TRMB_CORGB
ID TRMB_CORGB Reviewed; 255 AA.
AC A4QHQ6;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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=cgR_2753;
OS Corynebacterium glutamicum (strain R).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=340322;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R;
RX PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT "Comparative analysis of the Corynebacterium glutamicum group and complete
RT genome sequence of strain R.";
RL Microbiology 153:1042-1058(2007).
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; AP009044; BAF55772.1; -; Genomic_DNA.
DR RefSeq; WP_011015448.1; NC_009342.1.
DR AlphaFoldDB; A4QHQ6; -.
DR SMR; A4QHQ6; -.
DR EnsemblBacteria; BAF55772; BAF55772; cgR_2753.
DR KEGG; cgt:cgR_2753; -.
DR HOGENOM; CLU_050910_0_2_11; -.
DR OMA; PDPWHKS; -.
DR PhylomeDB; A4QHQ6; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000006698; 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; S-adenosyl-L-methionine; Transferase; tRNA processing.
FT CHAIN 1..255
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_1000064390"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..169
FT /note="Interaction with RNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT ACT_SITE 158
FT /evidence="ECO:0000250"
FT BINDING 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 108
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 135
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 158
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 162
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 232..235
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 255 AA; 28806 MW; 550F5003FAE01AA6 CRC64;
MSISDNSRDQ LGELPAGRPL QSDFDNDLDY PRLGSVTFRR GTLTENQQTM WDEKWPELGR
VLEDELIDVD AWFGREGAKT IVEIGSGTGT STAAMAPLEA DTNIVAVELY KPGLAKLMGS
VVRGEIDNVR MVRGDGIEVL NRMFADGSLD GIRVYFPDPW PKARHNKRRI IQSGPLNLFA
KKLKPGGVLH VATDHADYAE WINELVEVEP LLEYKGWPWE ECPQLTDRQV ITKFEGKGLE
KDHVINEYLW QKVQN