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.
Human phenylalanyl-tRNA synthetase: cloning, characterization of the deduced amino acid sequences in terms of the structural domains and coordinately regulated expression of the alpha and beta subunits in chronic myeloid leukemia cells.
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