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Database: UniProt
Entry: A0A091B9J1_9GAMM
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ID   A0A091B9J1_9GAMM        Unreviewed;       243 AA.
AC   A0A091B9J1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
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=P873_11185 {ECO:0000313|EMBL:KFN49328.1};
OS   Arenimonas composti TR7-09 = DSM 18010.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Arenimonas.
OX   NCBI_TaxID=1121013 {ECO:0000313|EMBL:KFN49328.1, ECO:0000313|Proteomes:UP000029391};
RN   [1] {ECO:0000313|EMBL:KFN49328.1, ECO:0000313|Proteomes:UP000029391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TR7-09 {ECO:0000313|EMBL:KFN49328.1,
RC   ECO:0000313|Proteomes:UP000029391};
RA   Chen F., Wang G.;
RT   "Genome sequencing of Arenimonas composti.";
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFN49328.1}.
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DR   EMBL; AWXU01000037; KFN49328.1; -; Genomic_DNA.
DR   RefSeq; WP_026816911.1; NZ_AWXU01000037.1.
DR   AlphaFoldDB; A0A091B9J1; -.
DR   STRING; 1121013.GCA_000426365_01645; -.
DR   eggNOG; COG0220; Bacteria.
DR   OrthoDB; 9802090at2; -.
DR   UniPathway; UPA00989; -.
DR   Proteomes; UP000029391; 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   Reference proteome {ECO:0000313|Proteomes:UP000029391};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01057};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01057};
KW   tRNA processing {ECO:0000256|ARBA:ARBA00022694, ECO:0000256|HAMAP-
KW   Rule:MF_01057}.
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         70
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         95
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         122
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         145
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="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         181
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
FT   BINDING         218..221
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01057"
SQ   SEQUENCE   243 AA;  27811 MW;  7FEB0941D4C555A8 CRC64;
     MAEQQPTADD VAGEPRPHRP IRSFVLRQGR QTPAQKRAFD LHWPRYGLEY GATPRDFDAV
     FGRAAPRIVE IGFGNGEQLL FAAQNEPRHD FIGIEVHGPG VGRLLNAAAE AGVHNLRLYQ
     HDAVEVLREE IAPASLAQVR IYFPDPWHKK RHHKRRLVQP EFVGLLCARL APGGLLHLAT
     DWENYAEHMF DVLDAEPRLR NRAGPRTPLP RPEWRRQTHF EQRGLKLGHG VWDLLYDRLP
     DDP
//
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