B2AXJ0 · B2AXJ0_PODAN
- ProteinPeptidyl-prolyl cis-trans isomerase-like 2
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids587 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
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)
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
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Sordariomycetes > Sordariomycetidae > Sordariales > Podosporaceae > Podospora > Podospora anserina
Accessions
- Primary accessionB2AXJ0
Organism-specific databases
Subcellular Location
Structure
Family & Domains
Features
Showing features for domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 43-116 | U-box | ||||
Sequence: KRLPFNFCAASLQPFKNPVCTADGTIFDIEVISAWLEKKGTNPVDGKPLSAKDLIKLNFARNADTNNSNDRNGI | ||||||
Region | 245-284 | Disordered | ||||
Sequence: EARQSASDINQSASSKTLTKSSSSTTTPRQSLIQEKQKPS | ||||||
Compositional bias | 248-284 | Polar residues | ||||
Sequence: QSASDINQSASSKTLTKSSSSTTTPRQSLIQEKQKPS | ||||||
Domain | 338-494 | PPIase cyclophilin-type | ||||
Sequence: STTLGDLTLELFPEFAPKAVWNFLRLSQKGYYNNTLFHRNIKNFMIQGGDPTGTGRGGTSIWKKTFNDELEGPLKHDKRGVVSMANKGKNTNSSQFFITYREASHLDRKHTVFGRVVDSEGTLAKMEGGEGGGGGIVRPFGRRSRSKEVVVLLDCFE | ||||||
Compositional bias | 501-536 | Basic and acidic residues | ||||
Sequence: GEKEREEEKKKEVERKGGTEDDRTTWTGKRLRGEDG | ||||||
Region | 501-587 | Disordered | ||||
Sequence: GEKEREEEKKKEVERKGGTEDDRTTWTGKRLRGEDGGGGKGGVGKYLKEVKGQRQEGEGEGETDTWEEPVKKKTRVGGGGFGNFDGW | ||||||
Compositional bias | 547-574 | Basic and acidic residues | ||||
Sequence: LKEVKGQRQEGEGEGETDTWEEPVKKKT |
Sequence similarities
Belongs to the cyclophilin-type PPIase family. PPIL2 subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length587
- Mass (Da)64,495
- Last updated2008-05-20 v1
- Checksum5F437DA853E076FF
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 248-284 | Polar residues | ||||
Sequence: QSASDINQSASSKTLTKSSSSTTTPRQSLIQEKQKPS | ||||||
Compositional bias | 501-536 | Basic and acidic residues | ||||
Sequence: GEKEREEEKKKEVERKGGTEDDRTTWTGKRLRGEDG | ||||||
Compositional bias | 547-574 | Basic and acidic residues | ||||
Sequence: LKEVKGQRQEGEGEGETDTWEEPVKKKT |
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU633900 EMBL· GenBank· DDBJ | CAP69114.1 EMBL· GenBank· DDBJ | Genomic DNA |