TRMB_THEMA
ID TRMB_THEMA Reviewed; 313 AA.
AC Q9X027;
DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=TM_0925;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD36006.1; -; Genomic_DNA.
DR PIR; F72317; F72317.
DR RefSeq; NP_228733.1; NC_000853.1.
DR RefSeq; WP_004080637.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X027; -.
DR SMR; Q9X027; -.
DR STRING; 243274.THEMA_00010; -.
DR EnsemblBacteria; AAD36006; AAD36006; TM_0925.
DR KEGG; tma:TM0925; -.
DR eggNOG; COG0220; Bacteria.
DR InParanoid; Q9X027; -.
DR OMA; PWPKAGH; -.
DR OrthoDB; 1025521at2; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000008183; 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; 3.40.50.150; -; 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..313
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171413"
FT BINDING 33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 58
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 85
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 112
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 177..180
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 313 AA; 36770 MW; 34EE4D3669AD2CF3 CRC64;
MVVTEYELKP QNFPRFPLDW SEIFGRKAKI VVEIGFGNGE FLAELARRHP EKDFVGFEVS
ITSFVKAQKK FKRYNLKNVR LVKVDARFGL RELFPDNSVE KVYINFPCPW PKKRHESRRI
TSYDFLQTLS AVLEMDGTVE FATDEEWYAR EVLDTFESSE YFVVDVFEEN FKRDVETRYE
RKWKSQGKKT FLIVARKVKN GTVKRLMEGE NTMAHSVFEG NVTWEKLKEL EGKVFKDKNK
IFVVKKVYRD GDYLLKVIST DEGGFQQVYY LNLSGRDGKW VLKLDEGSDP YRTPALKWSL
RRIPEELTAQ GSP
