ID   T257_ECOLI     STANDARD;      PRT;   997 AA.
AC   P25239;
DT   01-MAY-1992 (Rel. 22, Created)
DT   01-MAY-1992 (Rel. 22, Last sequence update)
DT   15-SEP-2003 (Rel. 42, Last annotation update)
DE   Type IIS restriction enzyme Eco57I (EC 3.1.21.4) (Endonuclease
DE   Eco57I) [Includes: Adenine-specific methyltransferase activity
DE   Eco57IA (EC 2.1.1.72) (M.Eco57IA)].
GN   ECO57IR.
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   SEQUENCE FROM N.A., AND PARTIAL SEQUENCE.
RC   STRAIN=RFL57;
RX   MEDLINE=93096595; PubMed=1334261;
RA   Janulaitis A., Vaisvila R., Timinskas A., Klimasauskas S.,
RA   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   CHARACTERIZATION.
RX   MEDLINE=93096594; PubMed=1334260;
RA   Janulaitis A., Petrusyte M., Maneliene Z., Klimasauskas S., Butkus V.;
RT   "Purification and properties of the Eco57I restriction endonuclease
RT   and methylase -- prototypes of a new class (type IV).";
RL   Nucleic Acids Res. 20:6043-6049(1992).
CC   -!- FUNCTION: RECOGNIZES THE DOUBLE-STRANDED SEQUENCES CTGAAG AND
CC       CTTCAG AND CLEAVES RESPECTIVELY 22 BASES AFTER C-1 AND 14 BASES
CC       BEFORE C'-1. ALSO ACTS AS A METHYLASE THAT CAUSES SPECIFIC
CC       METHYLATION ON A-5 ON ONE STRAND, THE OTHER STRAND BEING
CC       METHYLATED BY THE ECO57IB METHYLASE.
CC   -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give
CC       specific double-stranded fragments with terminal 5'-phosphates.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S-
CC       adenosyl-L-homocysteine + DNA 6-methylaminopurine.
CC   -!- SUBUNIT: Monomer.
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DR   EMBL; M74821; AAA23389.1; -.
DR   EMBL; X61122; CAA43434.1; -.
DR   PIR; S26426; S26426.
DR   REBASE; 941; Eco57I.
DR   REBASE; 5235; M.Eco57IA.
DR   InterPro; IPR007409; DUF450.
DR   InterPro; IPR002296; N12N6_mtfrase.
DR   InterPro; IPR002052; N6_Mtase.
DR   Pfam; PF04313; HSDR_N; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   PROSITE; PS00092; N6_MTASE; 1.
KW   Restriction system; Multifunctional enzyme; Hydrolase; Transferase;
KW   Nuclease; Endonuclease; Methyltransferase.
SQ   SEQUENCE   997 AA;  116709 MW;  58923F5BCD0E57E5 CRC64;
     MNKKDQLQRL IDKYKSDIDY YRSARYNETQ LRTDFLDQLF LLLGWDITNA AGKPTNEREV
     LVEEGLKARA GENTKKPDYT FRLFSERKFF LEAKKPSVDI STTIEPALQV RRYGFTAKLK
     ISVLSNFEYT AIYDCSNQVK ETDSVANSRI KLYHFTELVD KFDEINNLIG RESVYTGHFD
     NEWSEIENKI LRFSVDDLFL KQINDWGLLL ANEFLQIKNE LPEEKLNDLV QNYINSIVFL
     RVCEDRDLEE YETLYHFAQD KDFQSLVKKL KSSDKKYNSG LFSLEYIDEL LSNANSCIEH
     HRTIILPHKA HTLSLFSLLI FLGNIYEIFL SEKVRIDELG NVKIQPKEEH IDRDVVTTPT
     HIVKEIIRNT VVEYCKGKSD IEILNSKFAD IACGSGAFII VAFQFIQDIL IDYYIQNDKS
     KLQQISEHTY KLKFEVKREI LCKCIYGIDK DYNATKACTF GLLLKLLEGE TTETIGKDTP
     ILPALDTNIL FGNSLIDSGD KVKQEDIFSI NPFDLTNYQF DVIVGNPPYM ATEHMNQLTP
     KELDIYKRKY KSAYKQFDKY FLFIERSIQI LKEYGYLGYI LPSRFIKVDA GKKLRKFLSE
     NKYLSKLISF GSHQVFKNKT TYTCLLFLNK ENHDNFSFYE VKDNKKWLTR EDKYLLSSTY
     QTSSLDSDTW VLEKKINDIL KLMFSKSEQL GNIVGKSNVA NGIQTSANKY YIHKEIKSEN
     GFIYFEYDGI EYHIEKELTR PYFETNRSGD DSFYTYKDVE PNSFVVYPYK KVGERIQFIE
     YDELKRQYPK LFEFLQVVKV HLNDKKRSIK PDPTGLMMVQ IRRSQALENC DVDQKLIVGI
     LSNGYKYSID NHRTFVSSGG TAGYSIINIP NNVRYSIYYI QAILTSKYLE WFASIYGDIF
     RGRFVARGTK VQTRMPIPTI DFDDPKQKEI HDTISSKQQY LNKLYSQTQK SADRDKIIFE
     RQFEQEKIQM DYLIKNLFDL GDLDSEIPTV EDLYKNL
//