SCOPe 2.01: Domain d1tkya2: 1tky A:63-224

Lineage for d1tkya2 (1tky A:63-224)

1. Root: SCOPe 2.01

2. Class d: Alpha and beta proteins (a+b) [53931] (376 folds)

3. Fold d.67: RRF/tRNA synthetase additional domain-like [55185] (4 superfamilies)
   core: alpha-beta(2)-alpha-beta(2); 2 layers: alpha/beta

4. Superfamily d.67.1: ThrRS/AlaRS common domain [55186] (2 families)
   putative editing domain found in the N-terminal part of ThrRS, the C-terminal of AlaRS, and as a stand-alone protein; probable circular permutation of LuxS (d.185.1.2)

5. Family d.67.1.1: Threonyl-tRNA synthetase (ThrRS), second 'additional' domain [55187] (1 protein)

6. Protein Threonyl-tRNA synthetase (ThrRS), second 'additional' domain [55188] (2 species)

7. Species Escherichia coli [TaxId:562] [55189] (5 PDB entries)
   Uniprot P0A8M3

8. Domain d1tkya2: 1tky A:63-224 [112489]
   Other proteins in same PDB: d1tkya1
   protein/RNA complex; complexed with a3s

Details for d1tkya2

PDB Entry: 1tky, 1.48 Å

PDB Description: Crystal structure of the editing domain of threonyl-tRNA synthetase complexed with seryl-3'-aminoadenosine

PDB Compounds: (A:) threonyl-tRNA synthetase

SCOPe Domain Sequences for d1tkya2:

Sequence; same for both SEQRES and ATOM records:

>d1tkya2 d.67.1.1 (A:63-224) Threonyl-tRNA synthetase (ThrRS), second 'additional' domain {Escherichia coli [TaxId: 562]}
kdeegleiirhscahllghaikqlwphtkmaigpvidngfyydvdldrtltqedvealek
rmhelaeknydvikkkvswhearetfanrgesykvsildeniahddkpglyfheeyvdmc
rgphvpnmrfchhfklmktagaywrgdsnnkmlqriygtawa

Timeline for d1tkya2:

• d1tkya2 first appeared in SCOP 1.71
  
• d1tkya2 appears in SCOP 1.75
  
• d1tkya2 appears in SCOPe 2.02
  
• d1tkya2 appears in the current release, SCOPe 2.08