ID   MTE2_ECOLX              Reviewed;         477 AA.
AC   P05101;
DT   13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT   13-AUG-1987, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Type II methyltransferase M.EcoRII {ECO:0000303|PubMed:12654995};
DE            Short=M.EcoRII;
DE            EC=2.1.1.37 {ECO:0000305|PubMed:3029675};
DE   AltName: Full=Cytosine-specific methyltransferase EcoRII;
DE   AltName: Full=Modification methylase EcoRII;
GN   Name=ecoRIIM;
OS   Escherichia coli.
OG   Plasmid N3.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND MUTAGENESIS OF
RP   1-MET--LEU-34.
RC   STRAIN=ATCC 33694 / HB101;
RX   PubMed=3029675; DOI=10.1093/nar/15.1.313;
RA   Som S., Bhagwat A.S., Friedman S.;
RT   "Nucleotide sequence and expression of the gene encoding the EcoRII
RT   modification enzyme.";
RL   Nucleic Acids Res. 15:313-332(1987).
RN   [2]
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, recognizes the double-stranded sequence 5'-
CC       CCWGG-3', methylates C-2 on both strands, and protects the DNA from
CC       cleavage by the EcoRII endonuclease. {ECO:0000269|PubMed:3029675,
CC       ECO:0000303|PubMed:12654995}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-
CC         methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC         Xref=Rhea:RHEA:13681, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:11370,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:85452, ChEBI:CHEBI:85454; EC=2.1.1.37;
CC         Evidence={ECO:0000255|PROSITE-ProRule:PRU10018,
CC         ECO:0000305|PubMed:3029675};
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the class I-like SAM-binding methyltransferase
CC       superfamily. C5-methyltransferase family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01016}.
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DR   EMBL; X05050; CAA28725.1; -; Genomic_DNA.
DR   PIR; A25871; XYECR2.
DR   RefSeq; WP_001288432.1; NZ_CP025710.1.
DR   RefSeq; YP_007349454.1; NC_020086.1.
DR   RefSeq; YP_008574830.1; NC_022374.1.
DR   RefSeq; YP_008574963.1; NC_022375.1.
DR   RefSeq; YP_009023119.1; NC_023909.1.
DR   RefSeq; YP_009023200.1; NC_023910.1.
DR   RefSeq; YP_009060562.1; NC_024967.1.
DR   RefSeq; YP_009068675.1; NC_025141.1.
DR   RefSeq; YP_009071472.1; NC_025183.1.
DR   RefSeq; YP_724464.1; NC_007682.3.
DR   AlphaFoldDB; P05101; -.
DR   SMR; P05101; -.
DR   REBASE; 3396; M.EcoRII.
DR   PRO; PR:P05101; -.
DR   GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR040743; DNA_meth_N.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF18284; DNA_meth_N; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR00675; dcm; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   1: Evidence at protein level;
KW   DNA-binding; Methyltransferase; Plasmid; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..477
FT                   /note="Type II methyltransferase M.EcoRII"
FT                   /id="PRO_0000087874"
FT   DOMAIN          96..466
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
FT   MUTAGEN         1..34
FT                   /note="MSEFELLAQDLLEKAEAEEQLRQENDKKLLGQVL->MTMITPSLAAA: Has
FT                   25% activity."
FT                   /evidence="ECO:0000269|PubMed:3029675"
SQ   SEQUENCE   477 AA;  54556 MW;  9E595D3809BCCAEA CRC64;
     MSEFELLAQD LLEKAEAEEQ LRQENDKKLL GQVLEIYDQK YVAELLRKVG KNEWSRETLN
     RWINGKCSPK TLTLAEEELL RKMLPEAPAH HPDYAFRFID LFAGIGGIRK GFETIGGQCV
     FTSEWNKEAV RTYKANWFND AQEHTFNLDI REVTLSDKPE VPENDAYAYI NEHVPDHDVL
     LAGFPCQPFS LAGVSKKNSL GRAHGFECEA QGTLFFDVAR IIRAKKPAIF VLENVKNLKS
     HDKGKTFKVI MDTLDELGYE VADAAEMGKN DPKVIDGKHF LPQHRERIVL VGFRRDLNIH
     QGFTLRDISR FYPEQRPSFG ELLEPVVDSK YILTPKLWEY LYNYAKKHAA KGNGFGFGLV
     NPENKESIAR TLSARYHKDG SEILIDRGWD MATGETDFAN EENQAHRPRR LTPRECARLM
     GFEKVDGRPF RIPVSDTQSY RQFGNSVVVP VFEAVAKLLE PYILKAVNAD SCKVERI