ID   TRMB_AROAE              Reviewed;         259 AA.
AC   Q8G9C6;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=AZOSEA12950;
GN   ORFNames=c1A43;
OS   Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=12420173; DOI=10.1007/s00203-002-0487-2;
RA   Rabus R., Kube M., Beck A., Widdel F., Reinhardt R.;
RT   "Genes involved in the anaerobic degradation of ethylbenzene in a
RT   denitrifying bacterium, strain EbN1.";
RL   Arch. Microbiol. 178:506-516(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EbN1;
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI07420.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8G9C6; -.
DR   SMR; Q8G9C6; -.
DR   STRING; 76114.c1A43; -.
DR   EnsemblBacteria; CAI07420; CAI07420; c1A43.
DR   KEGG; eba:c1A43; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_050910_0_1_4; -.
DR   OMA; PDPWHKS; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000006552; 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..259
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000171287"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        166
FT                   /evidence="ECO:0000250"
FT   BINDING         91
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         116
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         143
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         166
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         237..240
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   259 AA;  28575 MW;  0659D4B4511FD1C1 CRC64;
     MTFPSHNPPE TGHPSAAPDE ALPAAEAPVP GDPEARFSSR SIRSFVLRQG RMSVAQQRHL
     DETLPKVGIP YRVAPLDLDA AFGRAAPKIV EIGFGMGETT AKIAAALPDK DFLTIEVHGP
     GVGSLCKLIA EGVLDNVRIV QHDAVEVLRD MIPERALAGV HVFFPDPWHK KRHHKRRIIQ
     PDFVALIASR LAPGAYLHCA TDWEEYAQWM LEVLAAEPAL ENTADGYAPR PAYRPLTKFE
     NRGLKLGHGV WDLVFRRRG