TRMD_BIFAA
ID TRMD_BIFAA Reviewed; 306 AA.
AC A0ZZV4;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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=BAD_0206;
OS Bifidobacterium adolescentis (strain ATCC 15703 / DSM 20083 / NCTC 11814 /
OS E194a).
OC Bacteria; Actinobacteria; Bifidobacteriales; Bifidobacteriaceae;
OC Bifidobacterium.
OX NCBI_TaxID=367928;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15703 / DSM 20083 / NCTC 11814 / E194a;
RA Suzuki T., Tsuda Y., Kanou N., Inoue T., Kumazaki K., Nagano S., Hirai S.,
RA Tanaka K., Watanabe K.;
RT "Bifidobacterium adolescentis complete genome sequence.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; AP009256; BAF38987.1; -; Genomic_DNA.
DR RefSeq; WP_011742733.1; NC_008618.1.
DR AlphaFoldDB; A0ZZV4; -.
DR SMR; A0ZZV4; -.
DR STRING; 1680.BADO_0214; -.
DR EnsemblBacteria; BAF38987; BAF38987; BAD_0206.
DR KEGG; bad:BAD_0206; -.
DR HOGENOM; CLU_047363_0_0_11; -.
DR OMA; ILCGHYK; -.
DR Proteomes; UP000008702; 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; -; 2.
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; 2.
DR Pfam; PF01746; tRNA_m1G_MT; 2.
DR SUPFAM; SSF75217; SSF75217; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..306
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_1000006453"
FT BINDING 157
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
FT BINDING 182..187
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00605"
SQ SEQUENCE 306 AA; 33553 MW; 2CD3E78B7D3087D6 CRC64;
MKIDIVSVFP EYFEVLNLSL LGKAQEKGLV EVTAHNLRDW THDVHHSVDD TPVGGGAGMV
MKPEVWSECL DELLHLEPTT VTCDSMVTCD STADADDTAS ADAAEPAESA TEIAANADTV
PATDRPVLIF PNPSAPLFTQ QDATELSHAN HLLFGCGRYE GYDARIPQYY RAQGVDVREY
SIGDYVLNGG EVAVSVMLEA ITRLLPGFMG NAASIVEESY TGENALLEHR QYTKPADWRG
IKVPDVLLSG DHAKVDRFRR DEALAKTNEL RPDLIEALDC SKLDKADRKT LMALGWEVSG
AHPRQR
