PROSITE documentation PDOC50886
tRNA-binding domain profile


The tRNA-binding domain (TRBD) [1] 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:

  • Mammalian endothelial-monocyte activating polypeptide II (EMAP-II). EMAP-II is an inflammatory cytokine produced after apoptotic cleavage of the multisynthetase complex auxiliary component p43.
  • Yeast GU4 nucleic-binding protein 1 or ARC1 protein. It binds to tRNA and functions as a cofactor for the methionyl- and glutamyl-tRNA synthetases.
  • Bacterial proteins of the Trb11/CsaA family, which consist only of a TRBD domain.

The profile we developed covers the entire TRBD domain.

Last update:

November 2002 / First entry.


Technical section

PROSITE method (with tools and information) covered by this documentation:

TRBD, PS50886; tRNA-binding domain profile  (MATRIX)


1AuthorsKaminska M. Deniziak M. Kerjan P. Barciszewski J. Mirande M.
TitleA recurrent general RNA binding domain appended to plant methionyl-tRNA synthetase acts as a cis-acting cofactor for aminoacylation.
SourceEMBO J. 19:6908-6917(2000).
PubMed ID11118226

2AuthorsGalani K. Grosshans H. Deinert K. Hurt E.C. Simos G.
TitleThe intracellular location of two aminoacyl-tRNA synthetases depends on complex formation with Arc1p.
SourceEMBO J. 20:6889-6898(2001).
PubMed ID11726524

3AuthorsKim Y. Shin J. Li R. Cheong C. Kim K. Kim S.
TitleA novel anti-tumor cytokine contains an RNA binding motif present in aminoacyl-tRNA synthetases.
SourceJ. Biol. Chem. 275:27062-27068(2000).
PubMed ID10852899

4AuthorsCrepin T. Schmitt E. Blanquet S. Mechulam Y.
TitleStructure and function of the C-terminal domain of methionyl-tRNA synthetase.
SourceBiochemistry 41:13003-13011(2002).
PubMed ID12390027

5AuthorsRenault L. Kerjan P. Pasqualato S. Menetrey J. Robinson J.-C. Kawaguchi S. Vassylyev D.G. Yokoyama S. Mirande M. Cherfils J.
TitleStructure of the EMAPII domain of human aminoacyl-tRNA synthetase complex reveals evolutionary dimer mimicry.
SourceEMBO J. 20:570-578(2001).
PubMed ID11157763

6AuthorsKawaguchi S. Mueller J. Linde D. Kuramitsu S. Shibata T. Inoue Y. Vassylyev D.G. Yokoyama S.
TitleThe crystal structure of the ttCsaA protein: an export-related chaperone from Thermus thermophilus.
SourceEMBO J. 20:562-569(2001).
PubMed ID11157762

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