{PDOC51880} {PS51880; TGS} {BEGIN} ********************** * 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 alpha-helix (see ) and belongs to the beta-grasp fold superfamily [3,4,5]. The profile we developed covers the entire TGS domain. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2018 / First entry. [ 1] 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." Genome Res. 9:689-710(1999). PubMed=10447505 [ 2] Cheung 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. "ATP binding by the P-loop NTPase OsYchF1 (an unconventional G protein) contributes to biotic but not abiotic stress responses." Proc. Natl. Acad. Sci. U. S. A. 113:2648-2653(2016). PubMed=26912459; DOI=10.1073/pnas.1522966113 [ 3] Teplyakov A., Obmolova G., Chu S.Y., Toedt J., Eisenstein E., Howard A.J., Gilliland G.L. "Crystal structure of the YchF protein reveals binding sites for GTP and nucleic acid." J. Bacteriol. 185:4031-4037(2003). PubMed=12837776 [ 4] Koller-Eichhorn R., Marquardt T., Gail R., Wittinghofer A., Kostrewa D., Kutay U., Kambach C. "Human OLA1 defines an ATPase subfamily in the Obg family of GTP-binding proteins." J. Biol. Chem. 282:19928-19937(2007). PubMed=17430889; DOI=10.1074/jbc.M700541200 [ 5] Iyer L.M., Burroughs A.M., Aravind L. "The prokaryotic antecedents of the ubiquitin-signaling system and the early evolution of ubiquitin-like beta-grasp domains." Genome Biol. 7:R60-R60(2006). PubMed=16859499; DOI=10.1186/gb-2006-7-7-r60 -------------------------------------------------------------------------------- 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 -------------------------------------------------------------------------------- {END}