ID   TRMB_STRP4              Reviewed;         211 AA.
AC   B5E261;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   27-MAR-2024, entry version 81.
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=SPG_0497;
OS   Streptococcus pneumoniae serotype 19F (strain G54).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=512566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RX   PubMed=11442348; DOI=10.1089/10766290152044995;
RA   Dopazo J., Mendoza A., Herrero J., Caldara F., Humbert Y., Friedli L.,
RA   Guerrier M., Grand-Schenk E., Gandin C., de Francesco M., Polissi A.,
RA   Buell G., Feger G., Garcia E., Peitsch M., Garcia-Bustos J.F.;
RT   "Annotated draft genomic sequence from a Streptococcus pneumoniae type 19F
RT   clinical isolate.";
RL   Microb. Drug Resist. 7:99-125(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G54;
RA   Mulas L., Trappetti C., Hakenbeck R., Iannelli F., Pozzi G., Davidsen T.M.,
RA   Tettelin H., Oggioni M.;
RT   "Pneumococcal beta glucoside metabolism investigated by whole genome
RT   comparison.";
RL   Submitted (MAR-2008) 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; CP001015; ACF55826.1; -; Genomic_DNA.
DR   RefSeq; WP_001266078.1; NC_011072.1.
DR   AlphaFoldDB; B5E261; -.
DR   SMR; B5E261; -.
DR   KEGG; spx:SPG_0497; -.
DR   HOGENOM; CLU_050910_2_1_9; -.
DR   UniPathway; UPA00989; -.
DR   GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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   NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1.
DR   PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR23417:SF14; PPR_LONG DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF02390; Methyltransf_4; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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..211
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_1000136369"
FT   REGION          124..129
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   ACT_SITE        118
FT                   /evidence="ECO:0000250"
FT   BINDING         44
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         69
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         96
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         118
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         122
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         154
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         191..194
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   211 AA;  24341 MW;  F9078B8D918F4C95 CRC64;
     MRVRNRKGAT ELLEANPQYV VLNPLEAKAK WRDLFGNDNP IHVEVGSGKG AFVSGMAKQN
     PDINYIGIDI QKSVLSYALD KVLEAGVSNI KLLWVDGSDL TDYFEDGEID RLYLNFSDPW
     PKKRHEKRRL TYKTFLDTFK RILPENGEIH FKTDNRGLFE YSLVSFSQYG MKLNGVWLDL
     HASDFEGNVM TEYEQKFSNK GQVIYRVEAE F
//