SCOPe 2.03: Domain d4lh6a_: 4lh6 A:

Lineage for d4lh6a_ (4lh6 A:)

1. Root: SCOPe 2.03

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] (5 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] (8 PDB entries)
   Uniprot Q837V6 5-317

8. Domain d4lh6a_: 4lh6 A: [235886]
   automated match to d4lh7a_
   complexed with 1x7, act, na, nmn

Details for d4lh6a_

PDB Entry: 4lh6, 1.65 Å

PDB Description: Crystal structure of a LigA inhibitor

PDB Compounds: (A:) DNA ligase

SCOPe Domain Sequences for d4lh6a_:

Sequence; same for both SEQRES and ATOM records:

>d4lh6a_ d.142.2.2 (A:) Adenylation domain of NAD+-dependent DNA ligase {Enterococcus faecalis [TaxId: 1351]}
eqqpltltaattraqelrkqlnqysheyyvkdqpsvedyvydrlykelvdietefpdlit
pdsptqrvggkvlsgfekaphdipmyslndgfskedifafdervrkaigkpvayccelki
dglaislryengvfvrgatrgdgtvgenitenlrtvrsvpmrltepisvevrgecympkq
sfvalneereengqdifanprnaaagslrqldtkivakrnlntflytvadfgpmkaktqf
ealeelsaigfrtnperqlcqsidevwayieeyhekrstlpyeidgivikvnefalqdel
gftvkaprwaiaykfppeeaet

Timeline for d4lh6a_:

• d4lh6a_ is new in SCOPe 2.03-stable
  
• d4lh6a_ appears in SCOPe 2.04
  
• d4lh6a_ appears in the current release, SCOPe 2.08