|Ensembl ID||Symbol||Entrez ID||RBD||RBPome||PRI||Expresion||Pathway||Phenotype||Paralog||Ortholog||GO|
Other tRNA synthetase sub-families are too dissimilar to be included. This family includes only arginyl tRNA synthetase.
Arginyl tRNA synthetase (ArgRS), a class I aminoacyl tRNA synthetase, is a monomer which aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. The core domain is based on the Rossman fold and is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. There are at least three subgroups of ArgRS. One type contains both characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding. The second subtype lacks the KMSKS motif; however, it has a lysine N-terminal to the HIGH motif, which serves as the functional counterpart to the second lysine of the KMSKS motif. A third group, which is found primarily in archaea and a few bacteria, lacks both the KMSKS motif and the HIGH loop lysine [PUBMED:11106639].