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.
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. FlyBase groups realized by this module: CCT (FBgg0000505), HSP60-II (FBgg0002199). Participants were generated from the FlyBase gene-group membership and mapped to UniProtKB by projects/FLYBASE_GENE_GROUPS/generate_modules.py from module_specs/dmel_cct_chaperonin.yaml. None of the member genes has a gene review in this repository yet.
All recommended fields populated.
✗ none found
No MODULE:dmel_cct_chaperonin deep-research report alongside the module YAML.
✓ every leaf node grounds to a representative protein.
✓ every declared conforms_to bundle matches its template motif.
0 gene-function check(s) reflected in core functions · 0 conflict(s) · 0 evidence or coverage gap(s) (1 comparison(s))
Retained noncore functions are reported separately; they do not require promotion to core functions. Support from representative genes does not establish conservation across the whole family. Missing reviews or identifiers leave a claim unverified.
| Annoton | Participant | Function | Assessment |
|---|---|---|---|
| dmel_cct_chaperonin_complex_activity | PROTEIN_COMPLEX Gene |
ATP-dependent protein folding chaperone GO:0140662 |
Participant Unchecked
No direct UniProt participant to compare. Abstract selectors and complex-wide activities cannot be inferred from donor or subunit gene reviews. |
0 complete review(s) · 0 with deep research · 8 missing review · 0 reviewed but lacking deep research
| Gene | Review | Complete | Deep research |
|---|---|---|---|
| CCT8 A1Z7K1 | ✗ | — | — |
| CCT5 A1Z8U4 | ✗ | — | — |
| CCT1 P12613 | ✗ | — | — |
| CCT3 P48605 | ✗ | — | — |
| CCT7 Q9VHL2 | ✗ | — | — |
| CCT4 Q9VK69 | ✗ | — | — |
| CCT6 Q9VXQ5 | ✗ | — | — |
| CCT2 Q9W392 | ✗ | — | — |
Hetero-oligomeric double-ring group II chaperonin of eight paralogous subunits that folds actin, tubulin and other cytosolic proteins.
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.