GroEL-like equatorial domain (IPR027413)

Short name: GROEL-like_equatorial

Domain relationships



Chaperonins are large cylindrical structures that transiently enclose a partially folded polypeptide and allow it to continue folding in a sequestered environment. Chaperonins are grouped into two families: group I chaperonins, found in eubacteria (e.g. GroEL in Escherichia coli) and eukaryotic organelles of eubacterial descent (e.g. Cpn60 in mitochondria and chloroplasts), and group II chaperonins, found in archaea and the eukaryotic cytosol (CCT or TCP-1 complex) [PMID: 11725484, PMID: 7601114]. Both groups share a common monomer architecture of three domains: an equatorial domain that carries ATPase activity, an intermediate domain, and an apical domain, involved in substrate binding [PMID: 8861908, PMID: 12083524, PMID: 19717599].

This entry represents the equatorial domain.

Contributing signatures

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