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The fidelity of protein synthesis requires efficient discrimination of amino acid substrates by aminoacyl-tRNA synthetases. ArgRS (Arginyl-tRNA synthetase), also known as RARS or DALRD1, belongs to the class-I aminoacyl-tRNA synthetase family that includes the related proteins, LeuRS, ValRS and IleRS. These proteins are large monomeric proteins and play a major role in catalyzing the aminoacylation of tRNA by their cognate amino acid. ArgRS localizes to the cytoplasm and exists as a monomer but can also associate with other tRNA synthetases and auxiliary proteins to form a multisubunit complex. In the presence of ATP, arginine (Arg) and tRNA, ArgRS joins Arg to tRNA(Arg) at its synthetic active site. Two cytoplasmic forms of ArgRS have been described in mammals, differing by the addition of a 73 amino acid sequence that is required for ArgRS assembly into the multisubunit complex.
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