDEITYEDRIEDNAQLTKMVEAYALPTEIYQNVTVDGYTLQLVERRPPHFNPAKKYPVLFYLYGGPGSQTVDRKFTVDFQSYVASSLGYIVVTVDGRGTGFIGRKARCIVRGNLGFYEAHDQIATAKMWAAKSYVDETRMAIWGWSFGGFMTLKTLEQDAGQTFQYGMAVAPVTDWRFYDSIYTERYMHTPQHNPSGYDNSTITDMAALSESVRFLVMHGASDDNVHLQNTLVLIDKLDLSNVENYDLQFYPDSDHSIYFHNAHTMVYDRLSDWLVNAFNGEWHLIAKPVPDESMWERMKRSLPLLYP
Enzyme Length 919
Uniprot Accession Number A1D7R6
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 102,984
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda