D
IPR032678

tRNA synthetases class I, catalytic domain

InterPro entry
Short nametRNA-synt_1_cat_dom
Overlapping
homologous
superfamilies
 

Description

This entry represents the catalytic (Rossmann-fold) domain found in cysteinyl tRNA synthetases
[3]
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
[1]
. 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
[2, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14]
.

References

1.Sequence determination and modeling of structural motifs for the smallest monomeric aminoacyl-tRNA synthetase. Hou YM, Shiba K, Mottes C, Schimmel P. Proc. Natl. Acad. Sci. U.S.A. 88, 976-80, (1991). View articlePMID: 1992490

2.Structural origins of amino acid selection without editing by cysteinyl-tRNA synthetase. Newberry KJ, Hou YM, Perona JJ. EMBO J. 21, 2778-87, (2002). View articlePMID: 12032090

3.Adaptation to tRNA acceptor stem structure by flexible adjustment in the catalytic domain of class I tRNA synthetases. Liu C, Sanders JM, Pascal JM, Hou YM. RNA 18, 213-21, (2012). View articlePMID: 22184460

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.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.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

7.A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases. Landes C, Perona JJ, Brunie S, Rould MA, Zelwer C, Steitz TA, Risler JL. Biochimie 77, 194-203, (1995). View articlePMID: 7647112

8.On the evolution of structure in aminoacyl-tRNA synthetases. O'Donoghue P, Luthey-Schulten Z. Microbiol. Mol. Biol. Rev. 67, 550-73, (2003). View articlePMID: 14665676

9.Phylogenetic analysis of the aminoacyl-tRNA synthetases. Nagel GM, Doolittle RF. J. Mol. Evol. 40, 487-98, (1995). View articlePMID: 7783224

10.Domain-domain communication in aminoacyl-tRNA synthetases. Alexander RW, Schimmel P. Prog. Nucleic Acid Res. Mol. Biol. 69, 317-49, (2001). View articlePMID: 11550797

11.The new aspects of aminoacyl-tRNA synthetases. Szymanski M, Deniziak M, Barciszewski J. Acta Biochim. Pol. 47, 821-34, (2000). PMID: 11310981

12.The aminoacyl-tRNA synthetase family: modules at work. Delarue M, Moras D. Bioessays 15, 675-87, (1993). View articlePMID: 8274143

13.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

14.The cytidylyltransferase superfamily: identification of the nucleotide-binding site and fold prediction. Bork P, Holm L, Koonin EV, Sander C. Proteins 22, 259-66, (1995). View articlePMID: 7479698

Cross References

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