E7RI51 · E7RI51_9BACL

Function

function

Has oligopeptidase activity and degrades a variety of small bioactive peptides.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion.

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
Molecular Functionmetal ion binding
Molecular Functionmetalloendopeptidase activity
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Oligopeptidase F
  • EC number

Gene names

    • ORF names
      GPDM_10795

Organism names

Accessions

  • Primary accession
    E7RI51

Proteomes

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain115-181Oligopeptidase F N-terminal
Domain206-583Peptidase M3A/M3B catalytic

Sequence similarities

Belongs to the peptidase M3B family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    603
  • Mass (Da)
    68,579
  • Last updated
    2011-04-05 v1
  • Checksum
    0D83DA8392BC8B4F
MVKSLPARSAVPVEETWDLSSLISSSPDFNQQLEDLAQQAEAINKKFQGTIVDPESITLVLTAYMRFMEKMVLLSTHANLTASTDQTNDEAQLQASKFGATAAKIGSQLSFITSELLALPTETLEQAMEQSTEFSVFLKKLLRKKPYQLHPEAEKSLAAYSSTFSAPYGLYNTTKMGDIDFEDFEVNGQKYPLSYGSFEGDWEAETNTELRRAAFDAFSKKLKEYQQTTAKTYDMQLQNEKTTADLRGYDSIFDYLLFNQEVDRTLYDRQIDLITTELAPHMRKYAKLLQKVHGLEQMTFADLKISLDPSYEPEITVAESKQYIDDALSIMGPDYLEMIDRSYSERWIDFAQNKGKSTGAFCSSPYGDHPYILISWTGRMNEVFVLAHELGHAGHFYHAHQEQNIFNGRPSLYFIEAPSTMNEMLVANHLLKNSEDPKFKRWVISSIVARTYYHNFVTHLLEAAYQRKVYERIDAGQSVNAGILNSIKRKVLEDFWGNTVEINEGAELTWMRQPHYYMGLYPYTYSAGLTISTQVSKRILKEGQPAVNEWLEVLKAGGTKDPVELAQMAGVDITTEQPLRDTIAYIGELIDELVKLTEEIEAE

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AEPB01000035
EMBL· GenBank· DDBJ
EGA89290.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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