ID   TRMB_MESFL              Reviewed;         223 AA.
AC   Q6F1P8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, 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=Mfl218;
OS   Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
OS   (Acholeplasma florum).
OC   Bacteria; Tenericutes; Mollicutes; Entomoplasmatales; Entomoplasmataceae;
OC   Mesoplasma.
OX   NCBI_TaxID=265311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33453 / NBRC 100688 / NCTC 11704 / L1;
RA   Birren B.W., Stange-Thomann N., Hafez N., DeCaprio D., Fisher S.,
RA   Butler J., Elkins T., Kodira C.D., Major J., Wang S., Nicol R., Nusbaum C.;
RL   Submitted (JUN-2004) 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; AE017263; AAT75575.1; -; Genomic_DNA.
DR   RefSeq; WP_011183115.1; NC_006055.1.
DR   RefSeq; YP_053459.1; NC_006055.1.
DR   AlphaFoldDB; Q6F1P8; -.
DR   SMR; Q6F1P8; -.
DR   STRING; 265311.Mfl218; -.
DR   EnsemblBacteria; AAT75575; AAT75575; Mfl218.
DR   GeneID; 2898269; -.
DR   KEGG; mfl:Mfl218; -.
DR   PATRIC; fig|265311.5.peg.218; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_050910_2_1_14; -.
DR   OMA; WRGAKTA; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000006647; 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..223
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000171347"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000250"
FT   BINDING         45
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         70
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
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         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         161
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         201..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   223 AA;  26158 MW;  719328A9762616DA CRC64;
     MRLRNKPWVK EYLEKNDKYL ISWDKETKIN LSDLFNNKKQ PVHLEIGCGK GNFITNHALK
     ESDINFIGME KEETVVGVAL KKTLAEFEQR NKEVTNLKYF NDFAEDLSDI FAPSSIDKIY
     LNFSDPWPKA RHSKKRLTYR TFLDIYANII KSHGILEFKT DNDGLFAFSL EEIAENKNWE
     LIYQTTDLYS DIEALKNNIP TEYETKFHTA GKNINKLIIK KTF