Lineage for Family a.129.1.2: Group II chaperonin (CCT, TRIC), ATPase domain
- Root: SCOPe 2.06
Class a: All alpha proteins [46456] (289 folds) 
Fold a.129: GroEL equatorial domain-like [48591] (1 superfamily)
multihelical; 8 helices arranged in 2 parallel layersSuperfamily a.129.1: GroEL equatorial domain-like [48592] (2 families) 
duplication: two 4-helical subdomains are related by a pseudo dyad passing through the ATP-binding siteFamily a.129.1.2: Group II chaperonin (CCT, TRIC), ATPase domain [48596] (1 protein)
Protein:
Thermosome, E domain [48597] (3 species) Species Thermococcus sp. ks-1, alpha chain [TaxId:79679] [101457] (4 PDB entries) 
Species Thermoplasma acidophilum, alpha chain [TaxId:2303] [100916] (2 PDB entries) 
Species Thermoplasma acidophilum, beta chain [TaxId:2303] [100917] (2 PDB entries)
More info for Family a.129.1.2: Group II chaperonin (CCT, TRIC), ATPase domain
Timeline for Family a.129.1.2: Group II chaperonin (CCT, TRIC), ATPase domain:
- Family a.129.1.2: Group II chaperonin (CCT, TRIC), ATPase domain first appeared (with stable ids) in SCOP 1.55, called Family a.129.1.2: Group II chaperonin (CCT, TRIC)
- Family a.129.1.2: Group II chaperonin (CCT, TRIC), ATPase domain appears in SCOPe 2.05
- Family a.129.1.2: Group II chaperonin (CCT, TRIC), ATPase domain appears in SCOPe 2.07
- Family a.129.1.2: Group II chaperonin (CCT, TRIC), ATPase domain appears in the current release, SCOPe 2.08