ID A0A0C1U6Y9_9CLOT Unreviewed; 583 AA.
AC A0A0C1U6Y9;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN ORFNames=U732_2902 {ECO:0000313|EMBL:KIE47573.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE47573.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE47573.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE47573.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KIE47573.1}.
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DR EMBL; AYSO01000014; KIE47573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C1U6Y9; -.
DR STRING; 29341.RSJ17_08215; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR003356; DNA_methylase_A-5.
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; PF02384; N6_Mtase; 1.
DR Pfam; PF12950; TaqI_C; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:KIE47573.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000031366};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KIE47573.1}.
FT DOMAIN 52..318
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 449..549
FT /note="TaqI-like C-terminal specificity"
FT /evidence="ECO:0000259|Pfam:PF12950"
SQ SEQUENCE 583 AA; 68836 MW; 7AD2D55E6389A1A3 CRC64;
MEVFRGKIKE LYILLLNPID AMFKLIAIEA LKKEFKIQDN KTIGEYYYDS LKTNKEKGIV
YTPYPIAKYI VENTVTSVDI INNPFIKIID PACGVGNLLI PCFLHLVNLY KENLKEINMK
NKLKLKEEDI NNHIIKNNIY GFDIDTIAIQ ILQIDLFYHS NSNISYNLIN EDFLLWKEDN
KFDIFIGNPP YVGPKFIDKD YSIVLKEKFK EIYKDKGDLS YCFFKKALDT LNNKGQISFI
TSRYFLESSS GKELRKALNE NTHIRRIIDF YGIRPFKGVG IDPVIIFMEK HKGSFGEVEV
IKPLSDKGKK NDKFYSSLFL NEGEEYNRFY IKQSTLQGER WILRSLEVKN IIKKIENKCN
VKLIDICTSH QGIITGCDKA FVVKNEIIED ENLEKELLKP WIKSSFIKQN QVNRQNSFII
YSDLIEDESK YPNCIEHISP YKEKLSSRRE CLRGVRKWYQ LQWGRNKEIF DDYKIIFPFK
ASSNKFSLDF DSYFSADVYA LKLKEKSEFT YEFLLFILNS KIYEFYFKTF AKKLGEDLYE
YYPNNLMKLL IPPINEISTY CEEELYKYFL LTTEEIELIN QSI
//
