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Database: UniProt
Entry: G5QJS6_SALRU
LinkDB: G5QJS6_SALRU
Original site: G5QJS6_SALRU 
ID   G5QJS6_SALRU            Unreviewed;       316 AA.
AC   G5QJS6;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
GN   ORFNames=LTSERUB_2884 {ECO:0000313|EMBL:EHC88114.1};
OS   Salmonella enterica subsp. enterica serovar Rubislaw str. A4-653.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=913081 {ECO:0000313|EMBL:EHC88114.1, ECO:0000313|Proteomes:UP000004903};
RN   [1] {ECO:0000313|EMBL:EHC88114.1, ECO:0000313|Proteomes:UP000004903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A4-653 {ECO:0000313|EMBL:EHC88114.1,
RC   ECO:0000313|Proteomes:UP000004903};
RX   PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA   den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA   Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA   Furtado M.R., Wiedmann M.;
RT   "Genome sequencing reveals diversification of virulence factor content and
RT   possible host adaptation in distinct subpopulations of Salmonella
RT   enterica.";
RL   BMC Genomics 12:425-425(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-
CC         homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-
CC         COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:90615, ChEBI:CHEBI:90616; EC=2.1.1.72;
CC         Evidence={ECO:0000256|ARBA:ARBA00001279,
CC         ECO:0000256|RuleBase:RU361257};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU361257}.
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:EHC88114.1}.
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DR   EMBL; AFCT01001057; EHC88114.1; -; Genomic_DNA.
DR   AlphaFoldDB; G5QJS6; -.
DR   REBASE; 44029; M.Sen653ORF2884P.
DR   PATRIC; fig|913081.3.peg.2246; -.
DR   Proteomes; UP000004903; Unassembled WGS sequence.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR012263; M_m6A_EcoRV.
DR   InterPro; IPR012327; MeTrfase_D12.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00571; dam; 1.
DR   PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR   PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR   Pfam; PF02086; MethyltransfD12; 1.
DR   PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR   PRINTS; PR00505; D12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000256|RuleBase:RU361257};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW   ECO:0000256|RuleBase:RU361257};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361257}.
FT   BINDING         17
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         21
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         62
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT   BINDING         202
FT                   /ligand="S-adenosyl-L-methionine"
FT                   /ligand_id="ChEBI:CHEBI:59789"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ   SEQUENCE   316 AA;  36926 MW;  A7183B087CB6FE67 CRC64;
     MGWCMKKPVF IRSPLKWAGG KYNALPELFK HLPREGECLI EPFVGSGTIF LNTNYRRYVL
     CDSNPALINF FHTLTWHTGE VIWWAGALFS VGDDKEDYYS RRKFYNTIKD YPRLVSDRVY
     WAALFLYLNR HSFNGLFRTN SKGEFNVPFG KREKAPYFPE KEMRRFALKA RQTKTKFICC
     DFRLALNPYL VPELDNAVIY CDPPYIPESK TADFTQYNGE RFTRRDHEHL VKYLTNNKLH
     FAKVVISNSD TPLTREIYAP FNLHKLKVRR SISANAKGRK NTPEVIGVLD GRERYVSAPR
     RAGKATVMAQ WRDTSC
//
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