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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC00614
WHEP-TRS domain signature and profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00614

Description

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.

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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)


References

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
DOI10.1021/bi001393h

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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