P0CP90 · PPIL2_CRYNJ
- ProteinPeptidyl-prolyl cis-trans isomerase-like 2
- GeneCYP8
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids573 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
May catalyze the cis-trans isomerization of proline imidic peptide bonds in oligopeptides thereby assisting the folding of proteins. May also function as a chaperone, playing a role in intracellular transport of proteins. May also have a protein ubiquitin ligase activity acting as an E3 ubiquitin protein ligase or as a ubiquitin-ubiquitin ligase promoting elongation of ubiquitin chains on proteins.
Catalytic activity
- [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Pathway
Protein modification; protein ubiquitination.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | catalytic step 2 spliceosome | |
Molecular Function | peptidyl-prolyl cis-trans isomerase activity | |
Molecular Function | ubiquitin protein ligase activity | |
Biological Process | protein folding | |
Biological Process | protein peptidyl-prolyl isomerization | |
Biological Process | protein polyubiquitination |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePeptidyl-prolyl cis-trans isomerase-like 2
- EC number
- Short namesPPIase
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Basidiomycota > Agaricomycotina > Tremellomycetes > Tremellales > Cryptococcaceae > Cryptococcus > Cryptococcus neoformans species complex
Accessions
- Primary accessionP0CP90
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000232984 | 1-573 | Peptidyl-prolyl cis-trans isomerase-like 2 | ||
Proteomic databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 37-119 | U-box | |||
Region | 223-247 | Disordered | |||
Domain | 312-469 | PPIase cyclophilin-type | |||
Region | 489-515 | Disordered | |||
Compositional bias | 490-515 | Basic and acidic residues | |||
Sequence similarities
Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length573
- Mass (Da)63,562
- Last updated2011-06-28 v1
- Checksum2921176BE24684D0
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Compositional bias | 490-515 | Basic and acidic residues | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE017350 EMBL· GenBank· DDBJ | AAW45760.1 EMBL· GenBank· DDBJ | Genomic DNA |