Conserved Site

Cyclophilin-type peptidyl-prolyl cis-trans isomerase, conserved site (IPR020892)

Short name: Cyclophilin-type_PPIase_CS


Cyclophilins exhibit peptidyl-prolyl cis-trans isomerase (PPIase) activity (EC:, accelerating protein folding by catalysing the cis-trans isomerisation of proline imidic peptide bonds in oligopeptides [PMID: 14731520, PMID: 2186809]. They also have protein chaperone-like functions [PMID: 15998457] and are the major high-affinity binding proteins for the immunosuppressive drug cyclosporin A (CSA) in vertebrates [PMID: 14731520].

Cyclophilins are found in all prokaryotes and eukaryotes, and have been structurally conserved throughout evolution, implying their importance in cellular function [PMID: 21309470]. 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 [PMID: 21295323].

This entry represents a conserved site in the central part of these enzymes.

GO terms

Biological Process

GO:0006457 protein folding

Molecular Function

GO:0003755 peptidyl-prolyl cis-trans isomerase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns