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Database: UniProt
Entry: T2SIU6_HELPX
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Original site: T2SIU6_HELPX 
ID   T2SIU6_HELPX            Unreviewed;       392 AA.
AC   T2SIU6;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=L932_06090 {ECO:0000313|EMBL:EQD92517.1};
OS   Helicobacter pylori PZ5026.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1337392 {ECO:0000313|EMBL:EQD92517.1, ECO:0000313|Proteomes:UP000015722};
RN   [1] {ECO:0000313|EMBL:EQD92517.1, ECO:0000313|Proteomes:UP000015722}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PZ5026 {ECO:0000313|EMBL:EQD92517.1,
RC   ECO:0000313|Proteomes:UP000015722};
RX   PubMed=24051318;
RA   Sheh A., Piazuelo M.B., Wilson K.T., Correa P., Fox J.G.;
RT   "Draft Genome Sequences of Helicobacter pylori Strains Isolated from
RT   Regions of Low and High Gastric Cancer Risk in Colombia.";
RL   Genome Announc. 1:e00736-13(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}.
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:EQD92517.1}.
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DR   EMBL; ASYT01000155; EQD92517.1; -; Genomic_DNA.
DR   RefSeq; WP_021173432.1; NZ_ASYT01000155.1.
DR   AlphaFoldDB; T2SIU6; -.
DR   PATRIC; fig|1337392.3.peg.862; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000015722; 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:EQD92517.1};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01057, ECO:0000313|EMBL:EQD92517.1};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   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         149
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         176
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         232
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   392 AA;  45398 MW;  7966FBEB676E7141 CRC64;
     MPHFLAKLDS KPLEYPIIKG DFCFYREFLS LKHPTKSCVH ASFKGDVFLL QKIRREGDFL
     IKSEKATPLK REILKQALRI YSQSFEVISH NLQENSKHAS QKKALDLEAF EYFIQKNQAP
     ILAEIGFGSG RHLIELAKNN PTKTCLGIEI HTPSIAQALK QIELLDLKNL HILQGDGRLV
     LESMPNHRCE KIFVHFPVPW NEKKHRRVLS EKFLNEALRV LKPRGFLELR TDDSLYFEDS
     LKLALKNFKC EIEIKKNAQI PVVSKYEARW NKLKKDIYDL RIYSLGLDEN PTQNHALDFS
     FDTITIDKES VGTILKTPKI IKEGYFAHVC NIYENKGDFL VELSMGDFDW PVRLFVLLAE
     NKLFYLNKSP LKTLNNHKAH LLLQNILSQK GV
//
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