ID   MTE8_ECOLX              Reviewed;         417 AA.
AC   P50196;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   13-SEP-2023, entry version 94.
DE   RecName: Full=Type II methyltransferase M.Eco47II {ECO:0000303|PubMed:12654995};
DE            Short=M.Eco47II {ECO:0000303|PubMed:7607524};
DE            EC=2.1.1.37;
DE   AltName: Full=Cytosine-specific methyltransferase Eco47II;
DE   AltName: Full=Modification methylase Eco47II;
GN   Name=eco47IIM {ECO:0000303|PubMed:7607524};
OS   Escherichia coli.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE FUNCTION.
RC   STRAIN=RFL47;
RX   PubMed=7607524; DOI=10.1016/0378-1119(94)00796-u;
RA   Stankevicius K., Povilionis P., Lubys A., Menkevicius S., Janulaitis A.;
RT   "Cloning and characterization of the unusual restriction-modification
RT   system comprising two restriction endonucleases and one
RT   methyltransferase.";
RL   Gene 157:49-53(1995).
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 that recognizes the double-stranded sequence 5'-
CC       GGNCC-3', methylates C-? on both strands, and protects the DNA from
CC       cleavage by both the Eco47I and Eco47II endonucleases.
CC       {ECO:0000303|PubMed:12654995, ECO:0000305|PubMed:7607524}.
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   -!- 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; X82105; CAA57629.1; -; Genomic_DNA.
DR   AlphaFoldDB; P50196; -.
DR   SMR; P50196; -.
DR   REBASE; 3372; M.Eco47II.
DR   PRO; PR:P50196; -.
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   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00315; Cyt_C5_DNA_methylase; 1.
DR   CDD; cd04762; HTH_MerR-trunc; 1.
DR   Gene3D; 1.10.1660.10; -; 1.
DR   Gene3D; 3.90.120.10; DNA Methylase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR018117; C5_DNA_meth_AS.
DR   InterPro; IPR001525; C5_MeTfrase.
DR   InterPro; IPR031303; C5_meth_CS.
DR   InterPro; IPR009061; DNA-bd_dom_put_sf.
DR   InterPro; IPR000551; MerR-type_HTH_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   NCBIfam; TIGR00675; dcm; 1.
DR   PANTHER; PTHR10629; CYTOSINE-SPECIFIC METHYLTRANSFERASE; 1.
DR   PANTHER; PTHR10629:SF52; DNA (CYTOSINE-5)-METHYLTRANSFERASE 1; 1.
DR   Pfam; PF00145; DNA_methylase; 1.
DR   Pfam; PF13411; MerR_1; 1.
DR   PRINTS; PR00105; C5METTRFRASE.
DR   SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS00094; C5_MTASE_1; 1.
DR   PROSITE; PS00095; C5_MTASE_2; 1.
DR   PROSITE; PS51679; SAM_MT_C5; 1.
PE   3: Inferred from homology;
KW   DNA-binding; Methyltransferase; Restriction system;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..417
FT                   /note="Type II methyltransferase M.Eco47II"
FT                   /id="PRO_0000087875"
FT   DOMAIN          81..414
FT                   /note="SAM-dependent MTase C5-type"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT   ACT_SITE        153
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT                   ECO:0000255|PROSITE-ProRule:PRU10018"
SQ   SEQUENCE   417 AA;  47513 MW;  C399A49E00BDAFD3 CRC64;
     MLAWLLNMLK EEFSLSEVAD ILGVSKETLR RWDTAGKLVS QRNDENNYRF YKKEQLKNFE
     QAQFLFKSQW PDETKISNNV YTVLELFAGA GGMALGLEKA GLKSVLLNEI DSHACKTLRK
     NRPEWNVVEG DVSQVDFTPY RNTVDVLAGG FPCQAFSYAG KKLGFEDTRG TLFFEFARAA
     KEINPKVLLA ENVRGLLNHD AGRTLETIKN IITDLGYTLF EPRVLKAIFY KVPQKRERLI
     IVAVRNDLAD GIDYEWPSSY NKILTLKDAL KKGELYDSDV PESEGQKYPK RKAEILSMVP
     PGGYWRDLPE DIQKEYMLKS FYLGGGKTGM ARRLSWDEPS LTLTCAPAQK QTERCHPEET
     RPLTVREYAR IQTFPDEWVF EGPMSAKYKQ IGNAVPVNLS FAVGKSVVHL LDKINKR
//