InterPro domain: IPR033729

Serine--tRNA ligase or seryl-tRNA synthetase (SerRS) is responsible for the attachment of serine to the 3' OH group of ribose of the appropriate tRNA. SerRS is a class II aminoacyl-tRNA synthetase, this assignment is based upon its structure and the presence of three characteristic sequence motifs in the core domain [ 1 , 2 , 3 , 4 ]. This core domain is primarily responsible for ATP-dependent formation of the enzyme bound aminoacyl-adenylate. SerRS synthetase is a homodimer [ 5 , 6 ].

1. Eleven down and nine to go. Nat. Struct. Biol. 2, 824-31
2. 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
3. Genomics and the evolution of aminoacyl-tRNA synthesis. Acta Biochim. Pol. 48, 313-21
4. On the evolution of structure in aminoacyl-tRNA synthetases. Microbiol. Mol. Biol. Rev. 67, 550-73
5. A second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A. Nature 347, 249-55
6. Refined crystal structure of the seryl-tRNA synthetase from Thermus thermophilus at 2.5 A resolution. J. Mol. Biol. 234, 222-33