SCOP 1.73: Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase

Root: SCOP 1.73
Class d: Alpha and beta proteins (a+b) [53931] (334 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 superfamilies
Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain [56091] (4 families)
has a circularly permuted topology
Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase [56096] (1 protein)

Adenylation domain of NAD+-dependent DNA ligase [56097] (3 species)
contains additional, N-terminal all-alpha subdomain
1. Species Bacillus stearothermophilus [TaxId:1422] [56098] (1 PDB entry)
2. Species Enterococcus faecalis [TaxId:1351] [118124] (2 PDB entries)
3. Species Thermus filiformis [TaxId:276] [56099] (2 PDB entries)

Timeline for Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase:

Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase first appeared (with stable ids) in SCOP 1.55
Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase appears in SCOP 1.71
Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase appears in SCOP 1.75
Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase appears in the current release, SCOPe 2.08