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Database: UniProt
Entry: A0A0P4UX49_9CYAN
LinkDB: A0A0P4UX49_9CYAN
Original site: A0A0P4UX49_9CYAN 
ID   A0A0P4UX49_9CYAN        Unreviewed;       704 AA.
AC   A0A0P4UX49;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-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=NIES2104_66680 {ECO:0000313|EMBL:GAQ00103.1};
OS   Leptolyngbya sp. NIES-2104.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya.
OX   NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAQ00103.1, ECO:0000313|Proteomes:UP000052243};
RN   [1] {ECO:0000313|EMBL:GAQ00103.1, ECO:0000313|Proteomes:UP000052243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2104 {ECO:0000313|EMBL:GAQ00103.1,
RC   ECO:0000313|Proteomes:UP000052243};
RX   PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA   Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA   Kawachi M.;
RT   "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT   and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL   DNA Res. 22:403-412(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   -!- 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:GAQ00103.1}.
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DR   EMBL; BBWW01000004; GAQ00103.1; -; Genomic_DNA.
DR   RefSeq; WP_059002670.1; NZ_BBWW01000004.1.
DR   AlphaFoldDB; A0A0P4UX49; -.
DR   STRING; 1552121.NIES2104_66680; -.
DR   InParanoid; A0A0P4UX49; -.
DR   OrthoDB; 467945at2; -.
DR   Proteomes; UP000052243; 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   CDD; cd02440; AdoMet_MTases; 1.
DR   Gene3D; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42998; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 1.
DR   PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDVIIP M PROTEIN-RELATED; 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   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000313|EMBL:GAQ00103.1};
KW   Transferase {ECO:0000313|EMBL:GAQ00103.1}.
FT   DOMAIN          9..146
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          156..437
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          556..609
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          664..691
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   704 AA;  80365 MW;  189E8BE516410F6B CRC64;
     MTPDDLKQLE ATLWKSADDL RANSDLKSSE YATPVLGLIF LKFADNKYRQ YAAEIQQEYE
     KLKGGRREKL LSEIAIEKCG FYLPDHARYD YLLTLPEEEN IAQALKVAMM AIEEHKPELK
     GVLPQDEYFR LVRGNDKSIP NRLLKNFSNI PADATGDMFG QIYQYFLAEF ALAEGQGGGE
     FFTPDTVVRL MVEIVEPRRG KLLDPACGSG GMFVQSRRFI QEHDREDGSD PNDFFVYGQE
     KTLETVKLAK MNIAVSGLKG DVRQANTYYE DPFNGFGEFD YVLANPPFNV DDVNLSRVEA
     DRRFNSYGIP RNKSKPTKKE QGNETVPNAN YLWINLFATS LKPKGRAALV MANSASDARH
     SEADIRETLI KQNLIYGMLT LPSNMFYTVT LPATLWFFDK GKSDDRILFI DARNVFTQID
     RAHREFSPEQ VSNLAVISHL HRGKRHRFIH LVDRYFQQGM EKLIENRVQV EPVSQQLIAV
     LEDETDDTKG KEAALGFVDS WRSLDALKTQ YQNYRDRYPA PPSNHEDSQT IEERNLAQHQ
     LSGAFEPFFV ELHSGLKQLD KTVRSHEAML AEKAKQAGTQ KRSLIDRQIK ALKTTLEELH
     AEVKSAESFF AHVGWLQERF PEAKYENVTG LCKLATLEEV EEQDYSLNPG RYVGVVIEED
     GKTEEEFITE ILEMNQELEK LNREAHQLEG IIAHNVKQLA GEDS
//
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