ID   TRMD_STRCO              Reviewed;         277 AA.
AC   P0A4P1; O69882;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=SCO5594; ORFNames=SC2E1.11;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RNA methyltransferase TrmD family.
CC       {ECO:0000305}.
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; AL939124; CAA19386.1; -; Genomic_DNA.
DR   PIR; T34779; T34779.
DR   RefSeq; NP_629728.1; NC_003888.3.
DR   RefSeq; WP_003973399.1; NZ_VNID01000034.1.
DR   AlphaFoldDB; P0A4P1; -.
DR   SMR; P0A4P1; -.
DR   STRING; 100226.SCO5594; -.
DR   PRIDE; P0A4P1; -.
DR   GeneID; 1101035; -.
DR   KEGG; sco:SCO5594; -.
DR   PATRIC; fig|100226.15.peg.5686; -.
DR   eggNOG; COG0336; Bacteria.
DR   HOGENOM; CLU_047363_0_0_11; -.
DR   InParanoid; P0A4P1; -.
DR   OMA; ILCGHYK; -.
DR   PhylomeDB; P0A4P1; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0002939; P:tRNA N1-guanine methylation; IBA:GO_Central.
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; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase; tRNA processing.
FT   CHAIN           1..277
FT                   /note="tRNA (guanine-N(1)-)-methyltransferase"
FT                   /id="PRO_0000060477"
FT   BINDING         140..145
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   277 AA;  30828 MW;  61CB740770A3A4C8 CRC64;
     MRLDVVTIFP EYLEPLNVSL VGKARARGQL GVHVHDLRDW TYDRHNTVDD TPYGGGPGMV
     MKTEPWGDAL DSVLADGYET GCGEPALVVP TPSGRPFTQE LAVHLSERPW LIFTPARYEG
     IDRRVVDEYA TRMPVYEVSI GDYVLAGGEA AVLVVTEAVA RLLPGVLGNA ESHRDDSFAP
     GAMANLLEGP VHTKPPQWRG RGIPDVLLSG HHGKIARWRR DEALRRTTAN RPDLIERCDP
     AAFDKKDREM LSILGWQPDP DGEPYGRFWR RTPGMEE