| Primary Identifier | IPR016304 | Type | Family |
| Short Name | PPIE |
| description | Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity (), accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [, ]. They also have protein chaperone-like functions []and are the major high-affinity binding proteins for the immunosuppressive drug cyclosporin A (CSA) in vertebrates [].Cyclophilins are found in all prokaryotes and eukaryotes, and have been structurally conserved throughout evolution, implying their importance in cellular function []. They share a common 109 amino acid cyclophilin-like domain (CLD) and additional domains unique to each member of the family. The CLD domain contains the PPIase activity, while the unique domains are important for selection of protein substrates and subcellular compartmentalisation [].This entry represents the peptidyl-prolyl cis-trans isomerase E family of enzymes, which are a type of cyclophilin. In addition to their PPIase activity and role in protein folding, PPIase E family members also possess RNA-binding activity and may be involved in pre-mRNA splicing [, ]. |
