The domain within your query sequence starts at position 142 and ends at position 376; the E-value for the TGT domain shown below is 1.4e-88.

RSVEIQNALGSDIIMQLDHVVSSTVTGPLVEEAMHRSVRWLDRCIAAHKHPDKQNLFAII
QGGLNADLRTTCLKEMTKRDVPGFAIGGLSGGESKAQFWKMVALSTSMLPKDKPRYLMGV
GYATDLVVCVALGCDMFDCVYPTRTARFGSALVPTGNLQLKKKQYAKDFSPINPECPCPT
CQTHSRAFLHALLHSDNTTALHHLTVHNIAYQLQLLSAVRSSILEQRFPDFVRNF

TGT

TGT
PFAM accession number:PF01702
Interpro abstract (IPR002616):

Queuine tRNA-ribosyltransferases, also known as tRNA-guanine transglycosylases (TGT) EC 2.4.2.29, modify tRNAs for asparagine, aspartic acid, histidine and tyrosine with queuine at position 34 and with archaeosine at position 15 in archaeal tRNAs. In bacteria it catalyses the exchange of guanine-34 at the wobble position with 7-aminomethyl-7-deazaguanine (preQ1), and subsequently the addition of a cyclopentenediol moiety to 7-aminomethyl-7-deazaguanine-34 tRNA giving a hypermodified base queuine (Q) in the wobble position [(PUBMED:8654383), (PUBMED:8323579)]. In eukaryotes, TGT catalyzes the irreversible exchange of guanine in the unmodified tRNA with free queuine. Eukaryotes cannot synthesize queuine de novo and must obtain it from the diet or gut flora [(PUBMED:11255023)].

The structure of TGT consists of an irregular (beta/alpha)8 barrel, represented by this entry, and a C-terminal zinc-containing subdomain [(PUBMED:8654383)].

GO process:tRNA modification (GO:0006400)
GO function:transferase activity, transferring pentosyl groups (GO:0016763)

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