Detail Information for IndEnz0002005431
IED ID IndEnz0002005431
Enzyme Type ID protease005431
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name DAPB UREG_01410
Organism Uncinocarpus reesii (strain UAMH 1704)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Onygenales Onygenaceae Uncinocarpus Uncinocarpus reesii Uncinocarpus reesii (strain UAMH 1704)
Enzyme Sequence MGAEKRINDEEAQPLTGRDRSRDSIDSTSTASISLALIDQANRSTHAGRTTPPRNFGNGEKYRDNDDDNPEGGLPPPSGAQRTPKKVSIIFWLVAALCVGGWLVAFFVFMGSPKKDSDKEVVVSGAENSTVPGVVSTGGKKVDLDGVLTGFWSPRSHEISWIPGPDGEDGLLLEQDGDENAGYLRVENIRNQKSTNKKDDAVVLMKRETFKVGARRVRPSKVWPSPDLKTVLVMSDRLKNWRHSYTGNYWLFNVETQTGEPLDPGSPDGRIQLASWSPKSDSVVFTRDNNMFIRNLSSKDVKPITTDGGVNLFYGIPDWVYEEEVFSGNSATWWDNDGKFVAFLRTNESRVPEYPVQYFIPTVGRVAHAGEEHYPNTRKIKYPKAGAPNPTVNIQFFDVEKGEVFSIEMEDDLPDHDRLIIEVIWASNGKVLVRETNRESDRLSMVLVDAKDRTAKVIRSQDFSKLDGGWIEPSQSTYFIPADPGNGRPHDGYIETVPFEGFNHLAYFTPLDNPSPVFLTSGNWEVTDAPSAVDLKRGLVYFVAAKEQPTERHVYTVRLDGSDLQPIVNTKAPAYYTISLSTGAGYALLKYEGPEIPWQKVISTPANEERFEETIENNTELAGRAKDYALPSLYYQTITIDGYTLPVVERRPPNFNPDKKYPVLFHLYGGPGSQTVSKRFKVDFQSYVASNLGYIVVTVDGRGTGFIGRKARCVVRDNLGHYEAIDQIETAKAWGKRPYVDATRMAIWGWSYGGFMTLKTLERDAGQTFQYGMAVAPVTDWQFYDSIYTERYMHTPQNNPAGYANTAVSNVTALGQTVRFMVIHGTGDDNVHYQNTLTLLDKLDVDNVGNFDVHVYPDSDHGIYFHNAYKMLHERLSDWLVNAFNGEWVKIRNPVPNKSLMRRARSLLKRMSNA
Enzyme Length 914
Uniprot Accession Number C4JHY5
Absorption
Active Site ACT_SITE 751; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 828; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 861; /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 (2); Glycosylation (6); 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 102,559
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda