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
The profile we developed covers the entire TGS domain.
December 2018 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Wolf Y.I. Aravind L. Grishin N.V. Koonin E.V.
Evolution of aminoacyl-tRNA synthetases--analysis of unique domain architectures and phylogenetic trees reveals a complex history of horizontal gene transfer events.
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