PROSITE documentation PDOC00614
WHEP-TRS domain signature and profile


A conserved domain of 46 amino acids has been shown [1] to exist in a number of higher eukaryote aminoacyl-transfer RNA synthetases. This domain is present one to six times in the following enzymes:

  • Mammalian multifunctional aminoacyl-tRNA synthetase. The domain is present three times in a region that separates the N-terminal glutamyl-tRNA synthetase domain from the C-terminal prolyl-tRNA synthetase domain.
  • Drosophila multifunctional aminoacyl-tRNA synthetase. The domain is present six times in the intercatalytic region.
  • Mammalian tryptophanyl-tRNA synthetase. The domain is found at the N- terminal extremity.
  • Mammalian, insect, nematode and plant glycyl-tRNA synthetase. The domain is found at the N-terminal extremity [2].
  • Mammalian histidyl-tRNA synthetase. The domain is found at the N-terminal extremity.

The structure of a human WHEP-TRS domain has been solved by NMR (see <PDB:1FYJ>) [3]. It consists of two helices arranged in a helix-turn-helix. This domain may play a role in the association of tRNA-synthetases into multienzyme complexes [4].

We developed a signature pattern based on the first 29 positions of the WHEP-domain. We also developed a profile that covers the whole WHEP-TRS domain.

Last update:

April 2006 / Pattern revised.


Technical section

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

WHEP_TRS_2, PS51185; WHEP-TRS domain profile  (MATRIX)

WHEP_TRS_1, PS00762; WHEP-TRS domain signature  (PATTERN)


1AuthorsCerini C. Kerjan P. Astier M. Gratecos D. Mirande M. Semeriva M.
TitleA component of the multisynthetase complex is a multifunctional aminoacyl-tRNA synthetase.
SourceEMBO J. 10:4267-4277(1991).
PubMed ID1756734

2AuthorsNada S. Chang P.K. Dignam J.D.
TitlePrimary structure of the gene for glycyl-tRNA synthetase from Bombyx mori.
SourceJ. Biol. Chem. 268:7660-7667(1993).
PubMed ID8463296

3AuthorsJeong E.J. Hwang G.S. Kim K.H. Kim M.J. Kim S. Kim K.S.
TitleStructural analysis of multifunctional peptide motifs in human bifunctional tRNA synthetase: identification of RNA-binding residues and functional implications for tandem repeats.
SourceBiochemistry 39:15775-15782(2000).
PubMed ID11123902

4AuthorsRho S.B. Lee J.S. Jeong E.J. Kim K.S. Kim Y.G. Kim S.
TitleA multifunctional repeated motif is present in human bifunctional tRNA synthetase.
SourceJ. Biol. Chem. 273:11267-11273(1998).
PubMed ID9556618

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