ID I7ZB30_9GAMM Unreviewed; 230 AA.
AC I7ZB30;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 46.
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=WQQ_24540 {ECO:0000313|EMBL:EIT68872.1};
OS Hydrocarboniphaga effusa AP103.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Nevskiales; Nevskiaceae;
OC Hydrocarboniphaga.
OX NCBI_TaxID=1172194 {ECO:0000313|EMBL:EIT68872.1, ECO:0000313|Proteomes:UP000003704};
RN [1] {ECO:0000313|EMBL:EIT68872.1, ECO:0000313|Proteomes:UP000003704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP103 {ECO:0000313|EMBL:EIT68872.1,
RC ECO:0000313|Proteomes:UP000003704};
RX PubMed=22933753; DOI=10.1128/JB.01017-12;
RA Chang H.K., Zylstra G.J., Chae J.C.;
RT "Genome Sequence of n-Alkane-Degrading Hydrocarboniphaga effusa Strain
RT AP103T (ATCC BAA-332T).";
RL J. Bacteriol. 194:5120-5120(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:EIT68872.1}.
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DR EMBL; AKGD01000002; EIT68872.1; -; Genomic_DNA.
DR RefSeq; WP_007185397.1; NZ_AKGD01000002.1.
DR AlphaFoldDB; I7ZB30; -.
DR STRING; 1172194.WQQ_24540; -.
DR PATRIC; fig|1172194.4.peg.2371; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000003704; 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:EIT68872.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000003704};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:EIT68872.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01057}.
FT REGION 142..147
FT /note="Interaction with RNA"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 61
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 113
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 136
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 140
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 172
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 209..212
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ SEQUENCE 230 AA; 25835 MW; 2DA6D031EBA2BE69 CRC64;
MSLEADAPHR RIRSFVRREG RMTDGQRLAL ESLWPTYGLD APAQPLAPAT LFGREAPVVF
EIGFGNGDHL LSRALNEPQH DFIGVEVHRP GCGRVMMLAE KQGSTNLRVA CHDAVEVLRD
WLVPGSLAEV VIYFPDPWHK KRHNKRRLVQ PEFLALIVGA LKPGGLLRMA TDWAPYAEHM
LESVRATPEL VNLAPGGAYA ERAQTRPKTR FEARGERLGH EVFDLLLQKR
//
