Lineage for Protein: Two-domain dihydroorotase
- Root: SCOP 1.73
Class b: All beta proteins [48724] (165 folds) 
Fold b.92: Composite domain of metallo-dependent hydrolases [51337] (1 superfamily)
pseudobarrel; mixed sheet of 7 strand folded upon itself and "buckled" by two beta-turnsSuperfamily b.92.1: Composite domain of metallo-dependent hydrolases [51338] (8 families) 
this domain is interrupted by the catalytic beta/alpha barrel domain
Family b.92.1.3: Hydantoinase (dihydropyrimidinase) [75044] (5 proteins) 
Protein Two-domain dihydroorotase [141686] (1 species)
Species:
Aquifex aeolicus [TaxId:63363] [141687] (2 PDB entries) - Domain for 1xrf:
Domain d1xrfa1: 1xrf A:1-55,A:366-422 [122254]
Other proteins in same PDB: d1xrfa2
complexed with so4, zn
- Domains for 1xrt:
Domain d1xrta1: 1xrt A:1-55,A:366-422 [122258]
Other proteins in same PDB: d1xrta2, d1xrtb2
automatically matched to 1XRF A:1-55,A:366-422
complexed with zn
Domain d1xrtb1: 1xrt B:1-55,B:366-422 [122260]
Other proteins in same PDB: d1xrta2, d1xrtb2
automatically matched to 1XRF A:1-55,A:366-422
complexed with zn
- Domain for 1xrf:
More info for Protein Two-domain dihydroorotase from b.92.1.3: Hydantoinase (dihydropyrimidinase)
Timeline for Protein Two-domain dihydroorotase from b.92.1.3: Hydantoinase (dihydropyrimidinase):
- Protein Two-domain dihydroorotase from b.92.1.3: Hydantoinase (dihydropyrimidinase) is new in SCOP 1.73
- Protein Two-domain dihydroorotase from b.92.1.3: Hydantoinase (dihydropyrimidinase) appears in SCOP 1.75
- Protein Two-domain dihydroorotase from b.92.1.3: Hydantoinase (dihydropyrimidinase) appears in the current release, SCOPe 2.08