ID D8G098_9CYAN Unreviewed; 527 AA.
AC D8G098;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=OSCI_2700004 {ECO:0000313|EMBL:CBN56038.1};
OS Kamptonema sp. PCC 6506.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Oscillatoriales; Microcoleaceae; Kamptonema.
OX NCBI_TaxID=272129 {ECO:0000313|EMBL:CBN56038.1, ECO:0000313|Proteomes:UP000004532};
RN [1] {ECO:0000313|Proteomes:UP000004532}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6506 {ECO:0000313|Proteomes:UP000004532};
RX PubMed=20675499; DOI=10.1128/JB.00704-10;
RA Mejean A., Mazmouz R., Mann S., Calteau A., Medigue C., Ploux O.;
RT "The genome sequence of the cyanobacterium Oscillatoria sp. PCC 6506
RT reveals several gene clusters responsible for the biosynthesis of toxins
RT and secondary metabolites.";
RL J. Bacteriol. 192:5264-5265(2010).
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};
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DR EMBL; CACA01000236; CBN56038.1; -; Genomic_DNA.
DR RefSeq; WP_007355251.1; NZ_CACA01000236.1.
DR AlphaFoldDB; D8G098; -.
DR REBASE; 28702; M.Osp6506ORF2700004P.
DR OrthoDB; 467945at2; -.
DR Proteomes; UP000004532; 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 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; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR038333; T1MK-like_N_sf.
DR PANTHER; PTHR42998:SF1; TYPE I RESTRICTION ENZYME HINDI METHYLASE SUBUNIT; 1.
DR PANTHER; PTHR42998; 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.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:CBN56038.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004532};
KW Transferase {ECO:0000313|EMBL:CBN56038.1}.
FT DOMAIN 21..157
FT /note="N6 adenine-specific DNA methyltransferase N-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF12161"
FT DOMAIN 170..484
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 527 AA; 59801 MW; AE497D5BB296F060 CRC64;
MVVRKKSTIK QNGKGANLGF EEKLWAAADK LRGQMDSAEY KHIVLGLIFL KSISDQFEER
YDQLEIWGLD SSSQFSLPDG NDKFTEEQDC GLTDNRFEIP ESVRWSNLKS QANLLNIGNL
IDEAMMVIEK ENSSLSSILP KAYSSLDPRR LSELIAIINT IDLGEKNSSS KDILGRVYEY
FLGRFANWEG KGGEFYTPQS VVKLLVEMTQ PYQGKIYDPC CGSGGIFVQS EKFVLAAGGK
ANDILIYGQE SNQTTWRLCK MNLAIRGIEA NIGECNADTL NSDLHPDLKA DFILANPPFN
MSDWEGYRLH QDQRWHYGIP PASNANFAWI QHIIYHLSDR GIAGFVLSNG SLNHGQVEGE
IRSKIIEDDL IDCIVALPSQ LFYTTQIAAS LWFIAKNKRD DKWRDRAGES LFIYAANFGQ
MADRTHRTIA DDEIAKIANT YNLWRSRDRI NEYKDIPGFC KSATLEEIRY HKMSLVPGRY
VGFDENLTKQ WDITELRAEF TDVENRIAEI DRASNSALNV LKELLYG
//
