ID   TRMB_HELPH              Reviewed;         393 AA.
AC   Q1CTC3;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=HPAG1_0732;
OS   Helicobacter pylori (strain HPAG1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=357544;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HPAG1;
RX   PubMed=16788065; DOI=10.1073/pnas.0603784103;
RA   Oh J.D., Kling-Baeckhed H., Giannakis M., Xu J., Fulton R.S., Fulton L.A.,
RA   Cordum H.S., Wang C., Elliott G., Edwards J., Mardis E.R., Engstrand L.G.,
RA   Gordon J.I.;
RT   "The complete genome sequence of a chronic atrophic gastritis Helicobacter
RT   pylori strain: evolution during disease progression.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:9999-10004(2006).
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; CP000241; ABF84799.1; -; Genomic_DNA.
DR   RefSeq; WP_001119911.1; NC_008086.1.
DR   AlphaFoldDB; Q1CTC3; -.
DR   SMR; Q1CTC3; -.
DR   PRIDE; Q1CTC3; -.
DR   EnsemblBacteria; ABF84799; ABF84799; HPAG1_0732.
DR   KEGG; hpa:HPAG1_0732; -.
DR   HOGENOM; CLU_041532_0_0_7; -.
DR   OMA; FVHFPVP; -.
DR   OrthoDB; 1025521at2; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000008835; 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..393
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000288158"
FT   BINDING         124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         176
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   393 AA;  45707 MW;  CC3EA4912DE0FD2C CRC64;
     MPHFLAKLDF KPLKYPLIEG DFCFHKEFLS LKNPTKSCVY ASFKDRIFLL QKIRRANDFL
     IKSEKTTPLK REILKQALRI YSQSFEVISH NLQENSKHAS GKKALDLGTF EDFIQKNQAP
     ILAEIGFGSG RHLIELAKNN PTKTCLGIEI HTPSIAQALK QIELLDLKNL HILQGDGRLI
     LESMPNYKCE KIFVHFPVPW NEKKHRRVLS EKFLNEALRV LKPRGFLELR TDDGLYFEDS
     LKLALKNFQC EIEIKKNAQI PVISKYEARW NKLKKDIYDL RIYSLELNET PFYNHAFDFS
     FDTITMSEKS VGTILKTKKI IQEGYFVHVC NIYENKGDFL VELSMGDFDW PVRLFVLLTE
     NQIFYLNKSP LKTLNNHKAH LLLQNILSQK GIG