TRMD_CAMJE
ID TRMD_CAMJE Reviewed; 234 AA.
AC Q9PPJ4; Q0PAG6;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 107.
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=Cj0713;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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; AL111168; CAL34850.1; -; Genomic_DNA.
DR PIR; D81342; D81342.
DR RefSeq; WP_002868040.1; NC_002163.1.
DR RefSeq; YP_002344131.1; NC_002163.1.
DR AlphaFoldDB; Q9PPJ4; -.
DR SMR; Q9PPJ4; -.
DR IntAct; Q9PPJ4; 35.
DR STRING; 192222.Cj0713; -.
DR PaxDb; Q9PPJ4; -.
DR PRIDE; Q9PPJ4; -.
DR EnsemblBacteria; CAL34850; CAL34850; Cj0713.
DR GeneID; 904477; -.
DR KEGG; cje:Cj0713; -.
DR PATRIC; fig|192222.6.peg.705; -.
DR eggNOG; COG0336; Bacteria.
DR HOGENOM; CLU_047363_0_1_7; -.
DR OMA; ILCGHYK; -.
DR Proteomes; UP000000799; 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_0000060350"
FT BINDING 112
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 132..137
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 234 AA; 27110 MW; 6A69B63BDEC8EF6C CRC64;
MKFSFVSLFP NLMEFYFQDS ILARAKEKKL FKLNFYNPRD FSKNSYHKVD DYKIGGGAGL
LMQAEPMYEV LRSIQEKKEN PYFIFLNPSG KTFNQKDAKR LSKKEHIVFV CGRYEGIDER
VLEIFANEVF SIGDFILTGG ELPALVMCDA ILRNVNGVLG NMESLEEESF ENNLLEAPAF
SKPFIFEKKN KKFYTPSEFL KGNHARIASL KTTLASCKTK FFRPDLFLEH ERKK