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TRMB_DEIGD
ID   TRMB_DEIGD              Reviewed;         331 AA.
AC   Q1IWK0;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-JUN-2006, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Dgeo_2090;
OS   Deinococcus geothermalis (strain DSM 11300 / AG-3a).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=319795;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11300 / AG-3a;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Daly M.J.,
RA   Fredrickson J.K., Makarova K.S., Gaidamakova E.K., Zhai M., Richardson P.;
RT   "Complete sequence of chromosome 1 of Deinococcus geothermalis DSM 11300.";
RL   Submitted (APR-2006) 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; CP000359; ABF46384.1; -; Genomic_DNA.
DR   RefSeq; WP_011531210.1; NC_008025.1.
DR   AlphaFoldDB; Q1IWK0; -.
DR   SMR; Q1IWK0; -.
DR   STRING; 319795.Dgeo_2090; -.
DR   EnsemblBacteria; ABF46384; ABF46384; Dgeo_2090.
DR   KEGG; dge:Dgeo_2090; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_077150_0_0_0; -.
DR   OMA; PWPKAGH; -.
DR   OrthoDB; 1025521at2; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000002431; 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..331
FT                   /note="tRNA (guanine-N(7)-)-methyltransferase"
FT                   /id="PRO_0000288144"
FT   ACT_SITE        105
FT                   /evidence="ECO:0000250"
FT   BINDING         29
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         55
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         105
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         109
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   331 AA;  36336 MW;  79FECB6096E34734 CRC64;
     MIFRLADFHF PDSAARLYPD TPQRPWILEV GFGDGRFWPH YAATFPEAPN YLGVEISGVS
     LLKAERRLRE AGLSNAVLTK LPATPLIREV VPAGSLDAIV VNFPDPWPKA GHAEHRLLRA
     PFFRLAASRL KPGGAVLLTT DHDEYFEFAC REAEASGVMR AELTDPPPAA LETKYARKWR
     ELGLEVQHAR FVPTHHPHVP HGTVARFPDS EDAPAVPHAI LTLPAAFDPG AFHKHTARGG
     QTREDPVGWT VVLLELYRSL KQDGWVMLAH VVEGELTQEV LIGISARGDG SHLVRLASFG
     GPIITPGVKA AVGVVTDWLE EQGAAVRHRG Y
 
 
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