ID   TRMB_FUSNN              Reviewed;         640 AA.
AC   Q8R6G8;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Bifunctional glycosyltransferase/methyltransferase;
DE   Includes:
DE     RecName: Full=KdtA protein homolog;
DE              EC=2.-.-.-;
DE   Includes:
DE     RecName: Full=tRNA (guanine-N(7)-)-methyltransferase;
DE              EC=2.1.1.33;
DE     AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase;
DE     AltName: Full=tRNA(m7G46)-methyltransferase;
GN   Name=trmB; OrderedLocusNames=FN1606;
OS   Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS   BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC   Bacteria; Fusobacteria; Fusobacteriales; Fusobacteriaceae; Fusobacterium.
OX   NCBI_TaxID=190304;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC   2640 / LMG 13131 / VPI 4355;
RX   PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA   Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA   Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA   Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA   Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA   Overbeek R.;
RT   "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT   strain ATCC 25586.";
RL   J. Bacteriol. 184:2005-2018(2002).
CC   -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC       (m7G46) in tRNA. {ECO:0000250}.
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;
CC   -!- SIMILARITY: In the C-terminal section; belongs to the class I-like SAM-
CC       binding methyltransferase superfamily. TrmB family. {ECO:0000305}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 1 family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE009951; AAL93721.1; -; Genomic_DNA.
DR   RefSeq; NP_602422.1; NC_003454.1.
DR   AlphaFoldDB; Q8R6G8; -.
DR   SMR; Q8R6G8; -.
DR   STRING; 190304.FN1606; -.
DR   CAZy; GT30; Glycosyltransferase Family 30.
DR   EnsemblBacteria; AAL93721; AAL93721; FN1606.
DR   KEGG; fnu:FN1606; -.
DR   PATRIC; fig|190304.8.peg.98; -.
DR   eggNOG; COG0220; Bacteria.
DR   eggNOG; COG1519; Bacteria.
DR   HOGENOM; CLU_427447_0_0_0; -.
DR   InParanoid; Q8R6G8; -.
DR   BioCyc; FNUC190304:G1FZS-109-MON; -.
DR   Proteomes; UP000002521; Chromosome.
DR   GO; GO:0043527; C:tRNA methyltransferase complex; IBA:GO_Central.
DR   GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IBA:GO_Central.
DR   GO; GO:0036265; P:RNA (guanine-N7)-methylation; IBA:GO_Central.
DR   GO; GO:0030488; P:tRNA methylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.11720; -; 1.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_01057; tRNA_methyltr_TrmB; 1.
DR   InterPro; IPR007507; Glycos_transf_N.
DR   InterPro; IPR038107; Glycos_transf_N_sf.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR003358; tRNA_(Gua-N-7)_MeTrfase_Trmb.
DR   PANTHER; PTHR23417; PTHR23417; 1.
DR   Pfam; PF04413; Glycos_transf_N; 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..640
FT                   /note="Bifunctional glycosyltransferase/methyltransferase"
FT                   /id="PRO_0000171430"
FT   REGION          1..438
FT                   /note="Glycosyltransferase"
FT   REGION          439..640
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT   ACT_SITE        544
FT                   /evidence="ECO:0000250"
FT   BINDING         470
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         495
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         544
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000250"
FT   BINDING         578
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         617..620
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   640 AA;  75760 MW;  6745564DC10BFE6E CRC64;
     MYNLLRKIAL TLYRPFMKEK MKTFINKRLS QDFSDLKDEE YIWIHCSSVG EVNLSEDLVK
     KFYSISRKNI LISVFTDTGY ENAVKKYSDK KKIKVIYFPV DDKKKINEIL NKIKLKLLVL
     VETELWPNLI NEVNEKNSRI IVVNGRISDR SYPRYKKLKF LLKSMLQKIA FFYMQSEIDK
     ERIVSLGAIK EKVENVGNLK FSISLEKYSD IEKKEYRKFL NIGDRKVFVA GSTRTGEDEI
     ILDVFKRLKN YVLIIVPRHL DRLPKIENLI KENNLTYVKY SDLENNTSTG KENIILVDKM
     GVLRKLYSIS DIAFVGGTLV NIGGHNLLEP LFYRKTVIFG KYTQNVVDIA KEILRRKIGF
     QVENVEEFVK AIETIENEKN SDEEINSFFE ENRLIALNIV KKENLIMNNI KEEAKDLWKH
     FFHSEKSNYN MYMYKLLDYP EYIMYDNDVM KEKKSKWSEY FGNSDQIAVE IGTGSGNFIY
     QLAERNPNKN FIGLELRFKR LVLAAQKCKK RNIKNVAFLR KRGEELEDFL ANNEISEMYI
     NFPDPWEGTE KNRIIQERLF KTLDKIMKKD GMLYFKTDHD VYYNDVLELV KTLDNYEVIY
     HTSDLHNSEK AENNIKTEFE QLFLHKHNKN INYIEIKKIV