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Database: UniProt
Entry: W6T844_9LACO
LinkDB: W6T844_9LACO
Original site: W6T844_9LACO 
ID   W6T844_9LACO            Unreviewed;       214 AA.
AC   W6T844;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ORFNames=LFAB_06470 {ECO:0000313|EMBL:ETY74444.1};
OS   Lactiplantibacillus fabifermentans T30PCM01.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactiplantibacillus.
OX   NCBI_TaxID=1400520 {ECO:0000313|EMBL:ETY74444.1, ECO:0000313|Proteomes:UP000019247};
RN   [1] {ECO:0000313|EMBL:ETY74444.1, ECO:0000313|Proteomes:UP000019247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T30PCM01 {ECO:0000313|EMBL:ETY74444.1,
RC   ECO:0000313|Proteomes:UP000019247};
RX   PubMed=24558238;
RA   Treu L., Vendramin V., Bovo B., Giacomini A., Corich V., Campanaro S.;
RT   "Genome Sequence of Lactobacillus fabifermentans Strain T30PCM01, Isolated
RT   from Fermenting Grape Marc.";
RL   Genome Announc. 2:e00060-e00014(2014).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETY74444.1}.
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DR   EMBL; AWWK01000032; ETY74444.1; -; Genomic_DNA.
DR   RefSeq; WP_024623780.1; NZ_KK036485.1.
DR   AlphaFoldDB; W6T844; -.
DR   STRING; 1400520.LFAB_06470; -.
DR   PATRIC; fig|1400520.3.peg.1259; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_050910_2_1_9; -.
DR   OrthoDB; 9802090at2; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000019247; 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:ETY74444.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:ETY74444.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01057}.
FT   REGION          124..129
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000256|HAMAP-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   214 AA;  24755 MW;  B573C56837833983 CRC64;
     MRVRNKPWAP KLINAHPELI TETPADLRGK WQTRFAKPQP IQIEVGSGKG QFIIEMAKQH
     PEINYIAIEI QTSVIAVILR KLVEEPLPNL QLCHADGQAV TAFFEPNEID RLYLNFSDPW
     PKSRHEKRRL TYKSFLAAYQ EVLKPAGQIE FKTDNRGLFE FSLTSMNNFG LHFEQVWLDL
     HAVVTPEENV ETEYEQKFSI HGPIYKIIAT FPTK
//
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