TGS
IPR004095
Definition
The TGS domain (named for its presence ThrRS, GTPase, and SpoT) is present in a number of enzymes, for example, in threonyl-tRNA synthetase (ThrRS), a distinct family of GTPases (the OBG family), and guanosine-3',5'-bis(diphosphate) 3'-pyrophosphohydrolase (SpoT) [[cite:PMID:10447505], [cite:PMID:26912459]] and synthetase (RelA) which are involved in stringent response in bacteria. The TGS domain is also present at the N-terminal of the uridine kinase from the spirochaete Treponema pallidum PMID:10678983 (but not any other organism, including the related spirochaete Borrelia burgdorferi). TGS is a small domain that consists of ~50 amino acid residues and has nucleic acid binding affinity. It is arranged in a six-stranded half-barrel that curves around an α-helix and belongs to the β-grasp fold superfamily [[cite:PMID:12837776], [cite:PMID:17430889], [cite:PMID:16859499]]. The function of the TGS domain of SpoT is in transcription of survival and virulence genes in response to environmental stress PMID:27279228.
7 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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