A0A072P3V9 · A0A072P3V9_9EURO

Function

function

PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at prolines on the histone H3 N-terminal tail. Proline isomerization influences H3 methylation thereby regulating gene expression.

Caution

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

Catalytic activity

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 Componentchromatin
Cellular Componentnucleolus
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    peptidylprolyl isomerase
  • EC number

Gene names

    • ORF names
      A1O9_09558

Organism names

  • Taxonomic identifier
  • Strain
    • CBS 119918
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Chaetothyriomycetidae > Chaetothyriales > Herpotrichiellaceae > Exophiala

Accessions

  • Primary accession
    A0A072P3V9

Proteomes

Organism-specific databases

Subcellular Location

Interaction

Subunit

Binds to histones H3 and H4.

Protein-protein interaction databases

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region42-178Disordered
Compositional bias45-70Basic and acidic residues
Compositional bias71-98Acidic residues
Compositional bias99-116Basic and acidic residues
Compositional bias117-141Acidic residues
Region222-437Disordered
Compositional bias233-279Acidic residues
Compositional bias280-314Basic and acidic residues
Compositional bias378-436Polar residues
Domain456-542PPIase FKBP-type

Sequence similarities

Belongs to the FKBP-type PPIase family. FKBP3/4 subfamily.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    542
  • Mass (Da)
    58,610
  • Last updated
    2014-10-01 v1
  • Checksum
    0FB0CB3C65B64F35
MSGIQPVAFYAMKVPPGDIMVPAVPEFAAMFRLTMAAIDPSAEPELENGDDKQPPRSTLKVVRIPDHLFDSDDDDSDDDDYADGLEDDDEDSEDDEEVNGGPSEKKSKKQALLEALAKDEEEDEDMADDDEDDDDDDEADAKAIAMLEKLIKNSKGKGKAIEGEDLSDDDEDSDDESIEMDEVVVCTLDPTQHYQQPLDFVVGEGEKVFFKVSGTHTVHLTGNYVIPQEDGNSSLYDEDDYLNEDEEDEEYDLSPYDEEEEEDELDDGLDEESDELDDLADPRITEVGSDEEAIPKLVKAAKGKGKNKRPAEESADEDGEEDNLDAIMAKSLKKPETTEAATNGDTKKLSKAEKKRQKKLKKNDGEAAPAGSEPTATETKKDAPSSNGSEKKVQFAKNLEQGPTPSATPASSTAKSDKSSSSTTTTTTSTSVGVKEVQGVTVDDRKVGSGPAAKKGSRVEMRYIGKLDSGKVFDSNKSGKPFGFKLGAGEVIKGWDIGVAGIQVGGERRLVIPAHLAYGSKALPGIPKNSKLTFDIKCLGIK

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias45-70Basic and acidic residues
Compositional bias71-98Acidic residues
Compositional bias99-116Basic and acidic residues
Compositional bias117-141Acidic residues
Compositional bias233-279Acidic residues
Compositional bias280-314Basic and acidic residues
Compositional bias378-436Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AMGV01000010
EMBL· GenBank· DDBJ
KEF54392.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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