<p>The aminoacyl-tRNA synthetases (<db_xref db="EC" dbkey="6.1.1."/>) catalyse the attachment of an amino acid to its cognate transfer RNA molecule in a highly specific two-step reaction. These proteins differ widely in size and oligomeric state, and have limited sequence homology [<cite idref="PUB00007191"/>]. The 20 aminoacyl-tRNA synthetases are divided into two classes, I and II. Class I aminoacyl-tRNA synthetases contain a characteristic Rossman fold catalytic domain and are mostly monomeric [<cite idref="PUB00006477"/>]. Class II aminoacyl-tRNA synthetases share an anti-parallel beta-sheet fold flanked by alpha-helices [<cite idref="PUB00000386"/>], and are mostly dimeric or multimeric, containing at least three conserved regions [<cite idref="PUB00000723"/>, <cite idref="PUB00005365"/>, <cite idref="PUB00004391"/>]. However, tRNA binding involves an alpha-helical structure that is conserved between class I and class II synthetases. In reactions catalysed by the class I aminoacyl-tRNA synthetases, the aminoacyl group is coupled to the 2'-hydroxyl of the tRNA, while, in class II reactions, the 3'-hydroxyl site is preferred. The synthetases specific for arginine, cysteine, glutamic acid, glutamine, isoleucine, leucine, methionine, tyrosine, tryptophan and valine belong to class I synthetases. The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine belong to class-II synthetases [<cite idref="PUB00015156"/>]. Based on their mode of binding to the tRNA acceptor stem, both classes of tRNA synthetases have been subdivided into three subclasses, designated 1a, 1b, 1c and 2a, 2b, 2c.</p><p>The class Ia aminoacyl-tRNA synthetases consist of the isoleucyl, methionyl, valyl, leucyl, cysteinyl, and arginyl-tRNA synthetases; the class Ib include the glutamyl and glutaminyl-tRNA synthetases, and the class Ic are the tyrosyl and tryptophanyl-tRNA synthetases [<cite idref="PUB00055442"/>].</p><p> Tyrosyl-tRNA synthetases (<db_xref db="EC" dbkey="6.1.1.1"/>) are widely distributed, being found in archaea, bacteria and eukaryotes. Studies on tyrosyl-tRNA synthetase have shown that the 'KMSKS' motif plays a role in the initial binding of tRNA(Tyr) to tyrosyl-tRNA synthetase [<cite idref="PUB00006465"/>].</p>