SCOPe 2.05: Domain d4eeqa_: 4eeq A:

Lineage for d4eeqa_ (4eeq 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 d4eeqa_: 4eeq A: [220460]
   automated match to d4efea_
   protein/DNA complex; complexed with 0ox, nmn, so4

Details for d4eeqa_

PDB Entry: 4eeq, 2.1 Å

PDB Description: Crystal structure of E. faecalis DNA ligase with inhibitor

PDB Compounds: (A:) DNA ligase

SCOPe Domain Sequences for d4eeqa_:

Sequence; same for both SEQRES and ATOM records:

>d4eeqa_ d.142.2.2 (A:) Adenylation domain of NAD+-dependent DNA ligase {Enterococcus faecalis [TaxId: 1351]}
pltltaattraqelrkqlnqysheyyvkdqpsvedyvydrlykelvdietefpdlitpds
ptqrvggkvlsgfekaphdipmyslndgfskedifafdervrkaigkpvayccelkidgl
aislryengvfvrgatrgdgtvgenitenlrtvrsvpmrltepisvevrgecympkqsfv
alneereengqdifanprnaaagslrqldtkivakrnlntflytvadfgpmkaktqfeal
eelsaigfrtnperqlcqsidevwayieeyhekrstlpyeidgivikvnefalqdelgft
vkaprwaiaykfp

Timeline for d4eeqa_:

• d4eeqa_ first appeared in SCOPe 2.03
  
• d4eeqa_ appears in SCOPe 2.04
  
• d4eeqa_ appears in SCOPe 2.06
  
• d4eeqa_ appears in the current release, SCOPe 2.08