Member database | Pfam |
Pfam type | domain |
Short name | tRNA-Thr_ED |
Author | Mistry J;0000-0003-2479-5322 Sammut SJ;0000-0003-4472-904X |
Sequence Ontology | 0000417 |
Description
Archaea-specific editing domain of threonyl-tRNA synthetase, with marked structural similarity to D-amino acids deacylases found in eubacteria and eukaryotes. This domain can bind D-amino acids, and ensures high fidelity during translation. It is especially responsible for removing incorrectly attached serine from tRNA-Thr. The domain forms a fold that can be be defined as two layers of beta-sheets (a three-stranded sheet and a five-stranded sheet), with two alpha-helices located adjacent to the five-stranded sheet
[1].
References
1.A D-amino acid editing module coupled to the translational apparatus in archaea. Dwivedi S, Kruparani SP, Sankaranarayanan R. Nat. Struct. Mol. Biol. 12, 556-7, (2005). View articlePMID: 15908961