Aminoacyl-tRNA synthetases (aaRSs) play a crucial role in the translation of the genetic code by means of covalent attachment of amino acids to their cognate tRNAs. Phenylalanine--tRNA synthetase (PheRS) is known to be among the most complex enzymes of the aaRS family. Bacterial and mitochondrial PheRSs share a ferredoxin-fold anticodon binding (FDX-ACB) domain, which represents a canonical double split α+β motif having no insertions. The FDX-ACB domain displays a typical RNA recognition fold (RRM) (see <PDOC00030>) formed by the four-stranded antiparallel β sheet, with two helices packed against it (see <PDB:3CMQ>) [1,2,3,4,5].

The profile we developed covers the entire FDX-ACB domain.

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