Lineage for Protein: Copper chaperone for superoxide dismutase, N-terminal domain
- Root: SCOP 1.69
Class d: Alpha and beta proteins (a+b) [53931] (279 folds) 
Fold d.58: Ferredoxin-like [54861] (49 superfamilies)
alpha+beta sandwich with antiparallel beta-sheet; (beta-alpha-beta)x2
Superfamily d.58.17: HMA, heavy metal-associated domain [55008] (1 family) 
Family d.58.17.1: HMA, heavy metal-associated domain [55009] (8 proteins) 
Protein Copper chaperone for superoxide dismutase, N-terminal domain [55019] (1 species)
Species:
Baker's yeast (Saccharomyces cerevisiae) [TaxId:4932] [55020] (2 PDB entries) - Domains for 1jk9:
Domain d1jk9b2: 1jk9 B:3-73 [63151]
Other proteins in same PDB: d1jk9a_, d1jk9b1, d1jk9c_, d1jk9d1
Domain d1jk9d2: 1jk9 D:3-73 [63154]
Other proteins in same PDB: d1jk9a_, d1jk9b1, d1jk9c_, d1jk9d1
- Domains for 1qup:
Domain d1qupa2: 1qup A:2-73 [39352]
Other proteins in same PDB: d1qupa1, d1qupb1
Domain d1qupb2: 1qup B:5-73 [39353]
Other proteins in same PDB: d1qupa1, d1qupb1
- Domains for 1jk9:
More info for Protein Copper chaperone for superoxide dismutase, N-terminal domain from d.58.17.1: HMA, heavy metal-associated domain
Timeline for Protein Copper chaperone for superoxide dismutase, N-terminal domain from d.58.17.1: HMA, heavy metal-associated domain:
- Protein Copper chaperone for superoxide dismutase, N-terminal domain from d.58.17.1: HMA, heavy metal-associated domain first appeared (with stable ids) in SCOP 1.55, called Protein Copper chaperone for superoxide dismutase, N-terminal domain from d.58.17.1: Metal-binding domain
- Protein Copper chaperone for superoxide dismutase, N-terminal domain from d.58.17.1: HMA, heavy metal-associated domain appears in SCOP 1.67
- Protein Copper chaperone for superoxide dismutase, N-terminal domain from d.58.17.1: HMA, heavy metal-associated domain appears in SCOP 1.71
- Protein Copper chaperone for superoxide dismutase, N-terminal domain from d.58.17.1: HMA, heavy metal-associated domain appears in the current release, SCOPe 2.08