PROSITE documentation PDOC51880 [for PROSITE entry PS51880]
TGS domain profile


The TGS domain, named after the presence in ThrRS, GTPase, and SpoT, is a small domain that consists of ~50 amino acid residues and has nucleic acid binding affinity. It is shared by eukaryotic and some of the bacterial ThrRS, a distinct family of GTPases (the OBG family), and guanosine polyphosphate hydrolase (SpoT) and synthetase (RelA), which are involved in stringent response in bacteria, and uridine kinase from the spirochaete Treponema pallidum (but not any other organisnm, including the related spirochaete Borrelia burgdorferi). The presence of the TGS domain in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role [1,2].

The TGS domain features a six-stranded half-barrel that curves around an α-helix (see <PDB:1JAL>) and belongs to the β-grasp fold superfamily [3,4,5].

The profile we developed covers the entire TGS domain.

Last update:

December 2018 / First entry.


Technical section

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

TGS, PS51880; TGS domain profile  (MATRIX)


1AuthorsWolf Y.I. Aravind L. Grishin N.V. Koonin E.V.
TitleEvolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events.
SourceGenome Res. 9:689-710(1999).
PubMed ID10447505

2AuthorsCheung M.Y. Li X. Miao R. Fong Y.-H. Li K.-P. Yung Y.-L. Yu M.-H. Wong K.-B. Chen Z. Lam H.-M.
TitleATP binding by the P-loop NTPase OsYchF1 (an unconventional G protein) contributes to biotic but not abiotic stress responses.
SourceProc. Natl. Acad. Sci. U. S. A. 113:2648-2653(2016).
PubMed ID26912459

3AuthorsTeplyakov A. Obmolova G. Chu S.Y. Toedt J. Eisenstein E. Howard A.J. Gilliland G.L.
TitleCrystal structure of the YchF protein reveals binding sites for GTP and nucleic acid.
SourceJ. Bacteriol. 185:4031-4037(2003).
PubMed ID12837776

4AuthorsKoller-Eichhorn R. Marquardt T. Gail R. Wittinghofer A. Kostrewa D. Kutay U. Kambach C.
TitleHuman OLA1 defines an ATPase subfamily in the Obg family of GTP-binding proteins.
SourceJ. Biol. Chem. 282:19928-19937(2007).
PubMed ID17430889

5AuthorsIyer L.M. Burroughs A.M. Aravind L.
TitleThe prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains.
SourceGenome Biol. 7:R60-R60(2006).
PubMed ID16859499

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 prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)