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