Detail Information for IndEnz0002003174
IED ID IndEnz0002003174
Enzyme Type ID protease003174
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name DAPB HCBG_06672
Organism Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Ajellomycetaceae Histoplasma Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum) Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum)
Enzyme Sequence MATEKGHGRDDEERVPLTRGSTEFRNSIDSFDYSSSTASLSLAVIDRINNSTQDAALGEKGPRDDDDDRYWDDDVEYDVEDADYIPSGGKPMHKSVKIALWTLLFLSLGGWSLAFVLFIFRSHDTYETPISSEDNISSGGLRGDRITLDDVLGEEWMPRHHFISWFPGPNGEDGLLLEKDGPGSTGYLRVEDIVSRKDTKSSKGSIVLMRKNTFTVGGETVICSQVWPSPDLKTVLVLSEKKQNWRHSFTGKYWLFDVDTQTGQPLDPAAQDQRIQLASWSPQSDAVVFTRDNNMFLRKLSSKEVTTITSDGGVDLFYGVPDWVYEEEVFSGNSATWWAHDGNYIAFLRTNESAVPEYPLQYFVSRPSGEDPNLGEENYPEVREIKYPKAGAPNPIVDLQFYDVRKGEIFSVDVADRFPDDNRLIIEVLWASNGKVLVRETNRESDILIIAAINVLSRTGKIVRKEDINALDGGWVEPTQSTRFIPADPSNGRPEDGYIDTVIHEGRDQLAYFTPLDNPEPLILTKGPSEVVNSPSGVDLKRGLVYFVVAGNEPWERHVYSVKFDGTALQPVTNVSESSYYDVSFSDGAGYALLNFQGPKVPWQKVISTPANENPFEEIIEQNNHLSRKLRLFSLESKVFQYINIDGFSLPVLERRPPNFDPTKKYPVLFYLYGGPGSQTVDKKFRVDFQSYVASTLGYIVVTVDGRGTGYIGRKSLSIVRGKLGHYEARDQIEVAKKWAAKPYVDESRMAIWGWSYGGFMTLKTIEEDGGRTFQYGMAVAPVTDWRYYDSIYAERYMHTPQHNPQGYDSSAISNTTALANNVRFLVMHGTADDNVHIQNTLTLLDKLDLANVDNYDVHVFPDSDHNINFHNAHKIVYTRLADWLVNAFNGQWLKTNNPTPNDSLFRRAATWAGLSYNFKHLH
Enzyme Length 923
Uniprot Accession Number C0NUQ8
Absorption
Active Site ACT_SITE 756; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 833; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 866; /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 (5); 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 104,146
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda