Detail Information for IndEnz0002018912
IED ID IndEnz0002018912
Enzyme Type ID protease018912
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name DAPB SNOG_04207
Organism Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta dothideomyceta Dothideomycetes Pleosporomycetidae Pleosporales Pleosporineae Phaeosphaeriaceae Parastagonospora Phaeosphaeria nodorum (Glume blotch fungus) (Parastagonospora nodorum) Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume blotch fungus) (Parastagonospora nodorum)
Enzyme Sequence MPRPRAAKEEETELLAQHQESPRPSSDGSEASASSISTTSLVLEHINDGGFNGARSKVSEKYTDDGNGDLGHARERFDIEDGKFHPLTPVDKKARRTLWIVGTICAVGWALALVSFLMNGNYKHSSTRPHDPDASVTKGSGKKITLDNVLGGQFYPQSQSVSWIAGPKGEDGLLLEKGVSGKDYLVVEDIRSKGNTEAAGDKFTLMKKGNFQIGEDIFIYPSNVWPSADFKKVLVMSEQQKNWRHSYTGLYWIFDVETQTGEPLDPENQSARVQYASFSPQSDAVVFTRDNNLYLRKLDSQKVVKITHDGGSELFYGVPDWVYEEEVFQDNSATWWSEDGKYVAFLRTDESMVPTYPVQYFVSRPSGKQPDAGKESYPEVREIKYPKAGAPNPIVTLQFYDIEKSEMFRVDIDNDFTDKDRLITEIVWAGKSGQVLVRETNRESDILKLILIDVSKRTGKTIREENVAKLDGGWFEVSHKTTFIPADSSLGRANDGYIDSVIHEGYDHIGYFTPLDSDKPILLTKGEWEVVEAPSRVDLKNNLVYYVSTERGSMERHPYVVALNGTDKREVMDHSGPAYYDSSFSTGGGYALMSYQGPGIPWQKIVSTPSNTEKFEKVLEENKALEKMVQKHELPILKYQTIDVDGFKLNVLERRPPHFSEKRKYPVLFYQYSGPGSQQVQRKFEVDFQSYIAANLGYIVVTVDGRGTGFLGRKLRCITRDNIGYYEAYDQIAAAKMWAAKKYVDAEKLAIWGWSYGGFTTLKTIEMDGGRTFKYGMAVAPVTDWRFYDSIYTERYMHTPQNNPTGYDNTSITDVHSLSQNVRFLIMHGVADDNVHMQNTLTLLDKLDVAGVENYDVHVFPDSDHSIYFHNAHKIVYDKLTWWLTNAFNGEWLKIQKVRPKAQADARSLGR
Enzyme Length 911
Uniprot Accession Number Q0UVK7
Absorption
Active Site ACT_SITE 755; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 832; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 865; /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 (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 103,088
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda