TRMB_RUTMC
ID TRMB_RUTMC Reviewed; 185 AA.
AC A1AXP6;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=Rmag_0997;
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Proteobacteria; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthia.
OX NCBI_TaxID=413404;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
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; Evidence={ECO:0000255|PROSITE-
CC ProRule:PRU00957};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000255|PROSITE-ProRule:PRU00957}.
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DR EMBL; CP000488; ABL02703.1; -; Genomic_DNA.
DR RefSeq; WP_011738328.1; NC_008610.1.
DR AlphaFoldDB; A1AXP6; -.
DR SMR; A1AXP6; -.
DR STRING; 413404.Rmag_0997; -.
DR EnsemblBacteria; ABL02703; ABL02703; Rmag_0997.
DR KEGG; rma:Rmag_0997; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_050910_0_1_6; -.
DR OMA; IHIATDW; -.
DR OrthoDB; 1025521at2; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000002587; Chromosome.
DR GO; GO:0008176; F:tRNA (guanine-N7-)-methyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; -; 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..185
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000288219"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00957"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00957"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00957"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00957"
FT BINDING 163..166
FT /ligand="substrate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00957"
SQ SEQUENCE 185 AA; 21883 MW; 7F98BCCB1F52422D CRC64;
MRLDLSKDKI NLDALFVKQQ KIDFDNGDSL LKIAINMPDI NFLDIEIYET SINRLINKTH
KYQLSNLKII QVDAHTKDNN FDSFQLFLSG PWYKKKYHKL RLVQTAFLDL LSKTIIHNGK
IHIATDWVRY VTTMMNALKN HLHFKNTQND PIYSLRPGHR PITKFERRSH RPGHDVLDLI
FKNEK
