ID A0A140DWT7_9FIRM Unreviewed; 508 AA.
AC A0A140DWT7;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=AALO17_19800 {ECO:0000313|EMBL:AMK55114.1};
OS Faecalibaculum rodentium.
OC Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC Erysipelotrichaceae; Faecalibaculum.
OX NCBI_TaxID=1702221 {ECO:0000313|EMBL:AMK55114.1, ECO:0000313|Proteomes:UP000069771};
RN [1] {ECO:0000313|EMBL:AMK55114.1, ECO:0000313|Proteomes:UP000069771}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Alo17 {ECO:0000313|EMBL:AMK55114.1,
RC ECO:0000313|Proteomes:UP000069771};
RX PubMed=26877770; DOI=10.1186/s13099-016-0087-3;
RA Lim S., Chang D.H., Ahn S., Kim B.C.;
RT "Whole genome sequencing of "Faecalibaculum rodentium" ALO17, isolated from
RT C57BL/6J laboratory mouse feces.";
RL Gut Pathog. 8:3-3(2016).
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};
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DR EMBL; CP011391; AMK55114.1; -; Genomic_DNA.
DR RefSeq; WP_067558382.1; NZ_CP011391.1.
DR AlphaFoldDB; A0A140DWT7; -.
DR STRING; 1702221.AALO17_19800; -.
DR REBASE; 139409; M.Fro17ORF19800P.
DR GeneID; 78478584; -.
DR KEGG; fro:AALO17_19800; -.
DR PATRIC; fig|1702221.3.peg.1927; -.
DR OrthoDB; 9814572at2; -.
DR Proteomes; UP000069771; Chromosome.
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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR Gene3D; 1.20.1260.30; -; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR022749; D12N6_MeTrfase_N.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR Pfam; PF12161; HsdM_N; 1.
DR Pfam; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:AMK55114.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000069771};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AMK55114.1}.
FT DOMAIN 6..124
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 151..467
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 508 AA; 58029 MW; D2F83FEB6A0300FA CRC64;
MITGELKNKI DSLWGIFWTG GLTNPLDVIE QMTYLMFIHD LDATDLRHQK EALMLGLDSK
SMFDGEVTIN DRVVSKQDLK WSRLGDMEPR QMYDTMANAV FPFIKGLDDG NDSAYSTYMQ
DAIFKIPTPL MLDKIMTAMN GIYELMEEDK SGDTRGDVYE YLLSKIATAG VNGQFRTPRH
IIKMMVELMD PRPDDTICDP AAGTSGFLVE AAEYLKNVKK EDVLFDPENR KHYMNDMFTG
FDMDRTMLRI GAMNMMTHGI EHPNIEYRDS LTDQNPDRDK YSLILANPPF KGSLDYDSVS
DDLRDIVNTK KPKTELLFLE LFLKMLKKGG RTACIVPDGV LFGSSKAHKA IRKELIENNK
LQAVISMPSG VFKPYAGVST AVLVFNKTGY GGTDKVWFYD MKNDGFSLDD KRSKIEANDI
PDIVERFRNL DKEVDRKRTD QSFLVDKEEI VKNDYDLSIN KYKEIEYEKV EYEPTSVILG
KINDLQTEIE AGLKELEKML KEQEPGDE
//
