DCM_ECO57
ID DCM_ECO57 Reviewed; 472 AA.
AC P0AEE0; P11876;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=DNA-cytosine methyltransferase;
DE EC=2.1.1.37;
DE AltName: Full=Probable type II methyltransferase M.Eco9331DcmP {ECO:0000303|PubMed:12654995};
DE Short=M.Eco9331DcmP {ECO:0000303|PubMed:12654995};
GN Name=dcm; OrderedLocusNames=Z3054, ECs2699;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
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: This methylase recognizes the double-stranded sequence 5'-
CC CCWGG-3', methylates C-2 on both strands.
CC {ECO:0000250|UniProtKB:P0AED9}.
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; AE005174; AAG56975.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36122.1; -; Genomic_DNA.
DR PIR; C85814; C85814.
DR PIR; C90966; C90966.
DR RefSeq; NP_310726.1; NC_002695.1.
DR RefSeq; WP_001157239.1; NZ_SEKU01000025.1.
DR AlphaFoldDB; P0AEE0; -.
DR SMR; P0AEE0; -.
DR STRING; 155864.EDL933_2969; -.
DR REBASE; 232038; M.Sen4024DcmP.
DR REBASE; 232756; M.Sen4839DcmP.
DR REBASE; 256726; M.Ssp9304ORF1801P.
DR REBASE; 5031; M.EcoO157DcmP.
DR REBASE; 5589; M.EcoKO157DcmP.
DR EnsemblBacteria; AAG56975; AAG56975; Z3054.
DR EnsemblBacteria; BAB36122; BAB36122; ECs_2699.
DR GeneID; 913056; -.
DR KEGG; ece:Z3054; -.
DR KEGG; ecs:ECs_2699; -.
DR PATRIC; fig|386585.9.peg.2828; -.
DR eggNOG; COG0270; Bacteria.
DR HOGENOM; CLU_006958_0_1_6; -.
DR OMA; AGYRKGF; -.
DR PRO; PR:P0AEE0; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
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 3: Inferred from homology;
KW DNA-binding; Methyltransferase; Reference proteome; Restriction system;
KW S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..472
FT /note="DNA-cytosine methyltransferase"
FT /id="PRO_0000087914"
FT DOMAIN 87..457
FT /note="SAM-dependent MTase C5-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016"
FT ACT_SITE 177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01016,
FT ECO:0000255|PROSITE-ProRule:PRU10018"
SQ SEQUENCE 472 AA; 53465 MW; 3635BFC001CF94B4 CRC64;
MQENISVTDS YSTGNAAQAM LEKLLQIYDV KTLVAQLNGV GENHWSAAIL KRALANDSAW
HRLSEKEFAH LQTLLPKPPA HHPHYAFRFI DLFAGIGGIR RGFESIGGQC VFTSEWNKHA
VRTYKANHYC DPATHHFNED IRDITLSHKE GVSDEAAAEH IRQHIPEHDV LLAGFPCQPF
SLAGVSKKNS LGRAHGFACD TQGTLFFDVV RIIDARRPAM FVLENVKNLK SHDQGKTFRI
IMQTLDELGY DVADAEDNGP DDPKIIDGKH FLPQHRERIV LVGFRRDLNL KADFTLRDIS
ECFPAQRVTL AQLLDPMVEA KYILTPVLWK YLYRYAKKHQ ARGNGFGYGM VYPNNPQSVT
RTLSARYYKD GAEILIDRGW DMATGEKDFD DPLNQQHRPR RLTPRECARL MGFEAPGEAK
FRIPVSDTQA YRQFGNSVVV PVFAAVAKLL EPKIKQAVAL RQQEAQHGRR SR