cyclophilinlike
Cyclophilin-like refers to proteins that contain a cyclophilin-like domain (CLD), a member of the peptidyl-prolyl cis-trans isomerase (PPIase) superfamily. Like canonical cyclophilins, cyclophilin-like proteins often catalyze the cis-trans isomerization of proline-containing peptide bonds, aiding in protein folding and conformational maturation. In some members, however, key catalytic residues are altered, and the protein functions as a non-enzymatic chaperone or scaffolding factor rather than an active PPIase.
CLDs are typically about 160–180 amino acids and adopt the conserved cyclophilin structure. Cyclophilin-like proteins can
Functional roles span protein folding, stress responses, signaling, and assembly of macromolecular complexes. The best-known example
Taxonomy and nomenclature: the term “cyclophilin-like” emphasizes sequence similarity to cyclophilins rather than strict functional identity.