ID   MTE1_ECOLX              Reviewed;         326 AA.
AC   P00472;
DT   21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Type II methyltransferase M.EcoRI {ECO:0000303|PubMed:12654995};
DE            Short=M.EcoRI {ECO:0000303|PubMed:12654995};
DE            EC=2.1.1.72;
DE   AltName: Full=Adenine-specific methyltransferase EcoRI;
DE   AltName: Full=Modification methylase EcoRI;
GN   Name=ecoRIM;
OS   Escherichia coli.
OG   Plasmid pMB1, and Plasmid pMB4.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   PLASMID=pMB1;
RX   PubMed=6257703; DOI=10.1016/s0021-9258(19)69752-8;
RA   Greene P.J., Gupta M., Boyer H.W., Brown W.E., Rosenberg J.M.;
RT   "Sequence analysis of the DNA encoding the Eco RI endonuclease and
RT   methylase.";
RL   J. Biol. Chem. 256:2143-2153(1981).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=C; PLASMID=pMB4;
RX   PubMed=6257701; DOI=10.1016/s0021-9258(19)69750-4;
RA   Newman A.K., Rubin R.A., Kim S.-H., Modrich P.;
RT   "DNA sequences of structural genes for Eco RI DNA restriction and
RT   modification enzymes.";
RL   J. Biol. Chem. 256:2131-2139(1981).
RN   [3]
RP   PROTEIN SEQUENCE OF 2, AND CONFIRMATION OF 2-25 AND CARBOXYL ENDS OF
RP   SEQUENCE BY AMINO ACID ANALYSIS.
RX   PubMed=6257702; DOI=10.1016/s0021-9258(19)69751-6;
RA   Rubin R.A., Modrich P., Vanaman T.C.;
RT   "Partial NH2- and COOH-terminal sequence analyses of Eco RI DNA restriction
RT   and modification enzymes.";
RL   J. Biol. Chem. 256:2140-2142(1981).
RN   [4]
RP   NOMENCLATURE.
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).
CC   -!- FUNCTION: A methylase that recognizes the double-stranded sequence 5'-
CC       GAATTC-3', methylates A-3 on both strands, and protects the DNA from
CC       cleavage by the EcoRI endonuclease. {ECO:0000303|PubMed:12654995}.
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   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000305}.
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DR   EMBL; J01675; AAA26372.1; -; Genomic_DNA.
DR   PIR; A92308; XYECP4.
DR   RefSeq; WP_002670781.1; NZ_VNZC01000056.1.
DR   AlphaFoldDB; P00472; -.
DR   REBASE; 3395; M.EcoRI.
DR   PRIDE; P00472; -.
DR   PATRIC; fig|562.8010.peg.1143; -.
DR   PRO; PR:P00472; -.
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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR025247; EcoRI-like_methylase.
DR   Pfam; PF13651; EcoRI_methylase; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; DNA-binding; Methyltransferase; Plasmid;
KW   Restriction system; S-adenosyl-L-methionine; Transferase.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:6257702"
FT   CHAIN           2..326
FT                   /note="Type II methyltransferase M.EcoRI"
FT                   /id="PRO_0000087959"
SQ   SEQUENCE   326 AA;  38044 MW;  5F6AFE1DD1CBB1A8 CRC64;
     MARNATNKLL HKAKKSKSDE FYTQYCDIEN ELQYYREHFS DKVVYCNCDD PRVSNFFKYF
     AVNFDNLGLK KLIASCYVEN KEGFSSSEAA KNGFYYEYHK ENGKKLVFDD ISVSSFCGDG
     DFRSSESIDL LKKSDIVVTN PPFSLFREYL DQLIKYDKKF LIIANVNSIT YKEVFNLIKE
     NKIWLGVHLG RGVSGFIVPE HYELYGTEAR IDSNGNRIIS PNNCLWLTNL DVFIRHKDLP
     LTRKYFGNES SYPKYDNYDA INVNKTKDIP LDYNGVMGVP ITFLHKFNPE QFELIKFRKG
     VDEKDLSING KCPYFRILIK NKRLQK