| Analysis | rpsblast_cdd | Start | 168 |
| End | 320 | Strand | + |
| Length | 153 | Note | Gaps:34 |
| Hit Coverage | 99.32 | Hit Length | 146 |
| Hit Pident | 28.97 | E Val | 1e-08 |
| Hit Description | cd00317 cyclophilin cyclophilin: cyclophilin-type peptidylprolyl cis- trans isomerases. This family contains eukaryotic bacterial and archeal proteins which exhibit a peptidylprolyl cis- trans isomerases activity (PPIase Rotamase) and in addition bind the immunosuppressive drug cyclosporin (CsA). Immunosuppression in vertebrates is believed to be the result of the cyclophilin A-cyclosporin protein drug complex binding to and inhibiting the protein-phosphatase calcineurin. PPIase is an enzyme which accelerates protein folding by catalyzing the cis-trans isomerization of the peptide bonds preceding proline residues. Cyclophilins are a diverse family in terms of function and have been implicated in protein folding processes which depend on catalytic /chaperone-like activities. This group contains human cyclophilin 40 a co-chaperone of the hsp90 chaperone system human cyclophilin A a chaperone in the HIV-1 infectious process and human cyclophilin H a component of the U4/U6 snRNP whose isomerization or chaperoning activities may play a role in RNA splicing. . | Hit Pcons | 15.17 |
| Name | Qrob_P0087780.2 |
| Protein Identifier |
Organism . Name |
Score | Score Type | Protein Description | Alias (in v1) | Code Enzyme | Gene Prediction Quality |
|---|---|---|---|---|---|---|---|
| Qrob_P0087780.2 | Quercus robur | 100.0 | egn | (M=52) 5.2.1.8 - Peptidylprolyl isomerase. | EC:5.2.1.8 | validated |
Powered by
