Lineage for Family a.129.1.1: GroEL chaperone, 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 site
Family a.129.1.1: GroEL chaperone, ATPase domain [48593] (1 protein)
Protein:
GroEL, E domain [48594] (4 species) Species Escherichia coli [TaxId:562] [48595] (11 PDB entries) 
Species Mycobacterium tuberculosis, GroEL2 [TaxId:1773] [117031] (1 PDB entry)
Uniprot P0A520 60-514
Species Paracoccus denitrificans [TaxId:266] [69116] (1 PDB entry) 
Species Thermus thermophilus [TaxId:274] [110024] (2 PDB entries)
Uniprot P61491
More info for Family a.129.1.1: GroEL chaperone, ATPase domain
Timeline for Family a.129.1.1: GroEL chaperone, ATPase domain:
- Family a.129.1.1: GroEL chaperone, ATPase domain first appeared (with stable ids) in SCOP 1.55, called Family a.129.1.1: GroEL
- Family a.129.1.1: GroEL chaperone, ATPase domain appears in SCOPe 2.05
- Family a.129.1.1: GroEL chaperone, ATPase domain appears in SCOPe 2.07
- Family a.129.1.1: GroEL chaperone, ATPase domain appears in the current release, SCOPe 2.08