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 16-OCT-2001 (Rel. 40, 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. 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; M74821; AAA23389.1; -. DR EMBL; X61122; CAA43434.1; -. DR PIR; S26426; S26426. DR REBASE; 941; Eco57I. DR REBASE; 5235; M.Eco57IA. 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 Hydrolase; Endonuclease; Nuclease; Transferase; Methyltransferase; KW Multifunctional enzyme; Restriction system. 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 //