Arginyl-tRNA synthetase, catalytic core domain (IPR035684)

Short name: ArgRS_core

Overlapping homologous superfamilies

Domain relationships



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 [PMID: 11106639].

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.