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.
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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
//