DMA7_ECOLX
ID DMA7_ECOLX Reviewed; 285 AA.
AC P21311;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Retron Ec67 DNA adenine methylase;
DE EC=2.1.1.72;
DE AltName: Full=M.Eco67Dam;
DE AltName: Full=ORF1-Ec67 dam {ECO:0000303|PubMed:1701261};
DE AltName: Full=Orphan methyltransferase M.EcoEc67Dam {ECO:0000303|PubMed:12654995};
DE Short=M.EcoEc67Dam {ECO:0000303|PubMed:12654995};
GN Name=dam {ECO:0000303|PubMed:1701261};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=O1:NM / CL-1;
RX PubMed=1701261; DOI=10.1073/pnas.87.23.9454;
RA Hsu M.-Y., Inouye M., Inouye S.;
RT "Retron for the 67-base multicopy single-stranded DNA from Escherichia
RT coli: a potential transposable element encoding both reverse transcriptase
RT and Dam methylase functions.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:9454-9458(1990).
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 that recognizes the double-
CC stranded sequence 5'-GATC-3' and methylates A-2 on both strands. May
CC play a regulatory role in the functions of the retron.
CC {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:1701261}.
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; M55249; AAA23396.1; -; Genomic_DNA.
DR PIR; JQ0851; JQ0851.
DR RefSeq; WP_001522695.1; NZ_VRWX01000020.1.
DR AlphaFoldDB; P21311; -.
DR SMR; P21311; -.
DR REBASE; 2846; M.EcoEc67Dam.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
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; Methyltransferase; S-adenosyl-L-methionine; Transferase;
KW Transposable element.
FT CHAIN 1..285
FT /note="Retron Ec67 DNA adenine methylase"
FT /id="PRO_0000087995"
FT BINDING 7
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 11
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 179
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
SQ SEQUENCE 285 AA; 32255 MW; 2F7F5FF2804F4841 CRC64;
MSTILKWAGN KTAIMSELKK HLPAGPRLVE PFAGSCAVMM ATDYPSYLVA DINPDLINLY
KKIAADCEAF ISRARVLFEI ANREVAYYNI RQEFNYSTEI TDFMKAVYFL YLNRHGYRGL
CRYNKSGHFN IPYGNYKNPY FPEKEIRKFA EKAQRATFIC ASFDETLAML QVGDVVYCDP
PYDGTFSGYH TDGFTEDDQY HLASVLEYRS SEGHPVIVSN SDTSLIRSLY RNFTHHYIKA
KRSIGVSAGE SKSATEIIAV SGARCWVGFD PSRGVDSSAV YEVRV
