Aminoacyl-tRNA synthetase, class I, anticodon-binding domain, subdomain 2
Short name | aa-tRNA-synth_I_codon-bd_sub2 |
Overlapping entries |
Description
References
1.Sequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases. Cusack S, Hartlein M, Leberman R. Nucleic Acids Res. 19, 3489-98, (1991). View articlePMID: 1852601
2.Structural basis for transfer RNA aminoacylation by Escherichia coli glutaminyl-tRNA synthetase. Perona JJ, Rould MA, Steitz TA. Biochemistry 32, 8758-71, (1993). View articlePMID: 8364025
3.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
4.Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Woese CR, Olsen GJ, Ibba M, Soll D. Microbiol. Mol. Biol. Rev. 64, 202-36, (2000). View articlePMID: 10704480
5.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
6.The 2.0 A crystal structure of Thermus thermophilus methionyl-tRNA synthetase reveals two RNA-binding modules. Sugiura I, Nureki O, Ugaji-Yoshikawa Y, Kuwabara S, Shimada A, Tateno M, Lorber B, Giege R, Moras D, Yokoyama S, Konno M. Structure 8, 197-208, (2000). View articlePMID: 10673435
7.Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Eriani G, Delarue M, Poch O, Gangloff J, Moras D. Nature 347, 203-6, (1990). View articlePMID: 2203971
8.Classes of aminoacyl-tRNA synthetases and the establishment of the genetic code. Schimmel P. Trends Biochem. Sci. 16, 1-3, (1991). View articlePMID: 2053131
9.The aminoacyl-tRNA synthetase family: modules at work. Delarue M, Moras D. Bioessays 15, 675-87, (1993). View articlePMID: 8274143
Cross References
Contributing Member Database Entry
- CATH-Gene3D:G3DSA:1.10.10.350