Detail Information for IndEnz0002018989
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