TRMD_MYCGA
ID TRMD_MYCGA Reviewed; 234 AA.
AC Q9RDV3;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 15-AUG-2003, sequence version 2.
DT 03-AUG-2022, entry version 118.
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=MYCGA6250; ORFNames=MGA_0439;
OS Mycoplasma gallisepticum (strain R(low / passage 15 / clone 2))
OS (Mycoplasmoides gallisepticum).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=710127;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A5969Var.B;
RX PubMed=11959450; DOI=10.1111/j.1574-6968.2002.tb11095.x;
RA Skamrov A.V., Feoktistova E.S., Gol'dman M.A., Bibilashvili R.S.;
RT "Mycoplasma gallisepticum rpoA gene cluster.";
RL FEMS Microbiol. Lett. 208:281-285(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R(low / passage 15 / clone 2);
RX PubMed=12949158; DOI=10.1099/mic.0.26427-0;
RA Papazisi L., Gorton T.S., Kutish G., Markham P.F., Browning G.F.,
RA Nguyen D.K., Swartzell S., Madan A., Mahairas G., Geary S.J.;
RT "The complete genome sequence of the avian pathogen Mycoplasma
RT gallisepticum strain R(low).";
RL Microbiology 149:2307-2316(2003).
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; L35043; AAF19036.1; -; Genomic_DNA.
DR EMBL; AE015450; AAP56975.1; -; Genomic_DNA.
DR RefSeq; WP_011113884.1; NC_004829.2.
DR AlphaFoldDB; Q9RDV3; -.
DR SMR; Q9RDV3; -.
DR KEGG; mga:MGA_0439; -.
DR PATRIC; fig|233150.7.peg.702; -.
DR HOGENOM; CLU_047363_0_1_14; -.
DR OMA; ILCGHYK; -.
DR OrthoDB; 525632at2; -.
DR Proteomes; UP000001418; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..234
FT /note="tRNA (guanine-N(1)-)-methyltransferase"
FT /id="PRO_0000060411"
FT BINDING 117
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 136..141
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT CONFLICT 23
FT /note="K -> R (in Ref. 1; AAF19036)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="P -> S (in Ref. 1; AAF19036)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="L -> I (in Ref. 1; AAF19036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 234 AA; 26682 MW; ED3707D15E1A0BCD CRC64;
MKIVVLTLFD DFVRSYYDFS IIKNALDKKA VELEVINFRQ YANDKHKTVD DTIYGGSAGM
LLKLEPLVNC LRDIKQNQFK DPNKIRTYLL SPQGEVYDQN KAVALSQSDH DLILIAGRYE
GFDERIYHYV DGALSVGDFV ITGGELAALI VVDSIVRLLP NVINKDSLSS ESFNNYLLDY
PMYTKPYDFE GYKVPDVLLS GNHQAIAAFN QQEAINNTKM KRPDLYLKYK SNLK
