Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Belongs to the TCP-1 chaperonin family. Note: This description may include information from UniProtKB.
Molecular Function: ATP binding; RNA binding; unfolded protein binding
Biological Process: binding of sperm to zona pellucida; chaperone cofactor-dependent protein folding; positive regulation of telomerase activity; positive regulation of telomere maintenance via telomerase; protein folding; protein stabilization