ID   TRMD_DEIGD              Reviewed;         265 AA.
AC   Q1IYA3;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
DE            EC=2.1.1.228 {ECO:0000255|HAMAP-Rule:MF_00605};
DE   AltName: Full=M1G-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
DE   AltName: Full=tRNA [GM37] methyltransferase {ECO:0000255|HAMAP-Rule:MF_00605};
GN   Name=trmD {ECO:0000255|HAMAP-Rule:MF_00605};
GN   OrderedLocusNames=Dgeo_1486;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000255|HAMAP-Rule:MF_00605}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-
CC         methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:36899, Rhea:RHEA-COMP:10145, Rhea:RHEA-COMP:10147,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:73542, ChEBI:CHEBI:74269; EC=2.1.1.228;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00605};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00605}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00605}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000255|HAMAP-Rule:MF_00605}.
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DR   EMBL; CP000359; ABF45781.1; -; Genomic_DNA.
DR   RefSeq; WP_011530615.1; NC_008025.1.
DR   AlphaFoldDB; Q1IYA3; -.
DR   SMR; Q1IYA3; -.
DR   STRING; 319795.Dgeo_1486; -.
DR   KEGG; dge:Dgeo_1486; -.
DR   eggNOG; COG0336; Bacteria.
DR   HOGENOM; CLU_047363_0_1_0; -.
DR   Proteomes; UP000002431; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N1)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd18080; TrmD-like; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   Gene3D; 1.10.1270.20; tRNA(m1g37)methyltransferase, domain 2; 1.
DR   HAMAP; MF_00605; TrmD; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR   InterPro; IPR002649; tRNA_m1G_MeTrfase_TrmD.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   NCBIfam; TIGR00088; trmD; 1.
DR   PANTHER; PTHR46417; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR46417:SF1; TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   PIRSF; PIRSF000386; tRNA_mtase; 1.
DR   SUPFAM; SSF75217; alpha/beta knot; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..265
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_0000257413"
FT   REGION          243..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        245..265
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         110
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT   BINDING         129..134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
SQ   SEQUENCE   265 AA;  28752 MW;  CAE80C3A93B89808 CRC64;
     MLTFSFLTLF PELLAPFASE ALVGKARARG LLDVQLVNMR DFAENKHLKV DDTPYGGGAG
     MVIRVDVVER ALASLPPADE VILLTPAGER FTQQMAEELS RTTHLAFLCG RYEGFDARVE
     RLATRELSLG DFVMMGGEAA AACVLEAVAR LVPGVLGDED SHRADSFSSG LLDYPEYTRP
     AEWRGEGVPE VLKGGNHAAV ARWRREQALA RTLARRPDLL PSAGLTPQDS AYLLTLGVTP
     EQLAAWGAPP PPLPKRRRGA KPNPN
//