ID A5I1A4_CLOBH Unreviewed; 741 AA.
AC A5I1A4; A7G305;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 90.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=CBO1266 {ECO:0000313|EMBL:CAL82816.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL82816.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL82816.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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 Evidence={ECO:0000256|ARBA:ARBA00001279};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; AM412317; CAL82816.1; -; Genomic_DNA.
DR RefSeq; WP_011948890.1; NC_009698.1.
DR RefSeq; YP_001253790.1; NC_009495.1.
DR RefSeq; YP_001387170.1; NC_009698.1.
DR AlphaFoldDB; A5I1A4; -.
DR GeneID; 5187022; -.
DR KEGG; cbh:CLC_1304; -.
DR KEGG; cbo:CBO1266; -.
DR PATRIC; fig|413999.7.peg.1252; -.
DR HOGENOM; CLU_022175_0_0_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR Gene3D; 3.90.220.10; Adenine-n6-DNA-methyltransferase Taqi, Chain A, domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR023135; N6_DNA_MeTrfase_TaqI_C.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR025931; TaqI_C.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF07669; Eco57I; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CAL82816.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 371..483
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
FT DOMAIN 564..681
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 741 AA; 88427 MW; 9F8DFD691CD32458 CRC64;
MGGSYNLYKI KDISCISKYC NCLQLVFEDL YDLKKYFNEN KTLFCNKALY VLINKIIISK
IFMEKNNITG ELAKKNIKYY ALTLDTINLV NLVFDNVDKR FLESIFKDNI KYEYINPSYY
SLDKEDFLHY EDNIFYRYNI FLNKIIDEIN GFDFIHSSCE IGEIYEKIIA KEYKKSMGIF
YTPEYIIDYI LENVFYEFSP LENPFVKLID ISAGAGYFII KAYDKLKKVF TENIQNLQEK
YKQNIYTIRK KGQSIKVTGE YYWQKENLHY HIINNCIYAA DIDIYAIQIT TINLLLKDTK
SYVGKVNVAN CDSLIRWEKD FNPTIKFLDN KYKYKTYKIK NKGIEEAVNY KEKEVCNWKT
YFKLYKFWRK KFDYIIGNPP WVSLSRKNKK ACWKNSLEYY IKNYGQCVHS PNLFEYFIKR
ALEKTKKDGY LAFVVPINFS RNSQYIQLRN EILNKYEIKN LFFNIAFSGV ITDGMVFILK
KNKKCFNEIK IKVQGKDEYK IDKNELFSCN EYGFTFNNND FDEKIKNKIL ENSSFLSEIS
DTFTGFIGDC KNIYKENVDK SYIKIYKGKN IKKFICYSYF YYDFKDENIK GGTKDLKKLK
YKGKILVRKT GNEIIAAYDE EGIIIEQSLY GIINLKQNFS HKYILGILNS QLMSWYYKKY
LITNKDSTPQ LKKYRLNKIP IKNCNKNVQE EVEILSDKIF QALKNENVKE IDYYYKILNQ
KVFSIYGIDD IKIIRYIIND K
//
