ID G5Q8S2_SALMO Unreviewed; 271 AA.
AC G5Q8S2;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=LTSEMON_4787 {ECO:0000313|EMBL:EHC74401.1};
OS Salmonella enterica subsp. enterica serovar Montevideo str. S5-403.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913242 {ECO:0000313|EMBL:EHC74401.1, ECO:0000313|Proteomes:UP000003221};
RN [1] {ECO:0000313|EMBL:EHC74401.1, ECO:0000313|Proteomes:UP000003221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5-403 {ECO:0000313|EMBL:EHC74401.1,
RC ECO:0000313|Proteomes:UP000003221};
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:EHC74401.1}.
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DR EMBL; AFCS01001077; EHC74401.1; -; Genomic_DNA.
DR AlphaFoldDB; G5Q8S2; -.
DR REBASE; 44019; M.Sen403DamP.
DR PATRIC; fig|913242.3.peg.4139; -.
DR Proteomes; UP000003221; 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 3
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 7
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 47
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
FT BINDING 174
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|PIRSR:PIRSR000398-1"
SQ SEQUENCE 271 AA; 31169 MW; 716E7F8DE87C121F CRC64;
MKWAGGKYPL LDDIKRHLPK GECLVEPFVG AGSVFLNTDF SRYILADINS DLISLYNIVK
LRTDEYVQAS RELFMPETNQ AEVYYQLREE FNTCQDPFRR AVLFLYLNRY GYNGLCRYNL
RGEFNVPFGR YKRPYFPEAE LYHFAEKAQN AFFYCESYAD SMARADKSSV VYCDPPYAPL
SATANFTAYH TNSFSLTQQA HLAEIAENLV SNRIPVLISN HDTALTREWY QLAKLHVVKV
RRSISSNGGT RKKVDELLAL YQPGVATPAR K
//
