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 27-MAR-2024, entry version 101. 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; Pseudomonadota; 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 BRENDA; 3.1.21.4; 2026. DR PRO; PR:P25239; -. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0008170; F:N-methyltransferase activity; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases_sf. DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1. DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1. DR Pfam; PF02384; N6_Mtase; 1. DR PRINTS; PR00507; N12N6MTFRASE. DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 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 //