ID T257_ECOLX Reviewed; 998 AA. AC P25239; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2004, sequence version 2. DT 07-OCT-2020, entry version 91. DE RecName: Full=Type IIS restriction enzyme Eco57I; DE EC=3.1.21.4; DE AltName: Full=Endonuclease Eco57I; DE Includes: DE RecName: Full=Adenine-specific methyltransferase activity Eco57IA; DE Short=M.Eco57IA; DE EC=2.1.1.72; GN Name=eco57IR; OS Escherichia coli. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=562; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. 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 X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS), AND SEQUENCE REVISION. 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 bifunctional RT restriction endonuclease Eco57I."; RL Biochim. Biophys. Acta 1698:251-254(2004). RN [3] RP CHARACTERIZATION. 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). CC -!- FUNCTION: Recognizes the double-stranded sequences CTGAAG and CTTCAG CC and cleaves respectively 22 bases after C-1 and 14 bases before C'-1. CC Also acts as a methylase that causes specific methylation on A-5 on one CC strand, the other strand being methylated by the Eco57IB methylase. 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 -!- 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 -!- 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; -; Genomic_DNA. DR EMBL; X61122; CAA43434.3; -; Genomic_DNA. DR PIR; S26426; S26426. DR REBASE; 941; Eco57I. DR PRIDE; P25239; -. DR PRO; PR:P25239; -. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. 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; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR011639; RM_methylase_Eco57I. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF07669; Eco57I; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 1: Evidence at protein level; KW Direct protein sequencing; Endonuclease; Hydrolase; Methyltransferase; KW Multifunctional enzyme; Nuclease; Restriction system; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1..998 FT /note="Type IIS restriction enzyme Eco57I" FT /id="PRO_0000077274" FT CONFLICT 42 FT /note="I -> L (in Ref. 1; AAA23389)" FT /evidence="ECO:0000305" FT CONFLICT 207 FT /note="R -> G (in Ref. 1; AAA23389)" FT /evidence="ECO:0000305" FT CONFLICT 299..321 FT /note="WSIIEQLYFPQSTYSFSVFSSDI -> EHHRTIILPHKAHTLSLFSLLIF FT (in Ref. 1; AAA23389)" FT /evidence="ECO:0000305" FT CONFLICT 401 FT /note="E -> V (in Ref. 1; AAA23389)" FT /evidence="ECO:0000305" FT CONFLICT 644 FT /note="F -> N (in Ref. 1; AAA23389)" FT /evidence="ECO:0000305" FT CONFLICT 816..823 FT /note="PNEWYRYG -> LMMVQIR (in Ref. 1; AAA23389)" FT /evidence="ECO:0000305" SQ SEQUENCE 998 AA; 117087 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 //