Lineage for Fold b.82: Double-stranded beta-helix
- Root: SCOPe 2.06
Class b: All beta proteins [48724] (177 folds) 
Fold b.82: Double-stranded beta-helix [51181] (7 superfamilies)
one turn of helix is made by two pairs of antiparallel strands linked with short turns
has appearance of a sandwich of distinct architecture and jelly-roll topology
Superfamilies:
b.82.1: RmlC-like cupins [51182] (25 families) 
b.82.2: Clavaminate synthase-like [51197] (16 families)
Iron and ketoglutarate-dependent enzymes; elaborated version of this common fold
b.82.3: cAMP-binding domain-like [51206] (4 families) 
b.82.4: Regulatory protein AraC [51215] (1 family)
automatically mapped to Pfam PF02311
b.82.5: TRAP-like [51219] (2 families)
shorter variant of double-helix; assembles in large ring-like structures containing from 9 to 11 domains
b.82.6: Thiamin pyrophosphokinase, substrate-binding domain [63862] (1 family) 
b.82.7: Metal cation-transporting ATPase, actuator domain A [81653] (1 family)
a distorted variant of double-helix
More info for Fold b.82: Double-stranded beta-helix
Timeline for Fold b.82: Double-stranded beta-helix:
- Fold b.82: Double-stranded beta-helix first appeared (with stable ids) in SCOP 1.55
- Fold b.82: Double-stranded beta-helix appears in SCOPe 2.05
- Fold b.82: Double-stranded beta-helix appears in SCOPe 2.07
- Fold b.82: Double-stranded beta-helix appears in the current release, SCOPe 2.08