SCOPe 2.08: Family d.142.1.1: ATP-binding domain of peptide synthetases

Lineage for Family d.142.1.1: ATP-binding domain of peptide synthetases

1. Root: SCOPe 2.08

2. Class d: Alpha and beta proteins (a+b) [53931] (396 folds)

3. 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 superfamilies

4. Superfamily d.142.1: Glutathione synthetase ATP-binding domain-like [56059] (11 families)

5. Family d.142.1.1: ATP-binding domain of peptide synthetases [56060] (4 proteins)

Proteins:

1. D-ala-D-ala ligase, C-domain [56063] (1 species)

   • Species Escherichia coli, gene ddlB [TaxId:562] [56064] (3 PDB entries)

2. D-alanine:D-lactate ligase VanA, C-domain [56065] (2 species)

   1. Species Enterococcus faecium [TaxId:1352] [64402] (1 PDB entry)

   2. Species Leuconostoc mesenteroides, Ddl2 [TaxId:1245] [56066] (1 PDB entry)

3. Prokaryotic glutathione synthetase, C-domain [56061] (1 species)

   • Species Escherichia coli [TaxId:562] [56062] (4 PDB entries)

4. automated matches [268128] (1 species)
   not a true protein

   • Species Escherichia coli [TaxId:83333] [268129] (3 PDB entries)

More info for Family d.142.1.1: ATP-binding domain of peptide synthetases

Timeline for Family d.142.1.1: ATP-binding domain of peptide synthetases:

• Family d.142.1.1: ATP-binding domain of peptide synthetases first appeared (with stable ids) in SCOP 1.55, called Family d.142.1.1: Peptide synthetases, C-terminal domain
  
• Family d.142.1.1: ATP-binding domain of peptide synthetases appears in SCOPe 2.07