The domain within your query sequence starts at position 292 and ends at position 366; the E-value for the TGS domain shown below is 7.3e-28.

VRIYTKPKGQLPDYTSPVVLPYSRTTVEDFCMKIHKNLIKEFKYALVWGLSVKHNPQKVG
KDHTLEDEDVIQIVK

TGS

TGS
PFAM accession number:PF02824
Interpro abstract (IPR004095):

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) [ (PUBMED:10447505) (PUBMED: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 [ (PUBMED: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 alpha-helix and belongs to the beta-grasp fold superfamily [ (PUBMED:12837776) (PUBMED:17430889) (PUBMED:16859499) ]. There is no direct information on the functions of the TGS domain, but its presence in two types of regulatory proteins (the GTPases and guanosine polyphosphate phosphohydrolases/synthetases) suggests a ligand (most likely nucleotide)-binding, regulatory role [ (PUBMED:10447505) (PUBMED:26912459) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry TGS