module: dmel_cct_chaperonin
title: Chaperonin containing TCP-1 (CCT/TRiC) in Drosophila melanogaster
label: CCT chaperonin
module_type: PROTEIN_COMPLEX
description: >-
  The chaperonin containing TCP-1 (CCT, also called TRiC) is the group II
  chaperonin of the eukaryotic cytosol. It is a double ring in which each ring
  contains one copy of each of eight paralogous subunits (CCT1-CCT8) in a fixed
  order. Substrates bind in the central cavity, and ATP hydrolysis by the
  subunits closes a built-in lid and drives folding of the enclosed
  polypeptide. Major substrates include actin and tubulin, which receive
  newly made chains partly from prefoldin.
summary: >-
  Hetero-oligomeric double-ring group II chaperonin of eight paralogous
  subunits that folds actin, tubulin and other cytosolic proteins.
concepts:
  - {id: GO:0005832, label: chaperonin-containing T-complex}
groups: [CCT, HSP60-II]
notes: >-
  CCT has no stable subcomplexes, so each of the eight subunits is modelled as
  a part. The FlyBase groups CCT and HSP60-II have identical membership. The
  ATP-dependent folding activity belongs to the assembled complex, so it is
  recorded on a complex-level annoton (GO:0140662, which all eight subunits
  carry in GOA by IEA) with all eight subunits as active units. Each subunit
  has an equatorial ATPase domain, but nucleotide use is asymmetric (in yeast
  and mammals only some subunits bind ATP at physiological concentrations),
  so no molecular function is assigned to single subunits. The cross-species CCT folding module is modules/cct_chaperonin_folding.yaml.
complex_term: {id: GO:0005832, label: chaperonin-containing T-complex}
complex_function:
  function: {id: GO:0140662, label: ATP-dependent protein folding chaperone}
  role_description: >-
    Encloses non-native actin, tubulin and other cytosolic substrates in the
    central cavity and folds them in an ATP hydrolysis-driven cycle of lid
    closure and opening.