ID   TRMB_COPPD              Reviewed;         319 AA.
AC   B5Y822;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 62.
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=COPRO5265_0563;
OS   Coprothermobacter proteolyticus (strain ATCC 35245 / DSM 5265 / OCM 4 /
OS   BT).
OC   Bacteria; Coprothermobacterota; Coprothermobacteria; Coprothermobacterales;
OC   Coprothermobacteraceae; Coprothermobacter.
OX   NCBI_TaxID=309798;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35245 / DSM 5265 / OCM 4 / BT;
RA   Dodson R.J., Durkin A.S., Wu M., Eisen J., Sutton G.;
RT   "The complete genome sequence of Coprothermobacter proteolyticus strain
RT   ATCC 5245 / DSM 5265 / BT.";
RL   Submitted (AUG-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; CP001145; ACI18005.1; -; Genomic_DNA.
DR   RefSeq; WP_012544655.1; NC_011295.1.
DR   AlphaFoldDB; B5Y822; -.
DR   SMR; B5Y822; -.
DR   STRING; 309798.COPRO5265_0563; -.
DR   EnsemblBacteria; ACI18005; ACI18005; COPRO5265_0563.
DR   KEGG; cpo:COPRO5265_0563; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_077150_0_0_9; -.
DR   OMA; RTCLLEN; -.
DR   OrthoDB; 1025521at2; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000001732; 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   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..319
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000387946"
FT   BINDING         28
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         51
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         134
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         167..170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   319 AA;  36203 MW;  BA9AB3611373D08A CRC64;
     MLIKPQSTSS FPLNWDAIFP EKNPLAVEIG FGNGKFLKTL ETTGTNVVGF EVSLLSVEKA
     MKVIDHTKTA LLLMDGIWGL RELFSERSVD ALYINFPLPW PHKKHASRRL FTLPKLQIYA
     SRLVDNAILQ LQTDVKEYAE EAIRNSEESG LFSLADYAVR NEVQVGTKYE QKWVSQGKKI
     YKVVLRKKRH VSVPNYLDKE VIMPHAIVHD SHGTLKAGTY RTTFGTIKLW EPFSNNQAML
     LIPAIVSDDD FIGVSLQQRV YISVSPHREG FIVKLDNHAD VFKTENVKSL IWLIANQISN
     GNIKRINVQP PSKLEYEPA