TRMD_RICCN
ID TRMD_RICCN Reviewed; 234 AA.
AC Q92JB6;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=RC0151;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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}.
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DR EMBL; AE006914; AAL02689.1; -; Genomic_DNA.
DR PIR; G97718; G97718.
DR RefSeq; WP_010976828.1; NC_003103.1.
DR AlphaFoldDB; Q92JB6; -.
DR SMR; Q92JB6; -.
DR EnsemblBacteria; AAL02689; AAL02689; RC0151.
DR KEGG; rco:RC0151; -.
DR PATRIC; fig|272944.4.peg.179; -.
DR HOGENOM; CLU_047363_0_1_5; -.
DR OMA; ILCGHYK; -.
DR Proteomes; UP000000816; 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 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW tRNA processing.
FT CHAIN 1..234
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060443"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 135..140
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 234 AA; 26354 MW; F5BB0EED7888BB79 CRC64;
MSILHATILT VFPEMFPGTL GHSLAGQALN KNIWSYDVIN IRDFGLTKHK NIDDEAYGGG
NGLIMRPDVL GSSIDHALAL NPNAEMYYPS PRGRVFTQSF AKEMLKNKNL IFLCGRYEGI
DERVIEEYNV KEISVGDYIL SGGEIPTLTI LDCLIRLLPG VLMNQNTLSS ESFEEDGEFK
GGLECSLYTR PEIWRGRAVP SVLLSGNHRL INEWKKEQSH MITKLRRPEL LKDL
