Detail Information for IndEnz0002019381
IED ID IndEnz0002019381
Enzyme Type ID protease019381
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name DAPB BDBG_00095
Organism Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Ajellomycetaceae Blastomyces Blastomyces gilchristii Blastomyces gilchristii (strain SLH14081) (Blastomyces dermatitidis)
Enzyme Sequence MAGEKGGSRDEEREPLTRGSIEFRDSINSFDYSSSTASLSLAVIDRINGSTQDSRLGEKDQRDDDHDQYRNEEEYDVEDADYIPSGGKTVQKTTKIVLWALLFLCVGGWSLAFVIFLFRGHDTPQTSIASEENISSGGARGNRITLDEVLGGEWAPRAHSISWFPGPNGEDGLILEKDNLSATAYLRVEDIVGRKDPKASKKSIVLMQKKMFTVGRETVYSAQAWPSPDLKTVLVLSDQQKNWRHSFTGKYWLFDVETQTGQPLDPGAPDRRIQLASWSPQSDAVVFTRDNNMFLRKLTSNEVATITTDGGVDLFYGVPDWVYEEEVFSGNSATWWASDGDYIAFLRTNESSVPDYPIQYFASRPSGENPKPGEENYPEVREVKYPKAGAPNPIVDLQFYDVGKGEVFSVDVTSEFADDDRLIIEVLWASNGKALVRETNRESDILSIAIIDVLSRTGRIVRREDVNALDGGWVEPTQSTRFIPADPDHGRLDDGYIDTVIYEGRDQLAYFTPLDNPKPIMLTKGHSEVVNAPSGVDLKRGLVYFVVAGNEPWERHIYSVNFDGTSLQPLTNVTESSYYDVSFSNGAGYALLNYRGPKVPWQKVINTPANENSFEAIIEQNDHLSRKLRLFSLESKVYQHVTVDGFSLPVMERRPPNFDPAKKYPVLFHLYGGPGSQTVSKKFSVDFQSYVASTLGYIVVTVDGRGTGHIGRKARCIIRGNLGHYEARDQIETAKKWAAKPYVDESRMAIWGWSYGGFMTLKTLEQDGGRTFQYGMAVAPVTDWRYYDSIYTERYMRTPQHNQGGYDTSAISNTTALASNIRFLLMHGTADDNVHIQNSLTLLDKLDLDDVDNYDVHVFPDSDHSIYFHNAHKMVYNRLGDWLINAFNGEWLKVHKPTPNNSLFRRAETWGGLPV
Enzyme Length 915
Uniprot Accession Number C5JC30
Absorption
Active Site ACT_SITE 754; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 831; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 864; /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 (6); 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 102,912
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda