A0A1J9S4I1 · A0A1J9S4I1_9PEZI

  • Protein
    peptidylprolyl isomerase
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    2/5

Function

function

PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.

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 Componentcytoplasm
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Biological Processprotein folding
Biological Processprotein peptidyl-prolyl isomerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    peptidylprolyl isomerase
  • EC number

Gene names

    • ORF names
      BKCO1_20000116

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • CBS 112549
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Dothideomycetes > Dothideomycetes incertae sedis > Botryosphaeriales > Botryosphaeriaceae > Diplodia

Accessions

  • Primary accession
    A0A1J9S4I1

Proteomes

Subcellular Location

Keywords

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain, region, repeat, coiled coil.

Type
IDPosition(s)Description
Domain10-176PPIase cyclophilin-type
Region186-206Disordered
Repeat308-341TPR
Coiled coil314-368

Sequence similarities

Belongs to the cyclophilin-type PPIase family. PPIase D subfamily.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    371
  • Mass (Da)
    40,903
  • Last updated
    2017-02-15 v1
  • Checksum
    45D72EDEC598757A
MAEQKRSRVFFDIQVGSQPAGRVAFELYNDIVPKTAENFRALCTGEKGEGKSGKPLHYKGSGFHRVIKQFMIQGGDFTAGNGTGGESIYGEKFEDENFELKHEKPFLLSMANAGPGTNGSQFFVTTVPTPHLDGKHVVFGEVINGKSIVRQLENLPTAAQDRPSPENFPIIADCGELTGEDYEKCTERAPDSTGDPYEDFPEDQSEELTAPQIAKIAGELKDMGNKAFKGGDLRLGLAKYQKGLRYLNENPEVEEKDPPETKQQLSSLRFQLHNNSALLQNKLKEYEGAAKSATYALEVPGTADADKAKAYFRRAQAREARKSEEEAIQDYEAAQKLAPNDSAVLSGLANAKKRLAEFKKKEKAAYAKFFS

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MNUE01000020
EMBL· GenBank· DDBJ
OJD34868.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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