InterPro domain: IPR032678

This entry represents the catalytic (Rossmann-fold) domain found in cysteinyl tRNA synthetases [ 1 ] which is responsible for the ATP-dependent formation of the enzyme bound aminoacyl-adenylate. It contains the characteristic class I HIGH and KMSKS motifs, which are involved in ATP binding.

Cysteine-tRNA ligase (also known as cysteinyl-tRNA synthetase) ( 6.1.1.16 ) is an alpha monomer and belongs to class Ia [ 2 ]. It aminoacylates the 2'-OH of the nucleotide at the 3' of the appropriate tRNA. It is highly specific despite not possessing the amino acid editing activity characteristic of many other tRNA ligases [ 3 , 4 , 5 , 6 , 7 , 8 , 9 , 10 , 11 , 12 , 13 , 14 ].

1. Adaptation to tRNA acceptor stem structure by flexible adjustment in the catalytic domain of class I tRNA synthetases. RNA 18, 213-21
2. Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase. Proc. Natl. Acad. Sci. U.S.A. 88, 976-80
3. Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase. EMBO J. 21, 2778-87
4. Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Microbiol. Mol. Biol. Rev. 64, 202-36
5. Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation. RNA 8, 1363-72
6. Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Genome Res. 9, 689-710
7. A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases. Biochimie 77, 194-203
8. On the evolution of structure in aminoacyl-tRNA synthetases. Microbiol. Mol. Biol. Rev. 67, 550-73
9. Phylogenetic analysis of the aminoacyl-tRNA synthetases. J. Mol. Evol. 40, 487-98
10. Domain-domain communication in aminoacyl-tRNA synthetases. Prog. Nucleic Acid Res. Mol. Biol. 69, 317-49
11. The new aspects of aminoacyl-tRNA synthetases. Acta Biochim. Pol. 47, 821-34
12. The aminoacyl-tRNA synthetase family: modules at work. Bioessays 15, 675-87
13. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347, 203-6
14. The cytidylyltransferase superfamily: identification of the nucleotide-binding site and fold prediction. Proteins 22, 259-66