A0A2U7NFF2 · A0A2U7NFF2_9POAL
- ProteinPeptidyl-prolyl cis-trans isomerase
- GeneCYP
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids215 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score2/5
Function
function
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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 | intracellular membrane-bounded organelle | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Biological Process | protein folding | |
Biological Process | protein peptidyl-prolyl isomerization |
Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase
- EC number
- Short namesPPIase
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > Liliopsida > Poales > Poaceae > PACMAD clade > Panicoideae > Andropogonodae > Paspaleae > Paspalinae > Paspalum
Accessions
- Primary accessionA0A2U7NFF2
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for signal, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Signal | 1-37 | |||||
Sequence: MAPSGWRRSAAARAAWRPATVCLWLALAAAALTLAQA | ||||||
Chain | PRO_5016063409 | 38-215 | Peptidyl-prolyl cis-trans isomerase | |||
Sequence: KKDLTEVTHKVYFDIEIDGKPAGRIVMGLFGKTVPKTAENFRALCTGEKGVGKSGKPLHYKGSTFHRIIPSFMLQGGDFTLGDGRGGESIYGLKFADENFKIKHTGPGLLSMANAGRDTNGSQFFITTVTTSWLDGKHVVFGKVLSGMDVVYKVEAEGRQSGQPKSKVVIADSGELPM |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 49-212 | PPIase cyclophilin-type | ||||
Sequence: YFDIEIDGKPAGRIVMGLFGKTVPKTAENFRALCTGEKGVGKSGKPLHYKGSTFHRIIPSFMLQGGDFTLGDGRGGESIYGLKFADENFKIKHTGPGLLSMANAGRDTNGSQFFITTVTTSWLDGKHVVFGKVLSGMDVVYKVEAEGRQSGQPKSKVVIADSGE |
Sequence similarities
Belongs to the cyclophilin-type PPIase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length215
- Mass (Da)23,049
- Last updated2018-09-12 v1
- Checksum149B1515FF56F51E