SCOP 1.63: Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain

Lineage for Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain

1. Root: SCOP 1.63

2. Class d: Alpha and beta proteins (a+b) [53931] (224 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.142.2: DNA ligase/mRNA capping enzyme, catalytic domain [56091] (3 families)
   has a circularly permuted topology

Families:

1. d.142.2.1: ATP-dependent DNA ligase, N-terminal domain [56092] (1 protein)

2. d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase [56096] (1 protein)

3. d.142.2.3: RNA guanylyltransferase (mRNA capping enzyme), N-terminal domain [56100] (1 protein)

More info for Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain

Timeline for Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain:

• Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain first appeared (with stable ids) in SCOP 1.55
  
• Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain appears in SCOP 1.61
  
• Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain appears in SCOP 1.65
  
• Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain appears in the current release, SCOPe 2.08