A0A2R6QRF3 · A0A2R6QRF3_ACTCC

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 functionnucleotide bindingmolecular_functionnucleic acid bindingdna bindingchromatin bindingdna-binding transcription factor activityrna bindingcytoskeletal motor activitycatalytic activitynuclease activitysignaling receptor bindingstructural molecule activitytransporter activitybindingprotein bindingtranslation factor activity, rna bindinglipid bindingkinase activitytransferase activityhydrolase activityoxygen bindingenzyme regulator activitycarbohydrate bindingsignaling receptor activitytranslation regulator activitytranscription regulator activityother molecular functionall biological processcarbohydrate metabolic processgeneration of precursor metabolites and energynucleobase-containing compound metabolic processdna metabolic processtranslationlipid metabolic processtransportresponse to stresscell cyclecell communicationsignal transductioncell-cell signalingmulticellular organism developmentcircadian rhythmbiological_processmetabolic processcatabolic processbiosynthetic processresponse to light stimulusresponse to external stimulustropismresponse to biotic stimulusresponse to abiotic stimulusresponse to endogenous stimulusembryo developmentpost-embryonic developmentfruit ripeningabscissionpollinationflower developmentcellular processprogrammed cell deathphotosynthesiscellular component organizationcell growthprotein metabolic processcellular homeostasissecondary metabolic processreproductive processcell differentiationprotein modification processgrowthepigenetic regulation of gene expressionresponse to chemicalanatomical structure developmentregulation of molecular functionother biological processall cellular componentcellular_componentextracellular regioncell wallintracellular anatomical structurenucleusnuclear envelopenucleoplasmnucleoluscytoplasmmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuscytosolribosomecytoskeletonplasma membranechloroplastplastidthylakoidmembraneexternal encapsulating structureother cellular component
Cell color indicative of number of GO terms
AspectTerm
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidyl-prolyl cis-trans isomerase
  • EC number
  • Short names
    PPIase

Gene names

    • ORF names
      CEY00_Acc14308

Organism names

Accessions

  • Primary accession
    A0A2R6QRF3

Proteomes

Genome annotation databases

Interaction

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain1-108PPIase cyclophilin-type

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    112
  • Mass (Da)
    12,389
  • Last updated
    2018-06-20 v1
  • Checksum
    060CB1AAA098455B
MKDSFIKGGDWYTKNGYSSRSVYGQPFGDENFSLSHVGLGVVSMANSGQHSNGSQFFICMTEIPELDGKHVVFGQVLEGMDIVKLIESQEMDKNQYLQTMVVISNCGELPLD

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
NKQK01000013
EMBL· GenBank· DDBJ
PSS13699.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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