Lineage for Family c.1.9.11: D-aminoacylase, catalitic domain
- Root: SCOP 1.63
Class c: Alpha and beta proteins (a/b) [51349] (117 folds) 
Fold c.1: TIM beta/alpha-barrel [51350] (26 superfamilies)
contains parallel beta-sheet barrel, closed; n=8, S=8; strand order 12345678
the first seven superfamilies have similar phosphate-binding sites
Superfamily c.1.9: Metallo-dependent hydrolases [51556] (12 families) 
the beta-sheet barrel is similarly distorted and capped by a C-terminal helix
has transition metal ions bound inside the barrel
Family c.1.9.11: D-aminoacylase, catalitic domain [82264] (1 protein)
Protein:
N-acyl-D-aminoacid amidohydrolase, catalytic domain [82265] (1 species)
contains small a/b subdomain inserted after strand 7; unusual for the superfamily metal coordination by CysSpecies Alcaligenes faecalis [TaxId:511] [82266] (1 PDB entry)
More info for Family c.1.9.11: D-aminoacylase, catalitic domain
Timeline for Family c.1.9.11: D-aminoacylase, catalitic domain:
- Family c.1.9.11: D-aminoacylase, catalitic domain is new in SCOP 1.63
- Family c.1.9.11: D-aminoacylase, catalitic domain appears in SCOP 1.65
- Family c.1.9.11: D-aminoacylase, catalitic domain appears in the current release, SCOPe 2.08, called Family c.1.9.11: D-aminoacylase, catalytic domain