ID T257_ECOLI STANDARD; PRT; 998 AA. AC P25239; DT 01-MAY-1992 (Rel. 22, Created) DT 25-OCT-2004 (Rel. 45, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Type IIS restriction enzyme Eco57I (EC 3.1.21.4) (Endonuclease Eco57I) DE [Includes: Adenine-specific methyltransferase activity Eco57IA DE (EC 2.1.1.72) (M.Eco57IA)]. GN Name=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., 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 REVISIONS, AND X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS). RX PubMed=15134658; DOI=10.1016/j.bbapap.2003.12.006; RA Tamulaitiene G., Grazulis S., Janulaitis A., Janowski R., Bujacz G., RA Jaskolski M.; RT "Crystallization and preliminary crystallographic studies of a RT bifunctional restriction endonuclease Eco57I."; RL Biochim. Biophys. Acta 1698:251-254(2004). RN [3] 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; CAA43434.3; -. DR PIR; S26426; S26426. DR REBASE; 5235; M.Eco57IA. DR REBASE; 941; Eco57I. 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 Direct protein sequencing; Endonuclease; Hydrolase; Methyltransferase; KW Multifunctional enzyme; Nuclease; Restriction system; Transferase. FT CONFLICT 42 42 I -> L (in Ref. 1; AAA23389). FT CONFLICT 207 207 R -> G (in Ref. 1; AAA23389). FT CONFLICT 299 321 WSIIEQLYFPQSTYSFSVFSSDI -> EHHRTIILPHKAHT FT LSLFSLLIF (in Ref. 1; AAA23389). FT CONFLICT 401 401 E -> V (in Ref. 1; AAA23389). FT CONFLICT 644 644 F -> N (in Ref. 1; AAA23389). FT CONFLICT 816 823 PNEWYRYG -> LMMVQIR (in Ref. 1; FT AAA23389). SQ SEQUENCE 998 AA; 117086 MW; EDB090A7FBFFCC93 CRC64; MNKKDQLQRL IDKYKSDIDY YRSARYNETQ LRTDFLDQLF LILGWDITNA AGKPTNEREV LVEEGLKARA GENTKKPDYT FRLFSERKFF LEAKKPSVDI STTIEPALQV RRYGFTAKLK ISVLSNFEYT AIYDCSNQVK ETDSVANSRI KLYHFTELVD KFDEINNLIG RESVYTGHFD NEWSEIENKI LRFSVDDLFL KQINDWRLLL ANEFLQIKNE LPEEKLNDLV QNYINSIVFL RVCEDRDLEE YETLYHFAQD KDFQSLVKKL KSSDKKYNSG LFSLEYIDEL LSNANSCIWS IIEQLYFPQS TYSFSVFSSD ILGNIYEIFL SEKVRIDELG NVKIQPKEEH IDRDVVTTPT HIVKEIIRNT VVEYCKGKSD IEILNSKFAD IACGSGAFII EAFQFIQDIL IDYYIQNDKS KLQQISEHTY KLKFEVKREI LCKCIYGIDK DYNATKACTF GLLLKLLEGE TTETIGKDTP ILPALDTNIL FGNSLIDSGD KVKQEDIFSI NPFDLTNYQF DVIVGNPPYM ATEHMNQLTP KELDIYKRKY KSAYKQFDKY FLFIERSIQI LKEYGYLGYI LPSRFIKVDA GKKLRKFLSE NKYLSKLISF GSHQVFKNKT TYTCLLFLNK ENHDNFSFYE VKDFKKWLTR EDKYLLSSTY QTSSLDSDTW VLEKKINDIL KLMFSKSEQL GNIVGKSNVA NGIQTSANKY YIHKEIKSEN GFIYFEYDGI EYHIEKELTR PYFETNRSGD DSFYTYKDVE PNSFVVYPYK KVGERIQFIE YDELKRQYPK LFEFLQVVKV HLNDKKRSIK PDPTGPNEWY RYGRSQALEN CDVDQKLIVG ILSNGYKYSI DNHRTFVSSG GTAGYSIINI PNNVRYSIYY IQAILTSKYL EWFASIYGDI FRGRFVARGT KVQTRMPIPT IDFDDPKQKE IHDTISSKQQ YLNKLYSQTQ KSADRDKIIF ERQFEQEKIQ MDYLIKNLFD LGDLDSEIPT VEDLYKNL //