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
//