D4DCG0 · DAPB_TRIVH

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.

Catalytic activity

  • 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 (UniProtKB | ENZYME | Rhea)

Features

Showing features for active site.

1899100200300400500600700800
TypeIDPosition(s)Description
Active site765Charge relay system
Active site842Charge relay system
Active site875Charge relay system

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Cellular Componentvacuolar membrane
Molecular Functionaminopeptidase activity
Molecular Functiondipeptidyl-peptidase activity
Molecular Functionserine-type endopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Probable dipeptidyl-aminopeptidase B
  • EC number
  • Short names
    DPAP B

Gene names

    • Name
      DAPB
    • ORF names
      TRV_04813

Organism names

Accessions

  • Primary accession
    D4DCG0

Proteomes

Subcellular Location

Vacuole membrane
; Single-pass type II membrane protein
Note: Lysosome-like vacuoles.

Features

Showing features for topological domain, transmembrane.

Type
IDPosition(s)Description
Topological domain1-99Cytoplasmic
Transmembrane100-120Helical; Signal-anchor for type II membrane protein
Topological domain121-899Vacuolar

Keywords

PTM/Processing

Features

Showing features for chain, glycosylation.

Type
IDPosition(s)Description
ChainPRO_00004121651-899Probable dipeptidyl-aminopeptidase B
Glycosylation212N-linked (GlcNAc...) asparagine
Glycosylation308N-linked (GlcNAc...) asparagine
Glycosylation360N-linked (GlcNAc...) asparagine
Glycosylation819N-linked (GlcNAc...) asparagine
Glycosylation824N-linked (GlcNAc...) asparagine
Glycosylation827N-linked (GlcNAc...) asparagine
Glycosylation893N-linked (GlcNAc...) asparagine

Keywords

PTM databases

Structure

Family & Domains

Features

Showing features for region, compositional bias.

Type
IDPosition(s)Description
Region1-69Disordered
Compositional bias27-67Polar residues
Region128-149Disordered

Sequence similarities

Belongs to the peptidase S9B family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    899
  • Mass (Da)
    101,076
  • Last updated
    2010-05-18 v1
  • Checksum
    CD9AF2AD45BBFCB8
MKLDRMRVGSRINDEEAMPLTAPESRARDSIDSSSTASISLTLVEGASHATTEPSKPAHNHNGRTQGNYAEKYRDDLEEDWEENNYIPTNGKSSQRRTLIVFWLLVALCVGGWAVAFLFFVTSPGNKTSTSPHSGSNSPEGDVTKPGIPATGKKIPLDDAIGGVWSPAEHTISWIAGAKGEDGLLLQKSEGGTGPYLHVEDVRNIHGTQSNNNSIVLMKESVFFVNDERISPEKVWPSPDLKTVLAMTREKKNWRHSFTGLYWLFDVETQTAQPLDPDAPNGRIQLATWSPTSDAVAFTRDNNLYIRNLTSKSVKAITTDGGTNLFYGIPDWVYEEEVFEGNIATWWSLDGKYISYLRTNETLVPEFPIDFYLSSPPGYSPKPGEESYPYVQQIKYPKAGAPNPTVSLQFYDIEREESFSVDVKDTLKDDDRLIVEVIPGSKGKVLVRETNRESYIVKVAVIDANKREGKIVRSDNIDEIDGGWVEPSHTTTYIPADPSAGRPDDGYIDTVIHEGYIHLAYFTPLENPKPKMLTTGKWEVVAAPSGVDLKNNVVYFVATKESPIDRHVYSVKLDGSELRMLKDSDKSAYYDVSFSHGAGYMLLKYQGPQIPWQKLISSPSNADNYIEILEENKKLAKLSNEFALPSLHYSTITVDGFELPVVERRPPNFDETKKYPVLFQLYGGPGSQTVNKKFLVNFQTYVASNLGYIVVTVDGRGTGFNGRKFKCIVRRNLGHYEAHDQIQAAKAWGKKPYVDKTRMAIWGWSYGGFMTLKTLEQDAGETFQYGMAVAPVTNWRYYDSVYTERYMHMPQNNEGGYENASISNATNLSQNTRFLIMHGSADDNVHFQNTLTLLDKLDILGVHNYDMHVFPDSNHGIYFHHAYKMVHQRKYFNLSFLGH

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias27-67Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ACYE01000244
EMBL· GenBank· DDBJ
EFE40482.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

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