InterPro domain: IPR041616

This entry represents the core domain found in the beta chain of phe tRNA synthetase [ 1 ].

Phenylalanyl-tRNA synthetase (PheRS) belongs to class II aminoacyl-tRNA synthetases (aaRS) based upon its structure. While class II aaRSs generally aminoacylate the 3'-OH ribose of the appropriate tRNA, PheRS is an exception in that it attaches the amino acid at the 2'-OH group, like class I aaRSs. PheRS is an alpha-2/ beta-2 tetramer. While the alpha chain contains a catalytic core domain, the beta chain has a non-catalytic core domain [ 2 , 3 , 4 , 5 , 6 , 7 , 8 ].

1. Idiosyncrasy and identity in the prokaryotic Phe-system: crystal structure of E. coli phenylalanyl-tRNA synthetase complexed with phenylalanine and AMP. Protein Sci. 20, 160-7
2. On the evolution of structure in aminoacyl-tRNA synthetases. Microbiol. Mol. Biol. Rev. 67, 550-73
3. Transfer RNA recognition by aminoacyl-tRNA synthetases. Biopolymers 52, 1-28
4. Domain-domain communication in aminoacyl-tRNA synthetases. Prog. Nucleic Acid Res. Mol. Biol. 69, 317-49
5. The new aspects of aminoacyl-tRNA synthetases. Acta Biochim. Pol. 47, 821-34
6. The aminoacyl-tRNA synthetase family: modules at work. Bioessays 15, 675-87
7. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347, 203-6
8. 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