ID   TRMB_HELHP              Reviewed;         396 AA.
AC   Q7VI24;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=HH_0785;
OS   Helicobacter hepaticus (strain ATCC 51449 / 3B1).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=235279;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51449 / 3B1;
RX   PubMed=12810954; DOI=10.1073/pnas.1332093100;
RA   Suerbaum S., Josenhans C., Sterzenbach T., Drescher B., Brandt P., Bell M.,
RA   Droege M., Fartmann B., Fischer H.-P., Ge Z., Hoerster A., Holland R.,
RA   Klein K., Koenig J., Macko L., Mendz G.L., Nyakatura G., Schauer D.B.,
RA   Shen Z., Weber J., Frosch M., Fox J.G.;
RT   "The complete genome sequence of the carcinogenic bacterium Helicobacter
RT   hepaticus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7901-7906(2003).
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; AE017125; AAP77382.1; -; Genomic_DNA.
DR   RefSeq; WP_011115627.1; NC_004917.1.
DR   AlphaFoldDB; Q7VI24; -.
DR   SMR; Q7VI24; -.
DR   STRING; 235279.HH_0785; -.
DR   EnsemblBacteria; AAP77382; AAP77382; HH_0785.
DR   KEGG; hhe:HH_0785; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_041532_0_0_7; -.
DR   OMA; FVHFPVP; -.
DR   OrthoDB; 1025521at2; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000002495; 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..396
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000171334"
FT   BINDING         125
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         150
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         177
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         203
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   396 AA;  46253 MW;  76C6FB9B861941EF CRC64;
     MPHFLASHIT LPPMPFTQEG YTFVYEAKQC NDSSQSLILV RYEDNEFFLR KAWRGNKNNA
     ILKCEKSTKT QPTGIIKNAL KILCAYQKNV ISHNLNKNTP RQNLQSPYFQ SMDFFLDFAK
     PCLIEIGFGS GRHLLHLAQS NPHFMCIGIE IHTPSIEQIL RQVQLLGLEN LYIINGDARI
     LLEILSSHIA QGIYVHFPVP WNKKHHRRIF SPKFFQESLR VLDNNGVLHL RSDDEIYFQD
     ALSLALQQES ISLEIHKNQQ EVITSKYEAR WKKQQKNIYD LKIFHTYKNT NNEKNVKNTQ
     KNFYFDKILR KNLDNYKNFP HKKIANDWFL HIDNLYCAGD IYVLALCFGD FNQPQSKFLQ
     IEFCNNVSAR YIGSNPIPTQ AAIKAHKYLI QILTQE