|PROSITE documentation PDOC50886|
The tRNA-binding domain (TRBD)  is a domain of ~110 amino acids which is widespread among all living organisms, from eubacteria, archaea or eukarya. The TRBD domain, which is also called Trbp111-like domain or EMAP II-like domain, is widely distributed among different tRNA synthetases and their association factors (such as p43, ARC1, and Trbp111 isolated from various species). The TRBD domain has been shown to possess a general tRNA-binding capacity with recognition of the L shape of tRNA and it has been proposed that the TRBD domain might be a non-specific binder of tRNAs acting in cis or in trans to enhance the catalytic efficiency or substrate specificity of aminoacyl-tRNA synthetases [1,2,3,4].
The resolution of the structure of the TRBD domain has shown that part of it adopts the oligonucleotide/oligosaccharide-binding (OB)-fold (see <PDB:1FL0>). The OB-fold of the TRBD domain consists of a five-stranded Greek-key β-barrel capped by a short α-helix located between the third and fourth strands [3,4,5,6].
Some proteins known to contain a TRBD domain are listed below:
The profile we developed covers the entire TRBD domain.Last update:
November 2002 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Kaminska M. Deniziak M. Kerjan P. Barciszewski J. Mirande M.|
|Title||A recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation.|
|Source||EMBO J. 19:6908-6917(2000).|
|2||Authors||Galani K. Grosshans H. Deinert K. Hurt E.C. Simos G.|
|Title||The intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p.|
|Source||EMBO J. 20:6889-6898(2001).|
|3||Authors||Kim Y. Shin J. Li R. Cheong C. Kim K. Kim S.|
|Title||A novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases.|
|Source||J. Biol. Chem. 275:27062-27068(2000).|
|4||Authors||Crepin T. Schmitt E. Blanquet S. Mechulam Y.|
|Title||Structure and function of the C-terminal domain of methionyl-tRNA synthetase.|
|5||Authors||Renault L. Kerjan P. Pasqualato S. Menetrey J. Robinson J.-C. Kawaguchi S. Vassylyev D.G. Yokoyama S. Mirande M. Cherfils J.|
|Title||Structure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry.|
|Source||EMBO J. 20:570-578(2001).|
|6||Authors||Kawaguchi S. Mueller J. Linde D. Kuramitsu S. Shibata T. Inoue Y. Vassylyev D.G. Yokoyama S.|
|Title||The crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.|
|Source||EMBO J. 20:562-569(2001).|