ID F2IVK6_POLGS Unreviewed; 228 AA.
AC F2IVK6;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
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:ADZ72724.1};
GN OrderedLocusNames=SL003B_4307 {ECO:0000313|EMBL:ADZ72724.1};
OS Polymorphum gilvum (strain LMG 25793 / CGMCC 1.9160 / SL003B-26A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Polymorphum.
OX NCBI_TaxID=991905 {ECO:0000313|EMBL:ADZ72724.1, ECO:0000313|Proteomes:UP000008130};
RN [1] {ECO:0000313|EMBL:ADZ72724.1, ECO:0000313|Proteomes:UP000008130}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 25793 / CGMCC 1.9160 / SL003B-26A1
RC {ECO:0000313|Proteomes:UP000008130};
RX PubMed=21478361; DOI=10.1128/JB.00333-11;
RA Li S.G., Tang Y.Q., Nie Y., Cai M., Wu X.L.;
RT "Complete genome sequence of Polymorphum gilvum SL003B-26A1T, a crude oil-
RT degrading bacterium from oil-polluted saline soil.";
RL J. Bacteriol. 193:2894-2895(2011).
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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01057}.
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DR EMBL; CP002568; ADZ72724.1; -; Genomic_DNA.
DR AlphaFoldDB; F2IVK6; -.
DR STRING; 991905.SL003B_4307; -.
DR KEGG; pgv:SL003B_4307; -.
DR PATRIC; fig|991905.3.peg.4441; -.
DR eggNOG; COG0220; Bacteria.
DR HOGENOM; CLU_050910_0_3_5; -.
DR OrthoDB; 9802090at2; -.
DR UniPathway; UPA00989; -.
DR Proteomes; UP000008130; 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:ADZ72724.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008130};
KW S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:ADZ72724.1};
KW tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW Rule:MF_01057}.
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 59
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 84
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 111
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 133
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 169
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT BINDING 207..210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ SEQUENCE 228 AA; 26386 MW; F9E5BFAA0A9D16F9 CRC64;
MTDRYEGAFF GRRKGKPLSP RQVQRMETVL PRLAVDLSRP APDPLSDLFD GDVRAIWLEI
GFGGGEHLLQ RARETPDVGF IGCEPFVGSL AKAVSEIADT GLSNVRLHDD DATGLLDWLP
EASLDRIFQL YPDPWPKKRH WKRRFINAAN LDRFARVLKP GAEVRFASDI DTYVDWTLRH
FRDHPGFEWT AERADDWRLP WVSWPGTRYE AKALREGRVP RYLTFRRL
//
