Q8RWY7 · CYP95_ARATH

Function

function

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

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
Cellular Componentnucleus
Molecular Functionpeptidyl-prolyl cis-trans isomerase activity
Biological Processprotein peptidyl-prolyl isomerization

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Peptidyl-prolyl cis-trans isomerase CYP95
  • EC number
  • Short names
    AtCYP95; PPIase CYP95
  • Alternative names
    • Cyclophilin-like protein CypRS92

Gene names

    • Name
      CYP95
    • Synonyms
      CYPRS92
    • ORF names
      F8B4.120
    • Ordered locus names
      At4g32420

Organism names

  • Taxonomic identifier
  • Strain
    • cv. Columbia
  • Taxonomic lineage
    Eukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis

Accessions

  • Primary accession
    Q8RWY7
  • Secondary accessions
    • B3H620
    • F4JUB0
    • F4JUB1
    • Q9SUV0

Proteomes

Organism-specific databases

Genome annotation databases

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004297691-837Peptidyl-prolyl cis-trans isomerase CYP95

Proteomic databases

PTM databases

Expression

Tissue specificity

Expressed in leaves, flowers, roots and stems.

Gene expression databases

Interaction

Subunit

Interacts with SCL28, SCL30, SR34, RNU1 and SNRNP35.

Protein-protein interaction databases

Structure

Family & Domains

Features

Showing features for domain, region, compositional bias.

Type
IDPosition(s)Description
Domain10-174PPIase cyclophilin-type
Region176-837Disordered
Compositional bias184-204Basic residues
Compositional bias242-280Basic residues
Compositional bias330-345Basic and acidic residues
Compositional bias365-379Basic and acidic residues
Compositional bias381-430Polar residues
Compositional bias431-445Basic and acidic residues
Compositional bias454-468Basic and acidic residues
Compositional bias528-585Polar residues
Compositional bias586-600Basic residues
Compositional bias601-629Polar residues
Compositional bias632-651Basic residues
Compositional bias704-718Basic and acidic residues
Compositional bias719-740Basic residues
Compositional bias772-828Polar residues

Sequence similarities

Belongs to the cyclophilin-type PPIase family.

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q8RWY7-1

This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

  • Length
    837
  • Mass (Da)
    94,630
  • Last updated
    2014-07-09 v2
  • Checksum
    1E2ADDB203DE6B4C
MAKKKNPQVFMDVSIDGDPAETMVFELFPEVAPKTSENFRALCTGEKGIGPRSGKPLHYKGSFFHRIMKGSSAQAGDFVNRNGTAGESIYAGKFPDESPKLRHEETGLLSMSIADRDKFGSHFHITFRPNQQLDRNNVVFGKLIQGKEILKKIERVGDEEGKPTVSVKIIRCGEYSGDKKKSDGKKNGKHKKSLRVRRKKRRRHSSSESESSSDSETDSSESDSESDSDLSSPSFLSSSSHERQKKRKRSSKKDKHRRSKQRDKRHEKKRSMRDKRPKRKSRRSPDSLEDSNSGSEASLSDVNVEIGAKKRKHRVSRRTGNSAPAVEKEAESLHQGKRKGPDLLENRGLRSNGISDAASEQISDRQPDIVDDHPSKSRSRSLSPKRTVSKSTSVSPRRSQSKSPSSSPRWNGGRSPAKGSRQVKNLTNSRRESPGSEEKGRHVRRSPTKSVSRSPVRVKKERDISRSPSKSLSRSPLRSPKRVISRSPVRGRIARSPSRSPVRSASRGSLGRGPLRRSSRRSPSRSPVRSSRRSLSRSPIQLSRRSLSRSPTRLSRRSLSRSPIRSPRKSVSRSPVRSSRKSVSRSPVRSSRRRISRSPVRSSRKSVSRSPIRLSRRSISRSPIRLSRRSISRSPVRGRRRISRSPVPARRRSVRPRSPPPDRRRSLSRSASPNGRIRRGRGFSQRFSYARRYRTSPSPDRSPYRFSDRSDRDRFRSRRRFSPSRFRSPLRGRTPPRYRRRSRSVSPGLCYRNRRYSRSPIRSRSPPYRKRRSPSASHSLSPSRSRSRSKSYSKSPIGTGKARSVSRSPSKARSPSKSDSTSSDNSPGGKKGLVAYD

Q8RWY7-2

  • Name
    2
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Q8RWY7-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Sequence caution

The sequence CAA22569.1 differs from that shown. Reason: Erroneous gene model prediction
The sequence CAB79959.1 differs from that shown. Reason: Erroneous gene model prediction

Features

Showing features for alternative sequence, sequence conflict, compositional bias.

Type
IDPosition(s)Description
Alternative sequenceVSP_0552041-110in isoform 2
Sequence conflict54in Ref. 1; AAM13845 and 4; AAS75312
Alternative sequenceVSP_055205161-177in isoform 3
Compositional bias184-204Basic residues
Compositional bias242-280Basic residues
Compositional bias330-345Basic and acidic residues
Compositional bias365-379Basic and acidic residues
Compositional bias381-430Polar residues
Compositional bias431-445Basic and acidic residues
Compositional bias454-468Basic and acidic residues
Compositional bias528-585Polar residues
Compositional bias586-600Basic residues
Compositional bias601-629Polar residues
Compositional bias632-651Basic residues
Compositional bias704-718Basic and acidic residues
Compositional bias719-740Basic residues
Compositional bias772-828Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AY091023
EMBL· GenBank· DDBJ
AAM13845.1
EMBL· GenBank· DDBJ
mRNA
AL034567
EMBL· GenBank· DDBJ
CAA22569.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
AL161581
EMBL· GenBank· DDBJ
CAB79959.1
EMBL· GenBank· DDBJ
Genomic DNA Sequence problems.
CP002687
EMBL· GenBank· DDBJ
AEE86054.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE86055.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE86056.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
AEE86057.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
ANM67682.1
EMBL· GenBank· DDBJ
Genomic DNA
CP002687
EMBL· GenBank· DDBJ
ANM67683.1
EMBL· GenBank· DDBJ
Genomic DNA
AY568529
EMBL· GenBank· DDBJ
AAS75312.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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