ID A0A0U5BD55_9BACL Unreviewed; 224 AA.
AC A0A0U5BD55;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=tRNA (guanine-N(7)-)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
DE EC=2.1.1.33 {ECO:0000256|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA (guanine(46)-N(7))-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
DE AltName: Full=tRNA(m7G46)-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057};
GN Name=trmB {ECO:0000256|HAMAP-Rule:MF_01057,
GN ECO:0000313|EMBL:BAU29542.1};
GN ORFNames=CB4_03742 {ECO:0000313|EMBL:BAU29542.1}, DFP93_11947
GN {ECO:0000313|EMBL:PYE59122.1};
OS Aneurinibacillus soli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae;
OC Aneurinibacillus group; Aneurinibacillus.
OX NCBI_TaxID=1500254 {ECO:0000313|EMBL:BAU29542.1, ECO:0000313|Proteomes:UP000217696};
RN [1] {ECO:0000313|EMBL:BAU29542.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB4 {ECO:0000313|EMBL:BAU29542.1};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Aneurinibacillus soli.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PYE59122.1, ECO:0000313|Proteomes:UP000247363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8566 {ECO:0000313|EMBL:PYE59122.1,
RC ECO:0000313|Proteomes:UP000247363};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01057};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01057}.
CC -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC superfamily. TrmB family. {ECO:0000256|HAMAP-Rule:MF_01057}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01057}.
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DR EMBL; AP017312; BAU29542.1; -; Genomic_DNA.
DR EMBL; QJSZ01000019; PYE59122.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U5BD55; -.
DR KEGG; asoc:CB4_03742; -.
DR OrthoDB; 9802090at2; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000217696; Chromosome.
DR Proteomes; UP000247363; Unassembled WGS sequence.
DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 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 NCBIfam; TIGR00091; tRNA (guanosine(46)-N7)-methyltransferase TrmB; 1.
DR PANTHER; PTHR23417; 3-DEOXY-D-MANNO-OCTULOSONIC-ACID TRANSFERASE/TRNA GUANINE-N 7 - -METHYLTRANSFERASE; 1.
DR PANTHER; PTHR23417:SF14; PPR_LONG DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02390; Methyltransf_4; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS51625; SAM_MT_TRMB; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01057,
KW ECO:0000313|EMBL:BAU29542.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000217696};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:BAU29542.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01057}.
FT BINDING 44
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 69
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 96
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 118
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 122
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 154
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 192..195
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ SEQUENCE 224 AA; 25972 MW; 4796F6EFF2CCEB1D CRC64;
MRLRKRPGVR EEMATYPKLV PMNGPDHKGN WRAFFGNDNP IHIELGTGKG NFITTLAEQN
PDINFFGVEL HEEVLIQAVK KAEEKGLTNI SFLWINVNDL EDYFASGEVN RIYLNFSDPW
PKKRHAKRRL TDRSFLSKYK NVLNPDGYIQ LKTDNETLFE YSLNEFAHEM FLLSGITLDL
HKSEYAEGNV MTEYEAKFVE RGMRIYRCLA AHPMQLMAIA HGKK
//
