SCOPe 2.01: Domain d1taeb_: 1tae B:

Lineage for d1taeb_ (1tae B:)

1. Root: SCOPe 2.01

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] (1 protein)

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] (6 PDB entries)
   Uniprot Q837V6 5-317

8. Domain d1taeb_: 1tae B: [112377]
   complexed with na, nad, so4

Details for d1taeb_

PDB Entry: 1tae, 2.7 Å

PDB Description: Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal

PDB Compounds: (B:) DNA ligase, NAD-dependent

SCOPe Domain Sequences for d1taeb_:

Sequence; same for both SEQRES and ATOM records:

>d1taeb_ d.142.2.2 (B:) Adenylation domain of NAD+-dependent DNA ligase {Enterococcus faecalis [TaxId: 1351]}
qpltltaattraqelrkqlnqysheyyvkdqpsvedyvydrlykelvdietefpdlitpd
sptqrvggkvlsgfekaphdipmyslndgfskedifafdervrkaigkpvayccelkidg
laislryengvfvrgatrgdgtvgenitenlrtvrsvpmrltepisvevrgecympkqsf
valneereengqdifanprnaaagslrqldtkivakrnlntflytvadfgpmkaktqfea
leelsaigfrtnperqlcqsidevwayieeyhekrstlpyeidgivikvnefalqdelgf
tvkaprwaiaykfppeeaetv

Timeline for d1taeb_:

• d1taeb_ first appeared in SCOP 1.71
  
• d1taeb_ appears in SCOP 1.75
  
• d1taeb_ appears in SCOPe 2.02
  
• d1taeb_ appears in the current release, SCOPe 2.08