ID   TRMD_DESVH              Reviewed;         425 AA.
AC   Q72DU3;
DT   10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=tRNA (guanine-N(1)-)-methyltransferase;
DE            EC=2.1.1.228;
DE   AltName: Full=M1G-methyltransferase;
DE   AltName: Full=tRNA [GM37] methyltransferase;
GN   Name=trmD; OrderedLocusNames=DVU_0836;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
CC   -!- FUNCTION: Specifically methylates guanosine-37 in various tRNAs.
CC       {ECO:0000250}.
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q72DU3; Q72FB7: DVU_0297; NbExp=2; IntAct=EBI-10069213, EBI-10070463;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000305}.
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DR   EMBL; AE017285; AAS95316.1; -; Genomic_DNA.
DR   RefSeq; WP_010938137.1; NZ_CABHLV010000001.1.
DR   RefSeq; YP_010057.1; NC_002937.3.
DR   AlphaFoldDB; Q72DU3; -.
DR   SMR; Q72DU3; -.
DR   IntAct; Q72DU3; 2.
DR   STRING; 882.DVU_0836; -.
DR   PaxDb; Q72DU3; -.
DR   EnsemblBacteria; AAS95316; AAS95316; DVU_0836.
DR   KEGG; dvu:DVU_0836; -.
DR   PATRIC; fig|882.5.peg.782; -.
DR   eggNOG; COG0336; Bacteria.
DR   eggNOG; COG4752; Bacteria.
DR   HOGENOM; CLU_047363_2_0_7; -.
DR   OMA; NMDLHDI; -.
DR   PhylomeDB; Q72DU3; -.
DR   Proteomes; UP000002194; Chromosome.
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; cd18085; TM1570-like; 1.
DR   CDD; cd18080; TrmD-like; 1.
DR   Gene3D; 1.10.1270.20; -; 1.
DR   Gene3D; 3.40.1280.10; -; 2.
DR   HAMAP; MF_00605; TrmD; 1.
DR   InterPro; IPR029028; Alpha/beta_knot_MTases.
DR   InterPro; IPR019230; RNA_MeTrfase_C_dom.
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; PF09936; Methyltrn_RNA_4; 1.
DR   Pfam; PF01746; tRNA_m1G_MT; 1.
DR   SUPFAM; SSF75217; SSF75217; 1.
DR   TIGRFAMs; TIGR00088; trmD; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..425
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_0000060370"
FT   REGION          1..241
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT   REGION          242..425
FT                   /note="Unknown"
FT   BINDING         109
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         129..134
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   425 AA;  46629 MW;  76F514836570A9BC CRC64;
     MRCTILTLFP EFFDSPLDAG LMGKARESGL IDVALVNPRA YTTDRHSTVD DRPYGGGPGM
     VMRVEPWEKA LQGIEEPGRI LMMAPKGRPF TQAMARELAQ EESLTILCGR YEGFDARLEE
     IYPIEAVSMG DFVLNGGETA ALAVLEAVSR LVPGFMGKEE SGTEESFSAG LLEYPHYTRP
     EDYAGHVVPE VLRSGDHGRI AAWRKECSLR LTLSQRPDIL PEAQLDEADM DFLRGLSRNR
     PGRNLYCALV HYPVVLKEKN SGATSLTNLD IHDIGRSSCT YGLGGFYVTT PLEDQRRLLD
     TLLRHWTLGP GSRSNPDRAE ALGRIKGVDD VRAAIEDIAR RTGQVPYVVG TSAKGAGNAT
     PASVRAMLEE RPVLLVFGTG HGLAPEVLEG CDAILRPLRW MDGYNHLSVR AAAAIIMDRL
     LGDCY