Q8RWY7 · CYP95_ARATH
- ProteinPeptidyl-prolyl cis-trans isomerase CYP95
- GeneCYP95
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids837 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | nucleus | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Biological Process | protein peptidyl-prolyl isomerization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase CYP95
- EC number
- Short namesAtCYP95; PPIase CYP95
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > malvids > Brassicales > Brassicaceae > Camelineae > Arabidopsis
Accessions
- Primary accessionQ8RWY7
- Secondary accessions
Proteomes
Organism-specific databases
Genome annotation databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000429769 | 1-837 | Peptidyl-prolyl cis-trans isomerase CYP95 | ||
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in leaves, flowers, roots and stems.
Gene expression databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 10-174 | PPIase cyclophilin-type | |||
Region | 176-837 | Disordered | |||
Compositional bias | 184-204 | Basic residues | |||
Compositional bias | 242-280 | Basic residues | |||
Compositional bias | 330-345 | Basic and acidic residues | |||
Compositional bias | 365-379 | Basic and acidic residues | |||
Compositional bias | 381-430 | Polar residues | |||
Compositional bias | 431-445 | Basic and acidic residues | |||
Compositional bias | 454-468 | Basic and acidic residues | |||
Compositional bias | 528-585 | Polar residues | |||
Compositional bias | 586-600 | Basic residues | |||
Compositional bias | 601-629 | Polar residues | |||
Compositional bias | 632-651 | Basic residues | |||
Compositional bias | 704-718 | Basic and acidic residues | |||
Compositional bias | 719-740 | Basic residues | |||
Compositional bias | 772-828 | Polar residues | |||
Sequence similarities
Belongs to the cyclophilin-type PPIase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name1
- Length837
- Mass (Da)94,630
- Last updated2014-07-09 v2
- Checksum1E2ADDB203DE6B4C
Q8RWY7-2
- Name2
- Differences from canonical
- 1-110: Missing
Q8RWY7-3
- Name3
- Differences from canonical
- 161-177: Missing
Sequence caution
Features
Showing features for alternative sequence, sequence conflict, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Alternative sequence | VSP_055204 | 1-110 | in isoform 2 | ||
Sequence conflict | 54 | in Ref. 1; AAM13845 and 4; AAS75312 | |||
Alternative sequence | VSP_055205 | 161-177 | in isoform 3 | ||
Compositional bias | 184-204 | Basic residues | |||
Compositional bias | 242-280 | Basic residues | |||
Compositional bias | 330-345 | Basic and acidic residues | |||
Compositional bias | 365-379 | Basic and acidic residues | |||
Compositional bias | 381-430 | Polar residues | |||
Compositional bias | 431-445 | Basic and acidic residues | |||
Compositional bias | 454-468 | Basic and acidic residues | |||
Compositional bias | 528-585 | Polar residues | |||
Compositional bias | 586-600 | Basic residues | |||
Compositional bias | 601-629 | Polar residues | |||
Compositional bias | 632-651 | Basic residues | |||
Compositional bias | 704-718 | Basic and acidic residues | |||
Compositional bias | 719-740 | Basic residues | |||
Compositional bias | 772-828 | Polar residues | |||
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |