ID   TMG10_METTL             Reviewed;         162 AA.
AC   P05409;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1988, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=Probable tRNA (guanine(10)-N2)-dimethyltransferase;
DE            EC=2.1.1.213;
DE   AltName: Full=tRNA:G10 dimethyltransferase;
DE   Flags: Fragment;
GN   Name=trmG10;
OS   Methanothermococcus thermolithotrophicus (Methanococcus
OS   thermolithotrophicus).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanothermococcus.
OX   NCBI_TaxID=2186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2838639; DOI=10.1007/bf02099731;
RA   Souillard N., Magot M., Possot O., Sibold L.;
RT   "Nucleotide sequence of regions homologous to nifH (nitrogenase Fe protein)
RT   from the nitrogen-fixing archaebacteria Methanococcus thermolithotrophicus
RT   and Methanobacterium ivanovii: evolutionary implications.";
RL   J. Mol. Evol. 27:65-76(1988).
CC   -!- FUNCTION: Catalyzes the adenosylmethionine-dependent methylation of the
CC       exocyclic amino group (N(2)) of guanosine at position 10 of various
CC       tRNAs. Acts via a two-step process that leads to the formation of
CC       either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G) (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(10) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) +
CC         N(2)-dimethylguanosine(10) in tRNA + 2 S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:43124, Rhea:RHEA-COMP:10355, Rhea:RHEA-COMP:10358,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=2.1.1.213;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily. Trm-G10
CC       family. {ECO:0000305}.
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DR   EMBL; X07500; CAA30380.1; -; Genomic_DNA.
DR   PIR; S00737; S00737.
DR   AlphaFoldDB; P05409; -.
DR   SMR; P05409; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001510; P:RNA methylation; IEA:UniProt.
DR   GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR000241; RNA_methylase_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF01170; UPF0020; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   PROSITE; PS01261; UPF0020; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; RNA-binding; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           <1..162
FT                   /note="Probable tRNA (guanine(10)-N2)-dimethyltransferase"
FT                   /id="PRO_0000140483"
FT   NON_TER         1
SQ   SEQUENCE   162 AA;  18186 MW;  08EE977BE7F5622E CRC64;
     KLAMCLVNLS RLKKGDVLLD PFCGTGGFLI EGGFMGLKLI GSDIDDDMVN GTLLNLKSYN
     LTEHIISIKK WNAGDIKSFL KQLNVKYVDG IVTDPPYGIS TSAKGNIEEI FNNLGDVLKK
     DGYLVFASSR KINLDLELME MYELYIHKSL TRYIHVYKKT DN