Ontology highlight
ABSTRACT:
SUBMITTER: Shimizu S
PROVIDER: S-EPMC2564875 | biostudies-literature | 2008 Oct
REPOSITORIES: biostudies-literature
Acta crystallographica. Section F, Structural biology and crystallization communications 20080930 Pt 10
Threonyl-tRNA synthetase (ThrRS) plays an essential role in protein synthesis by catalyzing the aminoacylation of tRNA(Thr) and editing misacylation. ThrRS generally contains an N-terminal editing domain, a catalytic domain and an anticodon-binding domain. The sequences of the editing domain in ThrRSs from archaea differ from those in bacteria and eukaryotes. Furthermore, several creanarchaea including Aeropyrum pernix K1 and Sulfolobus tokodaii strain 7 contain two genes encoding either the cat ...[more]