Lineage for Protein: D-ala-D-ala ligase, C-domain
- Root: SCOPe 2.04
Class d: Alpha and beta proteins (a+b) [53931] (380 folds) 
Fold d.142: ATP-grasp [56058] (2 superfamilies)
Consists of two subdomains with different alpha+beta folds
shares functional and structural similarities with the PIPK and protein kinase superfamiliesSuperfamily d.142.1: Glutathione synthetase ATP-binding domain-like [56059] (10 families) 
Family d.142.1.1: ATP-binding domain of peptide synthetases [56060] (3 proteins) Protein D-ala-D-ala ligase, C-domain [56063] (1 species)
Species:
Escherichia coli, gene ddlB [TaxId:562] [56064] (3 PDB entries) - Domain for 1iov:
Domain d1iova2: 1iov A:97-306 [41482]
Other proteins in same PDB: d1iova1
complexed with adp, mg, pob
- Domain for 1iow:
Domain d1iowa2: 1iow A:97-306 [41481]
Other proteins in same PDB: d1iowa1
complexed with adp, mg, phy
- Domain for 2dln:
Domain d2dlna2: 2dln A:97-306 [41483]
Other proteins in same PDB: d2dlna1
complexed with adp, mg, phy
- Domain for 1iov:
More info for Protein D-ala-D-ala ligase, C-domain from d.142.1.1: ATP-binding domain of peptide synthetases
Timeline for Protein D-ala-D-ala ligase, C-domain from d.142.1.1: ATP-binding domain of peptide synthetases:
- Protein D-ala-D-ala ligase, C-domain from d.142.1.1: ATP-binding domain of peptide synthetases first appeared (with stable ids) in SCOP 1.55, called Protein D-ala-D-ala ligase from d.142.1.1: Peptide synthetases, C-terminal domain
- Protein D-ala-D-ala ligase, C-domain from d.142.1.1: ATP-binding domain of peptide synthetases appears in SCOPe 2.03
- Protein D-ala-D-ala ligase, C-domain from d.142.1.1: ATP-binding domain of peptide synthetases appears in SCOPe 2.05
- Protein D-ala-D-ala ligase, C-domain from d.142.1.1: ATP-binding domain of peptide synthetases appears in the current release, SCOPe 2.08