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Database: UniProt
Entry: A0A1F3LD68_9BACT
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ID   A0A1F3LD68_9BACT        Unreviewed;       509 AA.
AC   A0A1F3LD68;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
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=A2X18_08665 {ECO:0000313|EMBL:OFY38736.1};
OS   Bacteroidetes bacterium GWF2_40_14.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1797347 {ECO:0000313|EMBL:OFY38736.1, ECO:0000313|Proteomes:UP000176561};
RN   [1] {ECO:0000313|EMBL:OFY38736.1, ECO:0000313|Proteomes:UP000176561}
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   -!- 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:OFY38736.1}.
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DR   EMBL; MEOK01000038; OFY38736.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F3LD68; -.
DR   STRING; 1797347.A2X18_08665; -.
DR   Proteomes; UP000176561; 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   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; IPR004546; Restrct_endonuc_T1M.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   NCBIfam; TIGR00497; hsdM; 1.
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   Coiled coil {ECO:0000256|SAM:Coils};
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          11..149
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          164..475
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          472..506
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   509 AA;  57336 MW;  68488D037057BD09 CRC64;
     MATKTTQAEI NRIVWKACDT FRGVIDPSQY KDYILTMLFL KYVSDVHKSK FHEHLQKYDG
     NLERAERAMR HERFIVPKTS SFDFLYEFRN ESNIGELINI ALADLEDANR EKMSSEDGSG
     IFRNIDFNSS NLGDAKDKNT RLKNLILDFS DEKMIFDESH LEGNDIIGDA YMYLVSTFAS
     ESGKKAGDFF TPAEVSTLLA KLTKSKPGAR ICDPTCGSGS LLIKAGMEVD GDNFSLYGQE
     LNGSTWALAM MNMFLHGFDS AIIRWGDTLR TPKLKEGDLL MKFDTVVANP PFSLDKWGAD
     EAEHDSYQRF WRGVPPKSKG DWAFISHMIE VAHEKTGKVG VVVPHGVLFR GSSEGKIRKQ
     TVEENILEAV IGLPANLFFG TGIPAAIVIF NKGKKNKNVL FIDASKEFEN GKNQNKLRSQ
     DIEHIVSTYC KFSAGELKEG TAEDKYAYVA TPAEIAENDY NLNIPRYVDT FEEEEEIDIV
     AVQKEIDTLE IELKEVQAKM KQYLAELGF
//
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