ID   A0A0G1VEZ5_9BACT        Unreviewed;      1414 AA.
AC   A0A0G1VEZ5;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=UY35_C0003G0067 {ECO:0000313|EMBL:KKW04890.1};
OS   Candidatus Saccharibacteria bacterium GW2011_GWC2_48_9.
OC   Bacteria; Candidatus Saccharibacteria.
OX   NCBI_TaxID=1619071 {ECO:0000313|EMBL:KKW04890.1, ECO:0000313|Proteomes:UP000034790};
RN   [1] {ECO:0000313|EMBL:KKW04890.1, ECO:0000313|Proteomes:UP000034790}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKW04890.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LCPR01000003; KKW04890.1; -; Genomic_DNA.
DR   STRING; 1619071.UY35_C0003G0067; -.
DR   PATRIC; fig|1619071.3.peg.269; -.
DR   Proteomes; UP000034790; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF07669; Eco57I; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   SMART; SM00487; DEXDc; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR   PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR   PROSITE; PS00092; N6_MTASE; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000313|EMBL:KKW04890.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Helicase {ECO:0000313|EMBL:KKW04890.1};
KW   Hydrolase {ECO:0000313|EMBL:KKW04890.1};
KW   Nucleotide-binding {ECO:0000313|EMBL:KKW04890.1}.
FT   DOMAIN          164..337
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51192"
FT   COILED          751..789
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1414 AA;  162032 MW;  5C04C063355F11AA CRC64;
     MLCNMHDNTT DNSQLTGIPK IKTTKVVYPQ IYSYILPDEA DNEGSQKIGY TERKDVDKRI
     YEQTHTAAKR LRFEKQWSAP AFYADQQNDF KDTDFHKFLV KSDVRHRPDL GKEWFYFNGT
     PEKSKQLFDT FRQHGFAALQ DGGKKIPYEL RSEQQEAVEK AIEYFQAHEN GEFLWNAKPR
     FGKTLASYDL AKRLDAKKVL IVTNRPAIAN SWFDDFDTFI DGYYFISDTA SLADRKSLTR
     EQFNVIEGSD KPMITFLSLQ DLKGSKYFGG SHDKLRWVAD LEWDLLVIDE AHEGVDTGRT
     DDAFTIVKRS HTLHLSGTPF KAIANQKFPR DAIYNWTYLD EQKEKQKELA EGESGPHTDL
     PDLRLYTYRI SQMIADEVNE GIDIDDETRD YAFDLNEFFA TKNQKFVHED DVREFLRNLS
     TNEKYPFSTP ELRDQLRHTF WYVGNRVESV KALEQLLKQD EVFKDYKVVV AAGDGRSFDE
     EEADFKGNER SFDKVKKAIA ENSRTITLSC GQLTTGVTIK EWSAVLMLTD IKTPSQYMQA
     AFRAQNPYRF TEDGEVKAKK SAYLFDFAPT RVLEIYDTFA NALNPSAANG EITEAERKDN
     IKELLNYFPV ISEDVDGKMV ELDAEKVLTF PNALAATEIV QARFMTNLLF NDNIKGVFHF
     PKEVEEILDK MPVEKNKRAE STKQTLDLDD ARKLEQEKQT KINENTGVIL GEKIYRANID
     RVVDNVLDQA TPEETIDMLP AKVEALVEAP IAKLKEQYKW TAAEADEARK EATEKIKLVV
     AEFENSEDKD PEALKQSLAS VIEQDLVQAK VEQQETKVVE TVQKSKEEEV REHLRAFTRT
     IPMFVMANSS REVITIDNFD DQISDEDFID LTNITKEEFH KLRDGFEYTD DNGERQRFEG
     VFHKYKFNAS IAEFVAEKQK RANYFETDED IFELIPNQKN NQIFTPRKVV KMMVDGLEKE
     QPELFRRTDS TFIDLYMKSG MYITEIVKKL FTNTRHNYSS DAECLKHILE NQVYGLAPTS
     VLHGITTSYI FGFDTEHTIS SNNFIQHDLL PQAKDGTATT KLAQLFGNGG SMMKFDAVVG
     NPPYQDVATG DSTQAPPIYH LFLDSAYQLA YSACLISPAR FLFNAGATPS AWNKKMLNDN
     HLKVLSFEQD SSKVFPSTDI KGGVVVTFRD ANSDFGSIGV YTSFPELNSI LKKVESVSER
     SLSEIIYGQN AYQFTKTLHD ENPTAKSNMS KGHERDVITN AFETLSYVFY DQKPNDDESY
     IQIAGRLNNV RKNKFIKSSY IKAHENLNKW KVFIPKANGS GRLGEVLSTP LIAEPLVGHT
     QTYVSIGKFD SRDEADACMK YIKSKFTRAM LGILKITQDN PAPKWKCVPL QDFTPNSDIN
     WSKSIPEIDQ QLYRKYNLSP EEIDFIETRV KAME
//