ID   TRM1_METST              Reviewed;         390 AA.
AC   Q2NI56;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE            EC=2.1.1.216 {ECO:0000255|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
DE   AltName: Full=tRNA(m(2,2)G26)dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290};
GN   Name=trm1 {ECO:0000255|HAMAP-Rule:MF_00290}; OrderedLocusNames=Msp_0291;
OS   Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 /
OS   MCB-3).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanosphaera.
OX   NCBI_TaxID=339860;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3;
RX   PubMed=16385054; DOI=10.1128/jb.188.2.642-658.2006;
RA   Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R.,
RA   Gottschalk G., Thauer R.K.;
RT   "The genome sequence of Methanosphaera stadtmanae reveals why this human
RT   intestinal archaeon is restricted to methanol and H2 for methane formation
RT   and ATP synthesis.";
RL   J. Bacteriol. 188:642-658(2006).
CC   -!- FUNCTION: Dimethylates a single guanine residue at position 26 of a
CC       number of tRNAs using S-adenosyl-L-methionine as donor of the methyl
CC       groups. {ECO:0000255|HAMAP-Rule:MF_00290}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.216;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00290};
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. Trm1 family. {ECO:0000255|HAMAP-Rule:MF_00290}.
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DR   EMBL; CP000102; ABC56701.1; -; Genomic_DNA.
DR   RefSeq; WP_011405901.1; NC_007681.1.
DR   AlphaFoldDB; Q2NI56; -.
DR   SMR; Q2NI56; -.
DR   STRING; 339860.Msp_0291; -.
DR   PRIDE; Q2NI56; -.
DR   EnsemblBacteria; ABC56701; ABC56701; Msp_0291.
DR   GeneID; 41324864; -.
DR   KEGG; mst:Msp_0291; -.
DR   eggNOG; arCOG01219; Archaea.
DR   HOGENOM; CLU_010862_5_1_2; -.
DR   OMA; VFYNPVM; -.
DR   OrthoDB; 70865at2157; -.
DR   Proteomes; UP000001931; Chromosome.
DR   GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.56.70; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00290; tRNA_dimethyltr_TRM1; 1.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR002905; Trm1.
DR   InterPro; IPR022923; TRM1_arc_bac.
DR   InterPro; IPR042296; tRNA_met_Trm1_C.
DR   PANTHER; PTHR10631; PTHR10631; 1.
DR   Pfam; PF02005; TRM; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00308; TRM1; 1.
DR   PROSITE; PS51626; SAM_MT_TRM1; 1.
PE   3: Inferred from homology;
KW   Methyltransferase; Reference proteome; RNA-binding;
KW   S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..390
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_0000259376"
FT   DOMAIN          4..378
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ   SEQUENCE   390 AA;  44038 MW;  46E86601C5ED2FB9 CRC64;
     MDTHIIEEGL VKIEVPDFEK VSAKAPVFYN PVMEMNRDIS VAVINQYRKE VDHDISICDA
     FGGTGIRGAR YSKEIHGVEK VVVGDVNPLA VEISKKNMQL NNISNVEVQK NDANILLQSN
     KGLFDVVDID PFGTPAMFTQ STAANIRPGG LICISATDTS ALCGTYHDPC LRKYGAKPLK
     TEYCHENGIR ILIAFISRNL AVNQKYLHVL FSHSTEHYMR VYAIVKRGGK KTNKALDNIG
     FIAHCPNCLH RETTYGFAPK IPHTCPECGG EYDVAGPLWL GKIWDKEFIY NTMELVKNLN
     LNKKDDLMSL FEKCYMEADG PVTFYDIHKI CKKLKISSPK INDVMDEIRN RGYFISRTHF
     KLTGMRTDMP LDELKQLILD IKEDKLGPEK