ID Q72WX2_BACC1 Unreviewed; 438 AA.
AC Q72WX2;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 99.
DE RecName: Full=site-specific DNA-methyltransferase (cytosine-N(4)-specific) {ECO:0000256|ARBA:ARBA00012185};
DE EC=2.1.1.113 {ECO:0000256|ARBA:ARBA00012185};
GN OrderedLocusNames=BCE_5606 {ECO:0000313|EMBL:AAS44506.1};
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS44506.1, ECO:0000313|Proteomes:UP000002527};
RN [1] {ECO:0000313|EMBL:AAS44506.1, ECO:0000313|Proteomes:UP000002527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527};
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.,
RA Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(2004).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-
CC methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine;
CC Xref=Rhea:RHEA:16857, Rhea:RHEA-COMP:11369, Rhea:RHEA-COMP:13674,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:85452, ChEBI:CHEBI:137933; EC=2.1.1.113;
CC Evidence={ECO:0000256|ARBA:ARBA00001893};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. N(4)
CC subfamily. {ECO:0000256|ARBA:ARBA00010203}.
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DR EMBL; AE017194; AAS44506.1; -; Genomic_DNA.
DR AlphaFoldDB; Q72WX2; -.
DR REBASE; 7706; M1.BceSIII.
DR KEGG; bca:BCE_5606; -.
DR HOGENOM; CLU_027633_1_0_9; -.
DR Proteomes; UP000002527; Chromosome.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR017985; MeTrfase_CN4_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR PROSITE; PS00093; N4_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AAS44506.1};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 438 AA; 50414 MW; 4522B847DBAE448B CRC64;
MFKEELAIEK MEDEVVIEVE SLPMCIENGK TYAIKQPNPN SYTHGYFKYP CKFIPEIPRW
FMNKYLGEGK ASVLDPFSGS GTTLLESIIN GHDAYGTEID NFAKLLIKVK TTPLKLQEIN
EIIDWLERII KQYQESYMDY KNPVVPQINN LYHWFSEQNV QKLGLIKNEI NELENSAIID
FLNVCLASSI RKCSNADDVS PKPYVSSKIE KVPSDPFIVF PNIVNKYLAY MKEFLNYTLS
NKIGKVEILE GDALNIKANS KIDVAITSPP YINAFDYART LRLENLWLGL DSEETIKDKK
KSYVGTENIT TKKVKSELDL SILELSKQLK EVYYDIEKID QKRALIVKKF FEDMHKNLIE
VYNVLAEGGK YCIVIGNSSI RKINVESWSI ICDIARVIGF EIDTYFSYII KNHYLRIPRG
NKGGKINKDF VFVLKKST
//
