SCOPe 2.05: Domain d3baaa_: 3baa A:

Lineage for d3baaa_ (3baa A:)

1. Root: SCOPe 2.05

2. Class d: Alpha and beta proteins (a+b) [53931] (381 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 Enterococcus faecalis [TaxId:1351] [118124] (9 PDB entries)
   Uniprot Q837V6 5-317

8. Domain d3baaa_: 3baa A: [172516]
   automated match to d1taea_
   complexed with 3ba, gol, nmn, so4

Details for d3baaa_

PDB Entry: 3baa, 1.9 Å

PDB Description: Structural Basis for the Inhibition of Bacterial NAD+ Dependent DNA Ligase

PDB Compounds: (A:) DNA ligase

SCOPe Domain Sequences for d3baaa_:

Sequence; same for both SEQRES and ATOM records:

>d3baaa_ d.142.2.2 (A:) Adenylation domain of NAD+-dependent DNA ligase {Enterococcus faecalis [TaxId: 1351]}
ltltaattraqelrkqlnqysheyyvkdqpsvedyvydrlykelvdietefpdlitpdsp
tqrvggkvlsgfekaphdipmyslndgfskedifafdervrkaigkpvayccelkidgla
islryengvfvrgatrgdgtvgenitenlrtvrsvpmrltepisvevrgecympkqsfva
lneereengqdifanprnaaagslrqldtkivakrnlntflytvadfgpmkaktqfeale
elsaigfrtnperqlcqsidevwayieeyhekrstlpyeidgivikvnefalqdelgftv
kaprwaiaykfp

Timeline for d3baaa_:

• d3baaa_ first appeared in SCOPe 2.01
  
• d3baaa_ appears in SCOPe 2.04
  
• d3baaa_ appears in SCOPe 2.06
  
• d3baaa_ appears in the current release, SCOPe 2.08