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   03-AUG-2022, entry version 95.
DE   RecName: Full=Type II restriction enzyme and methyltransferase RM.Eco57I {ECO:0000303|PubMed:12654995};
DE            EC=3.1.21.4 {ECO:0000269|PubMed:1334260};
DE   AltName: Full=Endonuclease Eco57I;
DE   AltName: Full=Type IIS restriction enzyme Eco57I;
DE   Includes:
DE     RecName: Full=Adenine-specific methyltransferase activity Eco57IA;
DE              Short=M.Eco57IA;
DE              EC=2.1.1.72 {ECO:0000269|PubMed:1334260};
GN   Name=eco57IR {ECO:0000303|PubMed:1334261};
OS   Escherichia coli.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-5, AND FUNCTION.
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   NOMENCLATURE, AND SUBTYPES.
RX   PubMed=12654995; DOI=10.1093/nar/gkg274;
RA   Roberts R.J., Belfort M., Bestor T., Bhagwat A.S., Bickle T.A.,
RA   Bitinaite J., Blumenthal R.M., Degtyarev S.K., Dryden D.T., Dybvig K.,
RA   Firman K., Gromova E.S., Gumport R.I., Halford S.E., Hattman S.,
RA   Heitman J., Hornby D.P., Janulaitis A., Jeltsch A., Josephsen J., Kiss A.,
RA   Klaenhammer T.R., Kobayashi I., Kong H., Krueger D.H., Lacks S.,
RA   Marinus M.G., Miyahara M., Morgan R.D., Murray N.E., Nagaraja V.,
RA   Piekarowicz A., Pingoud A., Raleigh E., Rao D.N., Reich N., Repin V.E.,
RA   Selker E.U., Shaw P.C., Stein D.C., Stoddard B.L., Szybalski W.,
RA   Trautner T.A., Van Etten J.L., Vitor J.M., Wilson G.G., Xu S.Y.;
RT   "A nomenclature for restriction enzymes, DNA methyltransferases, homing
RT   endonucleases and their genes.";
RL   Nucleic Acids Res. 31:1805-1812(2003).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (4.2 ANGSTROMS) IN COMPLEX WITH DNA, AND SEQUENCE
RP   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   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP   PROPERTIES, AND SUBUNIT.
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: An E, G and S subtype restriction enzyme that recognizes the
CC       (non-palindromic) double-stranded sequence 5'-CTGAAG-3' and cleaves
CC       respectively 22 bases after C-1 and 14 bases before C'-1; cleavage of
CC       lambda DNA is never complete. Also acts as a methylase that causes
CC       specific methylation on A-5 in 5'-CTGAAG-3', the other strand is
CC       methylated by the M.Eco57I methylase. {ECO:0000269|PubMed:1334260,
CC       ECO:0000269|PubMed:1334261, ECO:0000303|PubMed:12654995}.
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         Evidence={ECO:0000269|PubMed:1334260};
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         Evidence={ECO:0000269|PubMed:1334260};
CC   -!- ACTIVITY REGULATION: Mg(2+) is absolutely required for DNA restriction.
CC       {ECO:0000269|PubMed:1334260}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 9.0 for DNA restriction and 7.5 for methylation.
CC         {ECO:0000269|PubMed:1334260};
CC   -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:1334260}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the N(4)/N(6)-
CC       methyltransferase family. {ECO:0000305}.
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   AlphaFoldDB; P25239; -.
DR   SMR; P25239; -.
DR   REBASE; 941; Eco57I.
DR   PRIDE; P25239; -.
DR   BRENDA; 3.1.21.4; 2026.
DR   PRO; PR:P25239; -.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; RM_methylase_Eco57I-like.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
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; DNA-binding; Endonuclease; Hydrolase;
KW   Methyltransferase; Multifunctional enzyme; Nuclease; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..998
FT                   /note="Type II restriction enzyme and methyltransferase
FT                   RM.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
//