Detail Information for IndEnz0002006025
IED ID IndEnz0002006025
Enzyme Type ID protease006025
Protein Name Probable dipeptidyl-aminopeptidase B
DPAP B
EC 3.4.14.5
Gene Name dapB PMAA_013400
Organism Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Pezizomycotina leotiomyceta Eurotiomycetes Eurotiomycetidae Eurotiales (green and blue molds) Trichocomaceae Talaromyces Talaromyces sect. Talaromyces Talaromyces marneffei (Penicillium marneffei) Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333) (Penicillium marneffei)
Enzyme Sequence MARKDKDNGPEFVPLTNRSHRSSASFSSTDSLSSDGSLFGDDDVNALHSQKITRTQLPEENPYRDDDVELERGDNIFSRPTENSKRNRGSRLIWVVGLLCLGGWILAFVLFWGRRNSELSSSIAAVHGADSATGSTSYGKPLTLDGVLNGSWGRRRHSISWVAGPNGQDGLLLERDEDEKKAYLRVESIHSRQNQTDAREGWVLMESGAFAVNGKSLQPSATWPSPDFKSVLVAANAVSNWRHSFTATYWLFDVDTQTAQPLDPDEPKGRIQLASWSPQSDAVVFTRDNNLYLRKLDSDKVSQLTKDGGKDVFNGVPDWVYEEEVFGTDSTTWWSKDGKYVAFLRTNESMVPEFPIEYYMSRPSGKKPPAGLDKYPDVRKIKYPKAGSPNPVVTLQFYDIENAEVFSVNVSGGFADDDRLITEVVWASSGKVLVKEFNRESDVIRTVLIDVPSRTGELVRVDNFAQDDGGWAEVTQSTTFIPADPANGRPDDGYIDIIVHDGYDHWGYFTPVNNSVPVLLTSGPWEVVDTEPAVDLANNIVYFVASKESPTQRHVYSVKLDGSDLQPLTDVTKAGYYDASFSIGGGYVLLSYDGPRVPWQKVINTPSNQNPFEEIIEQNEQLSKMIEKYALPAEIYQNITIDNVTLQVVERRPPHFNPVKKYPVLFWLYGGPGSQSVDRRFSVDFQSYVASTLGYIVVTVDGRGTGHIGRAARTIVRGNLGYWEARDQIETAKAWAKKPYVDKDHIAIWGWSYGGFMTLKTLEQDAGQTFQYGMAVSPVTDWRFYDSIYTERYMHTPEHNPTGYEHSAISNMTALQQNVRFLVMHGTADDNVHFQNTLSLIDKLDMAGVENYDVHVYPDSDHSIYFHNAHKMVYDRLSSWLVTAFTDGWQQGNSVLPVT
Enzyme Length 899
Uniprot Accession Number B6QVW4
Absorption
Active Site ACT_SITE 752; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 829; /note=Charge relay system; /evidence=ECO:0000250; ACT_SITE 862; /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 (8); 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 100,866
Kinetics
Metal Binding
Rhea ID
Cross Reference Brenda