Detail Information for IndEnz0002018908
IED ID IndEnz0002018908
Enzyme Type ID protease018908
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name DAPB PAAG_01724
Organism Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Onygenales incertae sedis Paracoccidioides Paracoccidioides lutzii Paracoccidioides lutzii (strain ATCC MYA-826 / Pb01) (Paracoccidioides brasiliensis)
Enzyme Sequence MAAEKGESSDEERKPLTRDSMEYRDSSNSLHYSSSAASLSLAVIDRINGSTHDTGPNEIGRGDRDYSDDGEYDLEEADYIPSGGKPVQKKVKIVLGFLLFLCLSGWSLSFVLFLFGGHESSKTSNVYDDNISDTGSQGNKITLDEVLDGTWSPAFHDISWIPGPNGEDGLLLERGASISNGYLRVEDIVSRKDPKSSKKPIVLMQKAYFNVSGEAVFPSRVWPSPDLKTVLVLSNEEKNWRHSFTGKYWLFDVESQTGQPLDPAAKDQRVQLASWSPRSDAVVFTRDNNMFLRKLSSNEVMKITTNGGVNLFYGVPDWVYEEEVYSGNSVTWWADDGEYIAFLRTNESSVPEYPVQYFVSLPNGEISKPGEESYPETRKIKYPKAGAPNPIVDLQFFDVGKDEVFSVDIKGDFADSNRLITEVVWASNGKVIVRSTNRESDVLHVAVIDVLSRTGKIVRKEDINALDGGWVEPSQTARFIPADPDNGRLNDGYIDTVIYEGRDQLAYYTPVDNPNPIVLTKGHSEVVQAPSGVDLKRGLVYFVVAGNEPWERHIYSVNFDGTSIQPVTNVSESSYYDVSFSNGAGYAFLKYAGPQVPWQKVISTPANEVTFEETIEENNRLSERLRQYTLESKIYQYIDIDGFSLPVLERRPPNFNQTKKYPVLFYLYGGPGSQTVNKKFNVDFQSYVAANLGYIVVTVDGRGTGFIGRKARCVIRGNLGHFESRDQIQAAKIWAAKPYVDESRISIWGWSYGGFMALKTIEQDGGRTFKYGIAVAPVTDWRYYDSIYTERYMHTPQRNPGGYDNAAISNTTALANNIRFLVMHGTADDNVHIQNSLTFIDKLDVNNVHNYDVHFFPDSDHSIYFHNAHKIVYSRLADWLVNAFNGEWLKTYNPAPNDSIFRRAAIWVGLSI
Enzyme Length 912
Uniprot Accession Number C1GT79
Absorption
Active Site ACT_SITE 751; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 828; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 861; /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 (1); Glycosylation (7); Region (2); 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 102,461
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda