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PROSITE documentation PDOC00363 [for PROSITE entry PS50861]

Aminoacyl-transfer RNA synthetases class-II profiles





Description

Aminoacyl-tRNA synthetases (EC 6.1.1.-) [1] are a group of enzymes which activate amino acids and transfer them to specific tRNA molecules as the first step in protein biosynthesis. In prokaryotic organisms there are at least twenty different types of aminoacyl-tRNA synthetases, one for each different amino acid. In eukaryotes there are generally two aminoacyl-tRNA synthetases for each different amino acid: one cytosolic form and a mitochondrial form. While all these enzymes have a common function, they are widely diverse in terms of subunit size and of quaternary structure.

The synthetases specific for alanine, asparagine, aspartic acid, glycine, histidine, lysine, phenylalanine, proline, serine, and threonine are referred to as class-II synthetases [2,3,4,5,6]. Class-II enzymes are generally dimeric or tetrameric, and attach their amino acid to the 3' OH of their tRNA, except for phenylalaninyl-tRNA synthetase which uses the 2' OH like the class-I tRNA synthetase.

Class-II tRNA synthetases are structurally distinct from the class-I enzymes and have a central antiparallel β-sheet instead of the Rossman fold found in Class-I structure (see <PDB:1SES>) [8].

Class-II tRNA synthetases do not share a high degree of similarity, however at least three conserved regions are present [2,5,9]. We have developed three profiles to detect class-II tRNA synthetases. The first one recognize all class-II enzymes except for heterodimeric glycyl-tRNA synthetases and alanyl-tRNA synthetases which are picked up by specific profiles.

There are at least two families of proteins related to class-II enzymes and that are also recognized by the first profile.

  • Bacterial aspartate--ammonia ligase (EC 6.3.1.1), the enzyme that produces asparagine from aspartate [10].
  • Bacterial ATP phosphoribosyltransferase regulatory subunit (gene hisZ). HisZ seems to allow the regulation of ATP phosphoribosyltransferase activity by histidine. It is distantly related to histidyl-tRNA synthetases and not all members of this family are picked up by the profile.

PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html --------------------------------------------------------------------------------.

Expert(s) to contact by email:

Cusack S.

Last update:

May 2002 / Text revised; profiles added; pattern deleted.

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Technical section

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

AA_TRNA_LIGASE_II_GLYAB, PS50861; Heterodimeric glycyl-transfer RNA synthetases family profile  (MATRIX)

AA_TRNA_LIGASE_II, PS50862; Aminoacyl-transfer RNA synthetases class-II family profile  (MATRIX)

AA_TRNA_LIGASE_II_ALA, PS50860; Alanyl-transfer RNA synthetases family profile  (MATRIX)


References

1AuthorsSchimmel P.
TitleAminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs.
SourceAnnu. Rev. Biochem. 56:125-158(1987).
PubMed ID3304131
DOI10.1146/annurev.bi.56.070187.001013

2AuthorsDelarue M. Moras D.
TitleThe aminoacyl-tRNA synthetase family: modules at work.
SourceBioEssays 15:675-687(1993).
PubMed ID8274143

3AuthorsSchimmel P.
TitleClasses of aminoacyl-tRNA synthetases and the establishment of the genetic code.
SourceTrends Biochem. Sci. 16:1-3(1991).
PubMed ID2053131

4AuthorsNagel G.M. Doolittle R.F.
TitleEvolution and relatedness in two aminoacyl-tRNA synthetase families.
SourceProc. Natl. Acad. Sci. U.S.A. 88:8121-8125(1991).
PubMed ID1896459

5AuthorsCusack S. Haertlein M. Leberman R.
TitleSequence, structural and evolutionary relationships between class 2 aminoacyl-tRNA synthetases.
SourceNucleic Acids Res. 19:3489-3498(1991).
PubMed ID1852601

6AuthorsCusack S.
TitleSequence, structure and evolutionary relationships between class 2 aminoacyl-tRNA synthetases: an update.
SourceBiochimie 75:1077-1081(1993).
PubMed ID8199242

7AuthorsCusack S. Berthet-Colominas C. Haertlein M. Nassar N. Leberman R.
TitleA second class of synthetase structure revealed by X-ray analysis of Escherichia coli seryl-tRNA synthetase at 2.5 A.
SourceNature 347:249-255(1990).
PubMed ID2205803
DOI10.1038/347249a0

8AuthorsDelarue M.
TitleAminoacyl-tRNA synthetases.
SourceCurr. Opin. Struct. Biol. 5:48-55(1995).
PubMed ID7773747

9AuthorsLeveque F. Plateau P. Dessen P. Blanquet S.
TitleHomology of lysS and lysU, the two Escherichia coli genes encoding distinct lysyl-tRNA synthetase species.
SourceNucleic Acids Res. 18:305-312(1990).
PubMed ID2183178

10AuthorsNakatsu T. Kato H. Oda J.
SourceNat. Struct. Biol. 5:15-19(1998).



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