ID   A0A9C7S8S0_9GAMM        Unreviewed;       912 AA.
AC   A0A9C7S8S0;
DT   03-MAY-2023, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 1.
DT   02-APR-2025, entry version 12.
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=ENG96_00295 {ECO:0000313|EMBL:HDH07902.1};
OS   Gammaproteobacteria bacterium.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=1913989 {ECO:0000313|EMBL:HDH07902.1, ECO:0000313|Proteomes:UP000886286};
RN   [1] {ECO:0000313|EMBL:HDH07902.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=HyVt-263 {ECO:0000313|EMBL:HDH07902.1};
RX   PubMed=31911466;
RA   Zhou Z., Liu Y., Xu W., Pan J., Luo Z.H., Li M.;
RT   "Genome- and Community-Level Interaction Insights into Carbon Utilization
RT   and Element Cycling Functions of Hydrothermarchaeota in Hydrothermal
RT   Sediment.";
RL   mSystems 5:e00795-e00719(2020).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an
CC         N(6)-methyl-2'-deoxyadenosine in DNA + S-adenosyl-L-homocysteine +
CC         H(+); 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:ARBA00047942};
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:HDH07902.1}.
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DR   EMBL; DRCZ01000015; HDH07902.1; -; Genomic_DNA.
DR   Proteomes; UP000886286; 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:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR   GO; GO:0032259; P:methylation; 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; IPR051537; DNA_Adenine_Mtase.
DR   InterPro; IPR003356; DNA_methylase_A-5.
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.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:HDH07902.1};
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..167
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          184..487
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          660..687
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   912 AA;  103123 MW;  FB469713DE388FC3 CRC64;
     MSPTKLTLAR LENLLLTACD DLRGSMDASE YKEYIFGMLF LKRASDLFDQ RRAELKKELA
     AKGMSVEDIA IELNDSDNYS GKYFYVPERA RWNQGWDEEV TKDGVTETIH HPALKHVKQN
     VGTTLNKALE AIEDANVDAL QDVLKGINFN RKIGQRTLDD NTLADFVLNF EKIPLKDEDF
     EFPDLLGAAY EWLIKFFADS AGKKAGEFYT PAEVVRICVE ICDPQKDMRV YDPTAGSGGM
     LIQTRDYLRE CGGDSSEISL FGQEKIGTTW SICKMNMLLH GISHADIRQE DTIKEPQHLD
     GETNELMRFD RVLANPPFSQ NYSKTNLKFP GRFPVMMPEK GKKADLMFVQ HMLSVLKHDG
     RLATVMPHGV LFRGGEERAA RKHFIEKGYL EAIIGLPSNL FYGTGIPACL LIMNKQGAAQ
     RDHVLFINAD REYREGKAQN HLRPEDIDKI VHAYRQGEDI PAYARRVPMA EIAAEDYNCN
     IRRYVDNAPP PEPHDVRAHL HGGVPIVEVD ALQHFWSNYP GLREDCFAAR DETYLDLADN
     IADKRSIADF VTNHPGVIER HETFMQQVEA WWRDNLPIVE ALAPVPENQH ENSGNVYLMR
     RKLLESIAEV LLGQDLLTPY QVRGAFANYV NLLKADFKSI AASGWGPQLI PDEDILQSQF
     PEVLEEMDQA QTRLAELQAL FAAADEDDFE DTEDTGVMAG SEVKSKNDKL KKFNGEWKAQ
     LKELKALATN IFTEIKVAGL LPTGAKKGYY CTEGLTQKEP QFANGGRILA LASQVKHQSD
     FVEPLTETME AGQLAWELAQ SIEQSLTCHK AREDEAKEQK AIIKGNQNKR DELVEKAREK
     ISTDEARTVI IERLRQVLLS TYQAYLKADL RACIKGIENL WHKYAVTAKT IEVARDAASK
     QLKKFLVELG YE
//