SCOPe 2.06: Domain d1dgsa3: 1dgs A:1-314

Lineage for d1dgsa3 (1dgs A:1-314)

1. Root: SCOPe 2.06

2. Class d: Alpha and beta proteins (a+b) [53931] (385 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] (6 families)
   has a circularly permuted topology

5. Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase [56096] (2 proteins)
   automatically mapped to Pfam PF01653

6. Protein Adenylation domain of NAD+-dependent DNA ligase [56097] (4 species)
   contains additional, N-terminal all-alpha subdomain

7. Species Thermus filiformis [TaxId:276] [56099] (3 PDB entries)

8. Domain d1dgsa3: 1dgs A:1-314 [41581]
   Other proteins in same PDB: d1dgsa1, d1dgsa2, d1dgsb1, d1dgsb2
   protein/DNA complex; complexed with amp, zn

Details for d1dgsa3

PDB Entry: 1dgs, 2.9 Å

PDB Description: crystal structure of nad+-dependent dna ligase from t. filiformis

PDB Compounds: (A:) DNA ligase

SCOPe Domain Sequences for d1dgsa3:

Sequence; same for both SEQRES and ATOM records:

>d1dgsa3 d.142.2.2 (A:1-314) Adenylation domain of NAD+-dependent DNA ligase {Thermus filiformis [TaxId: 276]}
mtreearrrinelrdliryhnyryyvladpeisdaeydrllrelkeleerfpefkspdsp
teqvgarpleptfrpvrhptrmysldnaftyeevlafeerlereaeapslytvehkvdgl
svlyyeegvwstgsgdgevgeevtqnlltiptiprrlkgvpdrlevrgevympieaflrl
neeleergekvfknprnaaagslrqkdprvtakrglratfyalglglgleesglksqyel
llwlkekgfpvehcyekalgaegveevyrrglaqrhalpfeadgvvlklddltlwgelgy
taraprfalaykfp

Timeline for d1dgsa3:

• d1dgsa3 first appeared (with stable ids) in SCOP 1.55
  
• d1dgsa3 appears in SCOPe 2.05
  
• d1dgsa3 appears in SCOPe 2.07
  
• d1dgsa3 appears in the current release, SCOPe 2.08