SCOPe 2.02: Domain d1v9pa3: 1v9p A:1-317

Lineage for d1v9pa3 (1v9p A:1-317)

1. Root: SCOPe 2.02

2. Class d: Alpha and beta proteins (a+b) [53931] (376 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] (4 families)
   has a circularly permuted topology

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

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] (2 PDB entries)

8. Domain d1v9pa3: 1v9p A:1-317 [100546]
   Other proteins in same PDB: d1v9pa1, d1v9pa2, d1v9pb1, d1v9pb2
   complexed with amp, zn

Details for d1v9pa3

PDB Entry: 1v9p, 2.9 Å

PDB Description: Crystal Structure Of Nad+-Dependent DNA Ligase

PDB Compounds: (A:) DNA ligase

SCOPe Domain Sequences for d1v9pa3:

Sequence; same for both SEQRES and ATOM records:

>d1v9pa3 d.142.2.2 (A:1-317) Adenylation domain of NAD+-dependent DNA ligase {Thermus filiformis [TaxId: 276]}
mtreearrrinelrdliryhnyryyvladpeisdaeydrllrelkeleerfpefkspdsp
teqvgarpleptfrpvrhptrmysldnaftyeevlafeerleralgrkrpflytvehkvd
glsvnlyyeegvlvfgatrgdgevgeevtqnlltiptiprrlkgvpdrlevrgevympie
aflrlneeleergekvfknprnaaagslrqkdprvtakrglratfyalglgleesglksq
yelllwlkekgfpvehgyekalgaegveevyrrflaqrhalpfeadgvvvklddlalwre
lgytaraprfalaykfp

Timeline for d1v9pa3:

• d1v9pa3 first appeared in SCOP 1.67
  
• d1v9pa3 appears in SCOPe 2.01
  
• d1v9pa3 appears in SCOPe 2.03
  
• d1v9pa3 appears in the current release, SCOPe 2.08