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Database: UniProt
Entry: L7W7P8_NONDD
LinkDB: L7W7P8_NONDD
Original site: L7W7P8_NONDD 
ID   L7W7P8_NONDD            Unreviewed;       222 AA.
AC   L7W7P8;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 56.
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   OrderedLocusNames=DDD_1052 {ECO:0000313|EMBL:AGC76179.1};
OS   Nonlabens dokdonensis (strain DSM 17205 / KCTC 12402 / DSW-6) (Donghaeana
OS   dokdonensis).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Nonlabens.
OX   NCBI_TaxID=592029 {ECO:0000313|EMBL:AGC76179.1, ECO:0000313|Proteomes:UP000011173};
RN   [1] {ECO:0000313|EMBL:AGC76179.1, ECO:0000313|Proteomes:UP000011173}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17205 / KCTC 12402 / DSW-6
RC   {ECO:0000313|Proteomes:UP000011173};
RX   PubMed=23292138; DOI=10.1093/gbe/evs134;
RA   Kwon S.K., Kim B.K., Song J.Y., Kwak M.J., Lee C.H., Yoon J.H., Oh T.K.,
RA   Kim J.F.;
RT   "Genomic makeup of the marine flavobacterium Nonlabens (Donghaeana)
RT   dokdonensis DSW-6 and identification of a novel class of rhodopsins.";
RL   Genome Biol. Evol. 5:187-187(2013).
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; CP001397; AGC76179.1; -; Genomic_DNA.
DR   RefSeq; WP_015361676.1; NC_020156.1.
DR   AlphaFoldDB; L7W7P8; -.
DR   STRING; 592029.DDD_1052; -.
DR   KEGG; ndo:DDD_1052; -.
DR   PATRIC; fig|592029.3.peg.1041; -.
DR   eggNOG; COG0220; Bacteria.
DR   HOGENOM; CLU_050910_2_2_10; -.
DR   OrthoDB; 9802090at2; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000011173; Chromosome.
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:AGC76179.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:AGC76179.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01057}.
FT   BINDING         50
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         75
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         124
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         160
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         201..204
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   222 AA;  25792 MW;  7067DF98D7EF3FE9 CRC64;
     MGSKNKLKRF HENETFKNVI QPTREEVLSD FKYQGNWDSF FGNDKPITLE LGCGKGEYTV
     ALARKYPDRN FIGIDIKGAR FWRGAKTALE EGLDNVAFMR TQIELVDSAF AKAEIQEIWI
     TFPDPQIKYK RTKHRMTNPD FLAKYKHILQ PNGVVNLKTD SEFMHGYTLG LLQARGEEIL
     YSHHDIYSNT ESPEEVTGTQ TFYEKQYLET GKAITYIKFR LK
//
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