TRMB_BRUA2
ID TRMB_BRUA2 Reviewed; 233 AA.
AC Q2YQS1;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=BAB1_2161;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM040264; CAJ12117.1; -; Genomic_DNA.
DR RefSeq; WP_002965223.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YQS1; -.
DR SMR; Q2YQS1; -.
DR STRING; 359391.BAB1_2161; -.
DR EnsemblBacteria; CAJ12117; CAJ12117; BAB1_2161.
DR GeneID; 3788579; -.
DR KEGG; bmf:BAB1_2161; -.
DR PATRIC; fig|359391.11.peg.1397; -.
DR HOGENOM; CLU_050910_0_3_5; -.
DR OMA; PDPWHKS; -.
DR PhylomeDB; Q2YQS1; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000002719; Chromosome I.
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..233
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000229156"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 138
FT /evidence="ECO:0000250"
FT BINDING 64
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 89
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 138
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 142
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 212..215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 233 AA; 26986 MW; 9CB9E04117775DCF CRC64;
MIDENHPMRA AGNFFGRRHG KPLRPHQSNL FEDLLPRLKL DLATPAPQDL RSLFEAPVET
VRMEIGFGGG EHLHHESGRY PQSGFIGVEP FINGMAKMLA ALDQAPRPNL RLYDEDATAV
LDWLPDASLA GIDLFYPDPW HKRRHWKRRF VSDANLDRFA RVLKPGAKFR FASDIEHYVN
WTLQHCRRHA AFDWQAESPA DWNDAYEGWP GTRYEAKAFH EGRRAAYLTF IRR