ID   T2E7_ECOLX              Reviewed;         230 AA.
AC   P50194;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   25-MAY-2022, entry version 49.
DE   RecName: Full=Type II restriction enzyme Eco47I {ECO:0000303|PubMed:12654995};
DE            Short=R.Eco47I {ECO:0000303|PubMed:7607524};
DE            EC=3.1.21.4;
DE   AltName: Full=Endonuclease Eco47I;
DE   AltName: Full=Type-2 restriction enzyme Eco47I;
GN   Name=eco47IR {ECO:0000303|PubMed:7607524};
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=RFL47;
RX   PubMed=7607524; DOI=10.1016/0378-1119(94)00796-u;
RA   Stankevicius K., Povilionis P., Lubys A., Menkevicius S., Janulaitis A.;
RT   "Cloning and characterization of the unusual restriction-modification
RT   system comprising two restriction endonucleases and one
RT   methyltransferase.";
RL   Gene 157:49-53(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: A P subtype restriction enzyme that recognizes the double-
CC       stranded sequence 5'-GGWCC-3' and cleaves after G-1.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:7607524}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endonucleolytic cleavage of DNA to give specific double-
CC         stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4;
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X82105; CAA57630.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50194; -.
DR   SMR; P50194; -.
DR   REBASE; 930; Eco47I.
DR   PRO; PR:P50194; -.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0009036; F:type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR019070; Restrct_endonuc_II_SinI.
DR   Pfam; PF09570; RE_SinI; 1.
PE   4: Predicted;
KW   Endonuclease; Hydrolase; Nuclease; Restriction system.
FT   CHAIN           1..230
FT                   /note="Type II restriction enzyme Eco47I"
FT                   /id="PRO_0000077306"
SQ   SEQUENCE   230 AA;  26864 MW;  AA3621FF506DFB11 CRC64;
     MSKETSFVKN AEELAKQKMD AINPELSSKF KFLIKFLSQF PEACSKPRSK KMQNKVGQEE
     HIEYLARSFH ESRLPRKPTP PTTVPDEVVS IVLNISFNIQ PENLERIKEE HRLSMAAENI
     VGDLLERYLA EKLEPSGWIW CSGTSVKAVD FIHYDEKNNE WNLLQVKNRD NTENSSSSKI
     RDNTTIKKWF RTYSQRDATN WDNFPDEVSS KNLNEEDFRA FVKNYLVKII