Member database | CDD |
CDD type | domain |
Short name | HisRS-like_core |
Set | class_II_aaRS-like_core |
Description
References
1.Genomics and the evolution of aminoacyl-tRNA synthesis. Ruan B, Ahel I, Ambrogelly A, Becker HD, Bunjun S, Feng L, Tumbula-Hansen D, Ibba M, Korencic D, Kobayashi H, Jacquin-Becker C, Mejlhede N, Min B, Raczniak G, Rinehart J, Stathopoulos C, Li T, Soll D. Acta Biochim. Pol. 48, 313-21, (2001). PMID: 11732603
2.The quaternary structure of the HisZ-HisG N-1-(5'-phosphoribosyl)-ATP transferase from Lactococcus lactis. Bovee ML, Champagne KS, Demeler B, Francklyn CS. Biochemistry 41, 11838-46, (2002). View articlePMID: 12269828
3.Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events. Wolf YI, Aravind L, Grishin NV, Koonin EV. Genome Res. 9, 689-710, (1999). View articlePMID: 10447505
4.A succession of substrate induced conformational changes ensures the amino acid specificity of Thermus thermophilus prolyl-tRNA synthetase: comparison with histidyl-tRNA synthetase. Yaremchuk A, Tukalo M, Grotli M, Cusack S. J. Mol. Biol. 309, 989-1002, (2001). View articlePMID: 11399074
5.Aminoacyl-tRNA synthetases: versatile players in the changing theater of translation. Francklyn C, Perona JJ, Puetz J, Hou YM. RNA 8, 1363-72, (2002). View articlePMID: 12458790
6.Proteobacterial histidine-biosynthetic pathways are paraphyletic. Bond JP, Francklyn C. J. Mol. Evol. 50, 339-47, (2000). PMID: 10795825
7.An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis. Sissler M, Delorme C, Bond J, Ehrlich SD, Renault P, Francklyn C. Proc. Natl. Acad. Sci. U.S.A. 96, 8985-90, (1999). View articlePMID: 10430882
8.Eleven down and nine to go. Cusack S. Nat. Struct. Biol. 2, 824-31, (1995). View articlePMID: 7552701