Detail Information for IndEnz0002018907
IED ID IndEnz0002018907
Enzyme Type ID protease018907
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name dapB NCU02515
Organism Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta sordariomyceta Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora Neurospora crassa Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)
Enzyme Sequence MPSTYSDDNTLRSGLDRFRDHSPSQHRRSMSQETDSTVSTTSIVFDRIQERLDTKEFPARGTDGDDNDSLKDELNNDDLETGPFLGNASPSSRSNQRSSADGQRMDRSLRRWLFIVSGALVATWVIGLIFFVSSKAYKPSSSFAHDPQATVTHGSGKKVTLDQVLNNEWRAKSHSISWIAGVNGEDGLLLEKEGANKDYLVVEDVRAQNPSSVEASKSKTLIKDKLFEFANKTYWPTVTVPSRDLKKVLLATDVQNNWRHSYYAVYWIFDVETQQAEPLVPYDADARLQLASWSPTSDAIVYTRDNNMFLRKLDSDKIVQITRDGSADVFNGVPDWVYEEEVLASGVATWWSEDGNYVAFLRTNETGVPEYPIQYFVSRPSGEEPKPGEENYPEVRQIKYPKAGAHNPIVDLKFYDVKRGDVFSVDISGRFADDDRLITEVIWAGKQVLIKETNRVSDVMRVVLVDVGSRTGKAVRTVDVNDIDGGWFEISHKTKFIPADPANGRPDDGYVDTIIHNNGDHLAYFTPLDNPNPIMLTSGDYEVVDAPSAVDLQRNLVYFVSTKESSIQRHVYQVKLTGEDMTPVTDTSKEGYYAISFSTGAGYALVSYQGPNIPWQKVISTPSNPDKYEHVVEENKDLAEAAKKHELPINIYGTINVDGVELNYIERRPPHFDKNKKYPVLFQQYSGPVSQTVKKTFAVDFQSFVAAGLGYICVTVDGRGTGFIGRKNRVIIRGNLGTWESHDQIAAAKHWAQKDYIDEDRLAIWGWSYGGYMTLKTLEQDAGQTFKYGMAVAPVTDWRFYDSIYTERYMRTPQTNPEGYESAAVTNVTALSQNVRFLLMHGVADDNVHMQNSLTLLDALDQRSVENYDVQVFPDSDHGIYFHNANRIVFDKLTNWLVNAFNGEWLKIANAQPNGMKRRALPTA
Enzyme Length 924
Uniprot Accession Number Q7SHU8
Absorption
Active Site ACT_SITE 768; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 845; /note=Charge relay system; /evidence=ECO:0000255|PROSITE-ProRule:PRU10084; ACT_SITE 878; /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 (4); 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 104,094
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda