ID K8GDK7_9CYAN Unreviewed; 310 AA.
AC K8GDK7;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900, ECO:0000256|RuleBase:RU361257};
GN ORFNames=OsccyDRAFT_4423 {ECO:0000313|EMBL:EKQ66635.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ66635.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ66635.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ66635.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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 ECO:0000256|RuleBase:RU361257};
CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594, ECO:0000256|RuleBase:RU361257}.
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:EKQ66635.1}.
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DR EMBL; AJUB01000019; EKQ66635.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GDK7; -.
DR STRING; 864702.OsccyDRAFT_4423; -.
DR PATRIC; fig|864702.5.peg.4744; -.
DR eggNOG; COG0338; Bacteria.
DR HOGENOM; CLU_063430_3_0_3; -.
DR OrthoDB; 9805629at2; -.
DR Proteomes; UP000001332; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-UniRule.
DR Gene3D; 1.10.1020.10; Adenine-specific Methyltransferase, Domain 2; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR023095; Ade_MeTrfase_dom_2.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR012263; M_m6A_EcoRV.
DR InterPro; IPR012327; MeTrfase_D12.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00571; dam; 1.
DR PANTHER; PTHR30481; DNA ADENINE METHYLASE; 1.
DR PANTHER; PTHR30481:SF3; DNA ADENINE METHYLASE; 1.
DR Pfam; PF02086; MethyltransfD12; 1.
DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1.
DR PRINTS; PR00505; D12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000256|RuleBase:RU361257};
KW Reference proteome {ECO:0000313|Proteomes:UP000001332};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691,
KW ECO:0000256|RuleBase:RU361257};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361257}.
SQ SEQUENCE 310 AA; 36228 MW; A4BCA0A0C5C7D2EC CRC64;
MPFLPTTRHR IGIPPLKCQG IKTKLVPFIL SQIHWQASTT ARWIEPFLGS GAVVFNLAPD
RALLTDSNQH LIRFYQAIQQ QIITQASVRD FLTHEGAKLH QLGAEFYYTV RDRFNQDHHP
LDFLFLNRAC FNGLMRFNSR GHFNVPFCHK PNRFSSSYIT KIVNQVGWVA QQMHGKDWEF
RVADWRESLQ NTQSEDFVYL DPPYIGRHTD YFNAWNQADA EELAAIAHQL PGGFALSMWL
ENQHRKNPHI QQCWSQTRLR VCQHFYHVGS QETWRGAVYE ALLIKPGYEA EENVSEKIVR
EMGKVREMRC
//
