Lineage for d1taed_ (1tae D:)

  1. Root: SCOPe 2.07
  2. 2494617Class d: Alpha and beta proteins (a+b) [53931] (388 folds)
  3. 2541368Fold 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. 2541972Superfamily d.142.2: DNA ligase/mRNA capping enzyme, catalytic domain [56091] (6 families) (S)
    has a circularly permuted topology
  5. 2541988Family d.142.2.2: Adenylation domain of NAD+-dependent DNA ligase [56096] (2 proteins)
    automatically mapped to Pfam PF01653
  6. 2541989Protein Adenylation domain of NAD+-dependent DNA ligase [56097] (4 species)
    contains additional, N-terminal all-alpha subdomain
  7. 2541993Species Enterococcus faecalis [TaxId:1351] [118124] (9 PDB entries)
    Uniprot Q837V6 5-317
  8. 2542005Domain d1taed_: 1tae D: [112379]
    complexed with na, nad, so4

Details for d1taed_

PDB Entry: 1tae (more details), 2.7 Å

PDB Description: Structural rearrangement accompanying NAD+ synthesis within a bacterial DNA ligase crystal
PDB Compounds: (D:) DNA ligase, NAD-dependent

SCOPe Domain Sequences for d1taed_:

Sequence; same for both SEQRES and ATOM records: (download)

>d1taed_ d.142.2.2 (D:) Adenylation domain of NAD+-dependent DNA ligase {Enterococcus faecalis [TaxId: 1351]}
qpltltaattraqelrkqlnqysheyyvkdqpsvedyvydrlykelvdietefpdlitpd
sptqrvggkvlsgfekaphdipmyslndgfskedifafdervrkaigkpvayccelkidg
laislryengvfvrgatrgdgtvgenitenlrtvrsvpmrltepisvevrgecympkqsf
valneereengqdifanprnaaagslrqldtkivakrnlntflytvadfgpmkaktqfea
leelsaigfrtnperqlcqsidevwayieeyhekrstlpyeidgivikvnefalqdelgf
tvkaprwaiaykfppeeaetv

SCOPe Domain Coordinates for d1taed_:

Click to download the PDB-style file with coordinates for d1taed_.
(The format of our PDB-style files is described here.)

Timeline for d1taed_: