A0A2I0NI76 · A0A2I0NI76_9EURY

Function

function

Molecular chaperone capable of stabilizing a range of proteins. Seems to fulfill an ATP-independent, HSP70-like function in archaeal de novo protein folding.

Caution

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

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 Componentcytoplasm
Cellular Componentprefoldin complex
Molecular Functionprotein-folding chaperone binding
Molecular Functionunfolded protein binding
Biological Processchaperone-mediated protein complex assembly
Biological Processprotein folding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Prefoldin subunit beta
  • Alternative names
    • GimC subunit beta

Gene names

    • Name
      pfdB
    • ORF names
      CVV36_05750

Organism names

Accessions

  • Primary accession
    A0A2I0NI76

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Heterohexamer of two alpha and four beta subunits.

Family & Domains

Features

Showing features for coiled coil.

TypeIDPosition(s)Description
Coiled coil9-107

Sequence similarities

Belongs to the prefoldin subunit beta family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    119
  • Mass (Da)
    13,633
  • Last updated
    2018-02-28 v1
  • Checksum
    114CD5614BDCCA20
MSSELPPQIQNQLAQLQQTQQQGQALAAQKNQVEITLKETELAFEELEKLDADAVVYRAVGDLMIKTDRDKTKETLNERKESLDLRLQTLARQEERIQKRFTQLQEQLKQAVGAPETAQ

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PGYG01000032
EMBL· GenBank· DDBJ
PKL53687.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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