ID   TRM1_METMI              Reviewed;         373 AA.
AC   P0CW64; Q9HH73;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 39.
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}; Synonyms=trmI;
OS   Methanococcus maripaludis (Methanococcus deltae).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=39152;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43000 / DSM 2067 / JCM 10722 / JJ;
RA   Graham D.E., Yu J.P., Whitman W.B., Olsen G.J.;
RT   "Genetic characterization of trmI in Methanococcus maripaludis JJ.";
RL   Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
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; AF298223; AAG37224.1; -; Genomic_DNA.
DR   RefSeq; WP_011170172.1; NC_005791.1.
DR   AlphaFoldDB; P0CW64; -.
DR   SMR; P0CW64; -.
DR   GeneID; 2762025; -.
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; RNA-binding; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing; tRNA-binding.
FT   CHAIN           1..373
FT                   /note="tRNA (guanine(26)-N(2))-dimethyltransferase"
FT                   /id="PRO_0000147685"
FT   DOMAIN          2..365
FT                   /note="Trm1 methyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00290"
SQ   SEQUENCE   373 AA;  41820 MW;  5CF5D79F5A905058 CRC64;
     MKIISEGETK LMVPEESTLS KKDTVFYNPV METNRDISVS VVQSFLDDFK RDEFLMCDPL
     GGSGARGIRY AKELKFNGDL KVSIGDINPS AVKMIKENLK LNELENVEVF HEDANVLLSK
     NFKVFNVVDL DPFGSPVPYL DSGIRASLTK GGLLCMTATD TAVLCGAYRK TCIRKYNAVP
     LKGDKELAVR LMIGYAVKMA SKYDIGLKPI FSHVTDHYAR TFMVTERGAG KADSAIENLG
     YIRQDSEQKS FKTFEEGSEK GYAGPFYLGE ISDKNIVQNA LNTAKTRNYS KRAVNILEMI
     SRESEINQVG CFDIHELCSF IKKLVPPVND IMENLKENGF KVTRVHYNPY GLKTDAELSD
     LVVLISEYHS KKY