TRMD_STAAR
ID TRMD_STAAR Reviewed; 245 AA.
AC Q6GHJ5;
DT 10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=SAR1216;
OS Staphylococcus aureus (strain MRSA252).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282458;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MRSA252;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40218.1; -; Genomic_DNA.
DR RefSeq; WP_000687323.1; NC_002952.2.
DR PDB; 3KY7; X-ray; 2.35 A; A=1-245.
DR PDBsum; 3KY7; -.
DR AlphaFoldDB; Q6GHJ5; -.
DR SMR; Q6GHJ5; -.
DR KEGG; sar:SAR1216; -.
DR HOGENOM; CLU_047363_0_1_9; -.
DR OMA; ILCGHYK; -.
DR OrthoDB; 525632at2; -.
DR EvolutionaryTrace; Q6GHJ5; -.
DR Proteomes; UP000000596; 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; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Methyltransferase; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..245
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060457"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 131..136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 10..13
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 14..19
FT /evidence="ECO:0007829|PDB:3KY7"
FT TURN 20..22
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 23..27
FT /evidence="ECO:0007829|PDB:3KY7"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 38..41
FT /evidence="ECO:0007829|PDB:3KY7"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 64..73
FT /evidence="ECO:0007829|PDB:3KY7"
FT STRAND 80..85
FT /evidence="ECO:0007829|PDB:3KY7"
FT STRAND 87..91
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 94..100
FT /evidence="ECO:0007829|PDB:3KY7"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 118..123
FT /evidence="ECO:0007829|PDB:3KY7"
FT STRAND 127..134
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 140..151
FT /evidence="ECO:0007829|PDB:3KY7"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 192..195
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 199..217
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 219..223
FT /evidence="ECO:0007829|PDB:3KY7"
FT HELIX 229..242
FT /evidence="ECO:0007829|PDB:3KY7"
SQ SEQUENCE 245 AA; 28026 MW; F0C28BD78E7FF696 CRC64;
MKIDYLTLFP EMFDGVLNHS IMKRAQENNK LQINTVNFRD YAINKHNQVD DYPYGGGQGM
VLKPEPVFNA MEDLDVTEQA RVILMCPQGE PFSHQKAVEL SKADHIVFIC GHYEGYDERI
RTHLVTDEIS MGDYVLTGGE LPAMTMTDAI VRLIPGVLGN EQSHQDDSFS DGLLEFPQYT
RPREFKGLTV PDVLLSGNHA NIDAWRHEQK LIRTYNKRPD LIEKYPLTNA DKQILERYKI
GLKKG
