The domain within your query sequence starts at position 55 and ends at position 499; the E-value for the TRM domain shown below is 4.9e-149.

VATVTEGAAKIVFPSANEVFYNPVQEFNRDLTCAVITEFARIHLGAKGIQIKVPGEKDSE
KIAVDLSDQEEETAGKNENLAPGDWPRTAAVGEICEEGLRVLEGLAASGLRSIRFALEVP
GLQSVVANDASARAVELMHRNVELNGVAHLVQPNQADARMLMYQHQKAPERFDVIDLDPY
GSPAPFLDAAVQAVSDGGLLCVTCTDMAVLAGNSGETCYSKYGAMALKSRACHEMALRIV
LHSLDLHANCYQRYIVPLLSISADFYIRVFVRVFTGQAKVKSSASKQALVFQCVGCGAFY
LQRLGKASGDPGGRIKFSAACGPPVTPECEHCGQRHQLGGPMWAEPIHDLDFVGRVLDAV
TTNPGRFHTSMRIQGVLSVVTEELPDVPLYYTLDQLSSTIHCNTPRLLQLRSALLHAGFR
VSLSHACKNAVKTDAPPEALWDIMR

TRM

TRM
PFAM accession number:PF02005
Interpro abstract (IPR002905): Trm1 (EC 2.1.1.216) dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups [(PUBMED:9685492), (PUBMED:10438627)]. In Saccharomyces cerevisiae, Trm1 is required for the modification of both mitochondrial and cytoplasmic tRNAs [(PUBMED:2426253)].
GO process:tRNA processing (GO:0008033)
GO function:tRNA (guanine-N2-)-methyltransferase activity (GO:0004809), RNA binding (GO:0003723)

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