MT57_ECOLX
ID MT57_ECOLX Reviewed; 544 AA.
AC P25240;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Type II methyltransferase M.Eco57I {ECO:0000303|PubMed:12654995, ECO:0000303|PubMed:1334260};
DE Short=M.Eco57I {ECO:0000303|PubMed:1334260};
DE EC=2.1.1.72 {ECO:0000269|PubMed:1334260};
DE AltName: Full=Adenine-specific methyltransferase Eco57IB;
DE AltName: Full=Modification methylase Eco57IB;
DE Short=Eco57IB;
GN Name=eco57IBM; Synonyms=eco57IM {ECO:0000303|PubMed:1334261};
OS Escherichia coli.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=562;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, AND FUNCTION.
RC STRAIN=RFL57;
RX PubMed=1334261; DOI=10.1093/nar/20.22.6051;
RA Janulaitis A., Vaisvila R., Timinskas A., Klimasauskas S., Butkus V.;
RT "Cloning and sequence analysis of the genes coding for Eco57I type IV
RT restriction-modification enzymes.";
RL Nucleic Acids Res. 20:6051-6056(1992).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=1334260; DOI=10.1093/nar/20.22.6043;
RA Janulaitis A., Petrusyte M., Maneliene Z., Klimasauskas S., Butkus V.;
RT "Purification and properties of the Eco57I restriction endonuclease and
RT methylase -- prototypes of a new class (type IV).";
RL Nucleic Acids Res. 20:6043-6049(1992).
RN [3]
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: A gamma subtype methylase that recognizes the (non-
CC palindromic) double-stranded sequence 5'-CTGAAG-3', methylates A-5 on
CC both strands, and protects the DNA from cleavage by the RM.Eco57I
CC endonuclease. {ECO:0000269|PubMed:1334260, ECO:0000269|PubMed:1334261,
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 Evidence={ECO:0000269|PubMed:1334260};
CC -!- ACTIVITY REGULATION: Stimulated by Ca(2+) and Mg(2+).
CC {ECO:0000269|PubMed:1334260}.
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000305}.
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DR EMBL; M74821; AAA23388.1; -; Genomic_DNA.
DR EMBL; X61122; CAA43433.1; -; Genomic_DNA.
DR PIR; S26425; S26425.
DR AlphaFoldDB; P25240; -.
DR SMR; P25240; -.
DR REBASE; 5234; M.Eco57I.
DR PRO; PR:P25240; -.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF02384; N6_Mtase; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Methyltransferase; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..544
FT /note="Type II methyltransferase M.Eco57I"
FT /id="PRO_0000087940"
SQ SEQUENCE 544 AA; 62013 MW; 53A1D5D7337AB4FA CRC64;
MKFKADQTSQ KLRGGYYTPQ NLADYVTKWV LSKNPKTILE PSCGDGVFIQ AIANNGYNSN
IELFCFELFD TEASKALERC KLNNFSNATI TEGDFLVWAN ECLKKNKQIF DGALGNPPFI
RYQFLERNFQ EQAQLVFEHL DLKFTKHTNA WVPFLLSSLA LLKQGGRIGM VIPSEISHVM
HAQSLRSYLG HVCSKIVIID PKEIWFEDTL QGAVILLAEK KQYPDEASQG VGIVSVSGFE
FLQEDPNVLF NDTAGINGET VEGKWTKATL SIDELQLIKR VIAHPDVRKF KDIAKVDVGR
YCDGANNYFL VDNETVKLYK LERFAHPMFG RSQHCPGIIY DEKQHIENQE KGLPTNFLYI
DEEFEYLSKS VKNYIKLGEV EEYHKRYKCR IRKPWFKVPS VYSTEIGMLK RCHDAPRLIH
NRVRAYTTDT AYRVSSTVTS TENLVCSFLN PITVITAELE GLFYGGGVLE LVPSEIEKLY
ILIVEGLEHN VEELNLLIKD GQIERVIRQQ GSLILGTLGF TQEENEKLVE IGRSLEIEGY
VSRV
