TRMB_CAMJE
ID TRMB_CAMJE Reviewed; 392 AA.
AC Q9PN20; Q0P8X8;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE EC=2.1.1.33 {ECO:0000255|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01057};
GN Name=trmB {ECO:0000255|HAMAP-Rule:MF_01057}; OrderedLocusNames=Cj1278c;
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: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000255|HAMAP-Rule:MF_01057}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-
CC methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:42708, Rhea:RHEA-COMP:10188, Rhea:RHEA-COMP:10189,
CC ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269,
CC ChEBI:CHEBI:74480; EC=2.1.1.33; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01057};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01057}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|HAMAP-Rule:MF_01057}.
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DR EMBL; AL111168; CAL35393.1; -; Genomic_DNA.
DR PIR; H81335; H81335.
DR RefSeq; WP_002858203.1; NC_002163.1.
DR RefSeq; YP_002344669.1; NC_002163.1.
DR AlphaFoldDB; Q9PN20; -.
DR SMR; Q9PN20; -.
DR STRING; 192222.Cj1278c; -.
DR PaxDb; Q9PN20; -.
DR PRIDE; Q9PN20; -.
DR EnsemblBacteria; CAL35393; CAL35393; Cj1278c.
DR GeneID; 905569; -.
DR KEGG; cje:Cj1278c; -.
DR PATRIC; fig|192222.6.peg.1261; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_041532_0_0_7; -.
DR OMA; FVHFPVP; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.150; -; 1.
DR HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR PANTHER; PTHR23417; PTHR23417; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00091; TIGR00091; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..392
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171312"
FT BINDING 123
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 148
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 201
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 231
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 392 AA; 46184 MW; 1EA67D8B6EA4A190 CRC64;
MPNFKSKKIK EINLPYSKDD VEFLWLAKND NVSLIYTKVQ EESFFLQIKK AQNGFVIKGD
KHTKPSKIGY LQKALKIFKE GFCEDIINEA FGLKNNALIE KTPFIVDNFD ELLSRLQGKI
YIEIGFGSGR HLLYQAKENP NVLILGVEIY NPALTQVAKL AKAQNVNNIL LIQSDARLLL
SVLKSKSVEK IFLHFPVPWD KKPHRRVIGK DFCKECARVL VQNGRFELRT DSFEYFNFTL
EQFLTFPAPK FSLRKNENLE ISSKYEDRWK KQEKNIYDLW VWNFNQECKN YELNEFNLSS
VEFSKEDLKK IEQNFKNITI KKDDFFLHFE SIYKQDENLL LKVAFGAFNK PEHCYLHLDK
TIDFAFKEPF KIQENIKAIN ELKEILKVQF KI
