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Database: UniProt
Entry: A0A1G0WJN3_9BACT
LinkDB: A0A1G0WJN3_9BACT
Original site: A0A1G0WJN3_9BACT 
ID   A0A1G0WJN3_9BACT        Unreviewed;      1010 AA.
AC   A0A1G0WJN3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 18.
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=A2475_13595 {ECO:0000313|EMBL:OGV21439.1};
OS   Ignavibacteria bacterium RIFOXYC2_FULL_35_21.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798452 {ECO:0000313|EMBL:OGV21439.1, ECO:0000313|Proteomes:UP000177327};
RN   [1] {ECO:0000313|EMBL:OGV21439.1, ECO:0000313|Proteomes:UP000177327}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(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};
CC   -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC       {ECO:0000256|ARBA:ARBA00006594}.
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:OGV21439.1}.
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DR   EMBL; MHAY01000064; OGV21439.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0WJN3; -.
DR   STRING; 1798452.A2475_13595; -.
DR   Proteomes; UP000177327; 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   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR025931; TaqI_C.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF07669; Eco57I; 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.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          338..469
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          539..654
FT                   /note="Type II methyltransferase M.TaqI-like"
FT                   /evidence="ECO:0000259|Pfam:PF07669"
FT   DOMAIN          778..941
FT                   /note="TaqI-like C-terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF12950"
SQ   SEQUENCE   1010 AA;  117724 MW;  F9A5E7D804E15447 CRC64;
     MADNIADKLS NLVTDFRLAN FRGLNEWQTR QTYIEPFWEI LGWNVRKQSE VQGEKTESSK
     RPDYRFRKDN KTLFFVEAKK PNENLKENQN HIYQAKIYCW NGKVPLAVLT DFEEFRPFRA
     YGLPKKDDRE KGIIKQFDMK CEEYPDRAYD LLNTFGKEAV YGGSLNEIIQ KPTQVELRDT
     VDKHFLITLT KWRTDLAAQI AKINKFANEF DLAEAVQRIL DRLVFLRVLQ DRDIETEDFM
     CGISKSKTDE PYSAFLKICK AMAPKYNGLI FNPHPLSENL KIEGRLFKKI VQELDFEESP
     YRFDEIPVEM LGTIYERFLG DEISFSPRGK LVIDKKPEVR KAGGVYYTPQ YIVEYIVQNT
     VGKLLEICKT PEDVAKLKIL DPACGSGSFL LGAFNLLIKW HEDYFSANPT KIIEKTGKQY
     FNLAYLDDNN ITKLTAKMKG RILQNNLYGV DLDKQATEVA QMSLYIRVLE GLTGESIMQL
     GFHEALLPRL DGNIKCGNSL IGPDFINEGF FKLPEREKHK INPFDWEEQF PFIKEKGGFD
     AVIGNPPYLR VQGLQEYHSN IIQYLKNYYK SASTGNFDIY VIFIEKGFSL LNDRGYFGFI
     VPHKFFPSQF GENIRELITS KNALEEIVHF GSNKVFEQAD TYTCLLFLSK KKNKEFKIIE
     FGSGADLESE LNLIAKSKNK ESNKFKIGFI NHPEKSKDKW SFKSGETGGL IDKLLNSNFP
     KLNEITEKIF VGLQTSADDI YVLKVKDNKY LNYKNLKSFK LFSKSLNEEV EIEKGLIKPF
     LMGRDVYRYD DPIFRNYVIF PYTIINNSAV IMAKENIKEK FPNGWHYLLE NRKVLEGREN
     GKMNHDKFYA YIYPKNLAYF EQEKILIREL GDKPNMFFDN ENFYHTAKIY SLLLKDKSNL
     NYLYMLGILN SKILNFFIKN TSEIWGTSHK FKTQFLNPFP IPNLTDRKVK IDMVSLVDRM
     LKLHKDKQTA SDFDRKQIDQ YIAKTDKEID KLVYELYTLT EEEIKVVEGI
//
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