ID   TRMD_CUPPJ              Reviewed;         260 AA.
AC   Q46Y84;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
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}; OrderedLocusNames=Reut_A2538;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(2010).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000090; AAZ61899.1; -; Genomic_DNA.
DR   RefSeq; WP_011298687.1; NC_007347.1.
DR   AlphaFoldDB; Q46Y84; -.
DR   SMR; Q46Y84; -.
DR   STRING; 264198.Reut_A2538; -.
DR   EnsemblBacteria; AAZ61899; AAZ61899; Reut_A2538.
DR   KEGG; reu:Reut_A2538; -.
DR   eggNOG; COG0336; Bacteria.
DR   HOGENOM; CLU_047363_0_2_4; -.
DR   OMA; ILCGHYK; -.
DR   OrthoDB; 525632at2; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC.
DR   CDD; cd18080; TrmD-like; 1.
DR   Gene3D; 1.10.1270.20; -; 1.
DR   Gene3D; 3.40.1280.10; -; 1.
DR   HAMAP; MF_00605; TrmD; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR002649; tRNA_m1G_MeTrfase_bac.
DR   InterPro; IPR023148; tRNA_m1G_MeTrfase_C_sf.
DR   InterPro; IPR029026; tRNA_m1G_MTases_N.
DR   InterPro; IPR016009; tRNA_MeTrfase_TRMD/TRM10.
DR   PANTHER; PTHR46417; PTHR46417; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   PIRSF; PIRSF000386; tRNA_mtase; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00088; trmD; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW   tRNA processing.
FT   CHAIN           1..260
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_0000257453"
FT   BINDING         117
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT   BINDING         137..142
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
SQ   SEQUENCE   260 AA;  29051 MW;  2666526C9DD7C78E CRC64;
     MQFDVITLFP EMFRALTDWG ITSRAAKQQR YALRTWNPRD FTTDNYRTID DRPYGGGPGM
     VMLPRPLDDA IDAASAAQSQ AGVDTPHVVL MSPQGATLTH EKVMSLAQRP GLVLLCGRYE
     AIDQRLIDRR VHEEISLGDF VLSGGELPAM ALIDAVVRHL PGVLGDAQSA VQDSFVNGLL
     DCPHYTRPEE YEGVRVPEIL LGGHHAEIEK WRRQQALANT ARKRPDLIEA ARKQGLLTRA
     DEKFLSEWLV KEGREMSPAR