TRMB_LACJO
ID TRMB_LACJO Reviewed; 218 AA.
AC Q74I98;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=LJ_1667;
OS Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=257314;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNCM I-1225 / La1 / NCC 533;
RX PubMed=14983040; DOI=10.1073/pnas.0307327101;
RA Pridmore R.D., Berger B., Desiere F., Vilanova D., Barretto C.,
RA Pittet A.-C., Zwahlen M.-C., Rouvet M., Altermann E., Barrangou R.,
RA Mollet B., Mercenier A., Klaenhammer T., Arigoni F., Schell M.A.;
RT "The genome sequence of the probiotic intestinal bacterium Lactobacillus
RT johnsonii NCC 533.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:2512-2517(2004).
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; AE017198; AAS09440.1; -; Genomic_DNA.
DR RefSeq; WP_011162354.1; NC_005362.1.
DR AlphaFoldDB; Q74I98; -.
DR SMR; Q74I98; -.
DR STRING; 257314.LJ_1667; -.
DR EnsemblBacteria; AAS09440; AAS09440; LJ_1667.
DR KEGG; ljo:LJ_1667; -.
DR PATRIC; fig|257314.6.peg.1493; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_050910_2_1_9; -.
DR OMA; WRGAKTA; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000000581; 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; Reference proteome; S-adenosyl-L-methionine;
KW Transferase; tRNA processing.
FT CHAIN 1..218
FT /note="tRNA (guanine-N(7)-)-methyltransferase"
FT /id="PRO_0000171337"
FT REGION 126..131
FT /note="Interaction with RNA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT ACT_SITE 120
FT /evidence="ECO:0000250"
FT BINDING 46
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 98
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 120
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
FT BINDING 196..199
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01057"
SQ SEQUENCE 218 AA; 25533 MW; 717A915A1C869AD2 CRC64;
MRLRNKPWAQ KLVAEHPEVI LNEPDPDKKI NWEERFEDFS KPLAIEIGSG KGQFITTLAK
EHPEMNFIGV ELQTTAAGMI LRTKLEEKID NLQLMCADAA NIAMYLPENS VDIVYLNFSD
PWPKTRHEKR RLTYKSFLDK YRQILKPEGH LEFKTDNRGL FEYSLVSLNN YGMKFDYVSL
DLHHADDEIF ERNVETEYEH KFAAKGNPIY CLHAHFVK