DMA_SALTY
ID DMA_SALTY Reviewed; 278 AA.
AC P0DMP3; P0A291; P55893;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 1.
DT 03-AUG-2022, entry version 33.
DE RecName: Full=DNA adenine methylase;
DE EC=2.1.1.72;
DE AltName: Full=DNA adenine methyltransferase;
DE AltName: Full=Deoxyadenosyl-methyltransferase;
DE AltName: Full=Orphan methyltransferase M.StyDam {ECO:0000303|PubMed:12654995};
DE Short=M.StyDam {ECO:0000303|PubMed:12654995};
GN Name=dam; OrderedLocusNames=STM3484;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP NOMENCLATURE, AND SUBTYPE.
RX PubMed=12654995; DOI=10.1093/nar/gkg274;
RA Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT endonucleases and their genes.";
RL Nucleic Acids Res. 31:1805-1812(2003).
CC -!- FUNCTION: An alpha subtype methylase, recognizes the double-stranded
CC sequence 5'-GATC-3' and methylates A-2 (PubMed:12654995) (By
CC similarity). May be involved in methyl-directed DNA mismatch repair,
CC initiation of chromosome replication and gene expression (By
CC similarity). {ECO:0000250|UniProtKB:P0AEE8,
CC ECO:0000250|UniProtKB:P0DMP4, ECO:0000303|PubMed:12654995}.
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL22346.1; -; Genomic_DNA.
DR RefSeq; NP_462387.1; NC_003197.2.
DR RefSeq; WP_000742132.1; NC_003197.2.
DR AlphaFoldDB; P0DMP3; -.
DR SMR; P0DMP3; -.
DR STRING; 99287.STM3484; -.
DR PaxDb; P0DMP3; -.
DR EnsemblBacteria; AAL22346; AAL22346; STM3484.
DR GeneID; 1255007; -.
DR KEGG; stm:STM3484; -.
DR PATRIC; fig|99287.12.peg.3682; -.
DR HOGENOM; CLU_063430_0_1_6; -.
DR OMA; MNRHGFN; -.
DR PhylomeDB; P0DMP3; -.
DR BioCyc; SENT99287:STM3484-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IBA:GO_Central.
DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IBA:GO_Central.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central.
DR Gene3D; 1.10.1020.10; -; 1.
DR Gene3D; 3.40.50.150; -; 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 PANTHER; PTHR30481; PTHR30481; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; SSF53335; 1.
DR TIGRFAMs; TIGR00571; dam; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; Methyltransferase; Reference proteome;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..278
FT /note="DNA adenine methylase"
FT /id="PRO_0000087994"
FT BINDING 10
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 14
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 181
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 278 AA; 32027 MW; 900F4B77D827C3A8 CRC64;
MKKNRAFLKW AGGKYPLLDD IKRHLPKGEC LVEPFVGAGS VFLNTDFSRY ILADINSDLI
SLYNIVKLRT DEYVQASREL FMPETNQAEV YYQLREEFNT CQDPFRRAVL FLYLNRYGYN
GLCRYNLRGE FNVPFGRYKR PYFPEAELYH FAEKAQNAFF YCESYADSMA RADKSSVVYC
DPPYAPLSAT ANFTAYHTNS FSLTQQAHLA EIAENLVSNR IPVLISNHDT ALTREWYQLA
KLHVVKVRRS ISSNGGTRKK VDELLALYQP GVATPARK
