ID   TRM1_METB6              Reviewed;         374 AA.
AC   A7I9E9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 79.
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=Mboo_1845;
OS   Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX   NCBI_TaxID=456442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX   PubMed=25998264; DOI=10.1099/mic.0.000117;
RA   Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA   Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT   "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT   peatland environments.";
RL   Microbiology 161:1572-1581(2015).
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; CP000780; ABS56360.1; -; Genomic_DNA.
DR   RefSeq; WP_012107411.1; NC_009712.1.
DR   AlphaFoldDB; A7I9E9; -.
DR   SMR; A7I9E9; -.
DR   STRING; 456442.Mboo_1845; -.
DR   PRIDE; A7I9E9; -.
DR   EnsemblBacteria; ABS56360; ABS56360; Mboo_1845.
DR   GeneID; 5410649; -.
DR   KEGG; mbn:Mboo_1845; -.
DR   eggNOG; arCOG01219; Archaea.
DR   HOGENOM; CLU_010862_5_1_2; -.
DR   OMA; VFYNPVM; -.
DR   OrthoDB; 70865at2157; -.
DR   Proteomes; UP000002408; 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..374
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_1000197036"
FT   DOMAIN          4..368
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ   SEQUENCE   374 AA;  40934 MW;  90693150DA475C1F CRC64;
     MDVIEATEGT TTFLVPVQDS TGQFPPGTAP VFFNRRMELN RDATVLLLSV LQPSDYLDAM
     GATGVRGLRV AHEVGIPVTI NDRDPEAIPL IRENVARLGL PVTVTCRDAC SLLFEQAFDA
     VDIDPFGTPA PFTDAGIRGT RRFLLLTATD TAPLCGAHLK AGIRRYFARP GNTGYHGEVG
     LRILLGFVAR ETVKYDRGIE PLFCFAREHF VRLNLRLTRG PKAADRTIER LGFILQCPTC
     AYREELPGMF PPAATCPFCG KPLRPIGPLF LGAISSDEIL GQMQARLPSC GLGTQKELEK
     LLTTCREELP TSSHYDYHRV AQQLVVSPPK IETLLEALRS AGFDASRTHY SGTGVKTNAP
     LPVLYDAIRG KNEP