<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>Phenylalanyl-tRNA synthetase (<db_xref db="EC" dbkey="6.1.1.20"/>) is an alpha2/beta2 tetramer composed of 2 subunits that belongs to class IIc. In eubacteria, a small subunit (pheS gene) can be designated as beta (E. coli) or alpha subunit (see <db_xref db="INTERPRO" dbkey="IPR002319"/>). Reciprocally the large subunit(pheT gene) can be designated as alpha (E. coli) or beta. In all other kingdoms the two subunits have equivalent length in eukaryota, and can be identified by specific signatures. The enzyme from <taxon tax_id="274">Thermus thermophilus</taxon> has an alpha 2 beta 2 type quaternary structure and is one of the most complicated members of the synthetase family. Identification of phenylalanyl-tRNA synthetase as a member of class II aaRSs was based only on sequence alignment of the small alpha-subunit with other synthetases [<cite idref="PUB00006305"/>].</p><p>This family describes the beta subunit. The beta subunits break into two subfamilies that are considerably different in sequence, length, and pattern of gaps (see also <db_xref db="INTERPRO" dbkey="IPR004531"/>). This family represents the subfamily that includes the beta subunit from bacteria other than spirochetes, as well as a chloroplast-encoded form from <taxon tax_id="2787">Porphyra purpurea</taxon>. The chloroplast-derived sequence is considerably shorter at the N-terminal.</p> Phenylalanyl-tRNA synthetase, class IIc, beta subunit, bacterial