DMA_HAEIN
ID DMA_HAEIN Reviewed; 286 AA.
AC P44431;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 122.
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=M.HindIV;
DE AltName: Full=Orphan methyltransferase M.HindDam {ECO:0000303|PubMed:12654995};
DE Short=M.HindDam {ECO:0000303|PubMed:12654995};
GN Name=dam; Synonyms=hindIVM; OrderedLocusNames=HI_0209;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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: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; L42023; AAC21877.1; -; Genomic_DNA.
DR PIR; H64054; H64054.
DR RefSeq; NP_438378.1; NC_000907.1.
DR RefSeq; WP_010868957.1; NC_000907.1.
DR STRING; 71421.HI_0209; -.
DR REBASE; 1152; M.HindDam.
DR REBASE; 204156; M.Lbr1174ORF79P.
DR EnsemblBacteria; AAC21877; AAC21877; HI_0209.
DR KEGG; hin:HI_0209; -.
DR PATRIC; fig|71421.8.peg.214; -.
DR eggNOG; COG0338; Bacteria.
DR HOGENOM; CLU_063430_0_1_6; -.
DR OMA; MNRHGFN; -.
DR PhylomeDB; P44431; -.
DR BioCyc; HINF71421:G1GJ1-220-MON; -.
DR Proteomes; UP000000579; 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..286
FT /note="DNA adenine methylase"
FT /id="PRO_0000087996"
FT BINDING 21
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 194
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 286 AA; 33219 MW; BE39C5725AE35DEE CRC64;
MLRPKKQSLK PKLKHRPFLK WAGGKFRLTD EINKAFPNKK NCLIEPFVGA GAVFLNSNFE
RYILADINPD LINLFNIVKX NVDGYIEDCK PIFFADDANT PDYYYAKRRQ FNASTEPFER
SIIFLYLNRF GFNGLCRYNS KNEFNVPFGA YKTHYFPEDE LRYFAHKAQS AVFLCCDFQK
TFEFADKDSV IYCDPPYAPL QQETNFTGYA GNEFGLAQQR ALADLAKSIQ KEKQISILIS
NHDTKFTREI YNGAKFKRVK VQRSISQNPE KRVKVKELIA IFGARK
