TRMB_CAMFF
ID TRMB_CAMFF Reviewed; 395 AA.
AC A0RQ93;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 78.
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};
GN OrderedLocusNames=CFF8240_1218;
OS Campylobacter fetus subsp. fetus (strain 82-40).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=360106;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=82-40;
RA Fouts D.E., Nelson K.E.;
RT "Sequence of Campylobacter fetus subsp. fetus 82-40.";
RL Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000487; ABK82983.1; -; Genomic_DNA.
DR RefSeq; WP_002849909.1; NC_008599.1.
DR AlphaFoldDB; A0RQ93; -.
DR SMR; A0RQ93; -.
DR STRING; 360106.CFF8240_1218; -.
DR EnsemblBacteria; ABK82983; ABK82983; CFF8240_1218.
DR GeneID; 61065043; -.
DR KEGG; cff:CFF8240_1218; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_041532_0_0_7; -.
DR OMA; FVHFPVP; -.
DR OrthoDB; 1025521at2; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000000760; 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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..395
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000288132"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 151
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 204
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 234
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 395 AA; 45516 MW; B46D6A5ACF835BD2 CRC64;
MPNFVATSLK NLKFPFGADG VEFLWSAKAG DESLIYTKTG KKEFFLLVKD KKTEFVVKSD
KLTRPASLGT IQKALSVYKD LNVLDLKSST IAIKNEKQLA KKEFILNDIQ FLEKLKSGEF
KKIFVEIGFG SGRHLLYQAK TDENTLVVGI EVYKRSCEQV NNLALSMGLK NVILLNLDAR
LVMSLLHSNS VDRLFLHFPV PWEKSEKRRV VSAEFANECQ RVLKSGGSFE LRSDDKNYTD
FTISCFLNLK EAKMEIYKNR FLDVSSKYED RWIKQNRDIY DVVFTNLIVS EQKVLHGDFE
FGTVLEEDIL SKFENKTIKK DDYFIHMERI YKKDSSEKNG GLLLRVAFGS FYRPEHCFIL
VENSKASYFI KKPLLTYENL KAHSTLKEYL SCSTS