ID H3RH68_PANSE Unreviewed; 239 AA.
AC H3RH68;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 58.
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=trmI {ECO:0000313|EMBL:EHT99408.1};
GN Synonyms=trmB {ECO:0000256|HAMAP-Rule:MF_01057};
GN ORFNames=CKS_1428 {ECO:0000313|EMBL:EHT99408.1}, DSJ_04575
GN {ECO:0000313|EMBL:ARF48692.1};
OS Pantoea stewartii subsp. stewartii DC283.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=660596 {ECO:0000313|EMBL:EHT99408.1, ECO:0000313|Proteomes:UP000005050};
RN [1] {ECO:0000313|EMBL:EHT99408.1, ECO:0000313|Proteomes:UP000005050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:EHT99408.1,
RC ECO:0000313|Proteomes:UP000005050};
RX PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA Wang X., Yang F., von Bodman S.B.;
RT "The genetic and structural basis of two distinct terminal side branch
RT residues in stewartan and amylovoran exopolysaccharides and their potential
RT role in host adaptation.";
RL Mol. Microbiol. 83:195-207(2012).
RN [2] {ECO:0000313|EMBL:EHT99408.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DC283 {ECO:0000313|EMBL:EHT99408.1};
RA Biehl B.S., Ding Y., Dugan-Rocha S.P., Gibbs R.A., Glasner J.D., Kovar C.,
RA Muzny D.M., Neeno-Eckwall E.C., Perna N.T., Qin X., von Bodman S.B.,
RA Weinstock G.M.;
RL Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ARF48692.1, ECO:0000313|Proteomes:UP000192380}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DC283 {ECO:0000313|EMBL:ARF48692.1,
RC ECO:0000313|Proteomes:UP000192380};
RA Duong D.A., Stevens A.M., Jensen R.V.;
RT "Complete Genome Assembly of Pantoea stewartii subsp. stewartii DC283, a
RT Corn Pathogen.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of N(7)-methylguanine at position 46
CC (m7G46) in tRNA. {ECO:0000256|ARBA:ARBA00003015, ECO:0000256|HAMAP-
CC 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;
CC Evidence={ECO:0000256|ARBA:ARBA00000142, ECO:0000256|HAMAP-
CC Rule:MF_01057};
CC -!- PATHWAY: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01057}.
CC -!- SUBUNIT: Monomer. {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}.
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DR EMBL; CP017581; ARF48692.1; -; Genomic_DNA.
DR EMBL; AHIE01000027; EHT99408.1; -; Genomic_DNA.
DR RefSeq; WP_006120864.1; NZ_CP017581.1.
DR AlphaFoldDB; H3RH68; -.
DR STRING; 660596.DSJ_04575; -.
DR KEGG; pstw:DSJ_04575; -.
DR PATRIC; fig|660596.6.peg.3582; -.
DR eggNOG; COG0220; Bacteria.
DR OrthoDB; 9802090at2; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000005050; Unassembled WGS sequence.
DR Proteomes; UP000192380; Chromosome.
DR GO; GO:0008176; F:tRNA (guanine(46)-N7)-methyltransferase activity; IEA:UniProtKB-UniRule.
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:EHT99408.1};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:EHT99408.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01057}.
FT REGION 150..155
FT /note="Interaction with RNA"
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 94
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 121
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 144
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 180
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 217..220
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ SEQUENCE 239 AA; 27266 MW; 0AC52B29F45522C6 CRC64;
MINDVITPEY DENGRPLRRI RSFVRRQGRL TKGQQQALDN YWPEMGVEYQ PEPIDLPALF
GRDAPVTLEI GFGMGASLVT MAQNNPHQNF LGIEVHAPGV GACLASAKDA NVSNLRVMCH
DAVEVLEKMI PDNSLRMVQL FFPDPWHKAR HNKRRIVQVP FAELVMRKLK LGGVFHMATD
WEAYAGHMLE VMSSIAGYRN LSEDNTYVPR PETRPLTKFE QRGQRLGHGV WDLMFERVK
//
