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Database: UniProt
Entry: I4W8J8_9GAMM
LinkDB: I4W8J8_9GAMM
Original site: I4W8J8_9GAMM 
ID   I4W8J8_9GAMM            Unreviewed;       171 AA.
AC   I4W8J8;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 44.
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:EIL95789.1};
GN   ORFNames=UU5_09517 {ECO:0000313|EMBL:EIL95789.1};
OS   Rhodanobacter sp. 115.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Rhodanobacteraceae; Rhodanobacter.
OX   NCBI_TaxID=1162282 {ECO:0000313|EMBL:EIL95789.1, ECO:0000313|Proteomes:UP000004557};
RN   [1] {ECO:0000313|EMBL:EIL95789.1, ECO:0000313|Proteomes:UP000004557}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=115 {ECO:0000313|EMBL:EIL95789.1,
RC   ECO:0000313|Proteomes:UP000004557};
RX   PubMed=22843592; DOI=10.1128/JB.00871-12;
RA   Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA   Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA   Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT   "Genome sequences for six rhodanobacter strains, isolated from soils and
RT   the terrestrial subsurface, with variable denitrification capabilities.";
RL   J. Bacteriol. 194:4461-4462(2012).
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   -!- 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:EIL95789.1}.
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DR   EMBL; AJXS01000234; EIL95789.1; -; Genomic_DNA.
DR   AlphaFoldDB; I4W8J8; -.
DR   PATRIC; fig|1162282.3.peg.1817; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000004557; Unassembled WGS sequence.
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:EIL95789.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:EIL95789.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01057}.
FT   REGION          83..88
FT                   /note="Interaction with RNA"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         2
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         27
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         54
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         77
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         150..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   171 AA;  19357 MW;  46B672FA245F55EA CRC64;
     MEIGFGNGEA LAWASEYDPA RDYLGVEVHG PGVGRLMNVL AARDAGNVRL YRHDAVEVLE
     NEIAPDTLAE ARIWFPDPWH KKRHNKRRII QPGFVAQLAT RMAPGGLLHL ATDWQAYAEH
     MLEVMEAAPA WSNAIAPGEY AEKPAWRIET HFERRGLKLG HGVWDLLYRR V
//
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