ID A0A0N1NEG2_9ACTN Unreviewed; 812 AA.
AC A0A0N1NEG2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=OK006_6824 {ECO:0000313|EMBL:KPI05065.1};
OS Actinobacteria bacterium OK006.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1592326 {ECO:0000313|EMBL:KPI05065.1, ECO:0000313|Proteomes:UP000037912};
RN [1] {ECO:0000313|EMBL:KPI05065.1, ECO:0000313|Proteomes:UP000037912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OK006 {ECO:0000313|EMBL:KPI05065.1,
RC ECO:0000313|Proteomes:UP000037912};
RA Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT "Draft genome sequences for four Actinobacteria strains OK006 OK074 OV450
RT and OV320.";
RL Submitted (SEP-2015) 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 -!- 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:KPI05065.1}.
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DR EMBL; LJCU01000237; KPI05065.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1NEG2; -.
DR REBASE; 133745; M.AbaOK006ORF6824P.
DR PATRIC; fig|1592326.3.peg.8464; -.
DR Proteomes; UP000037912; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_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; PF02384; N6_Mtase; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF116734; DNA methylase specificity domain; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Methyltransferase {ECO:0000313|EMBL:KPI05065.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:KPI05065.1}.
FT DOMAIN 235..453
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 48..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 623..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..500
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 84842 MW; 25F0345C0C00F818 CRC64;
MPGEDSTEHP GRRFQSEARL DKHDTESIVK QIGRLDDRYN VLTVHYPTGP RGAEPHAMPQ
QPPAQPAPSA HVTAAEISRI AGVTRATVSN WRRRHDDFPA PSAGTETSPL YDLTAVQAWL
RGRGHTSTAS PTEELRTALR LLGPGSGVTA RLFPLVAAAS RRTPKELAEL AALPDDQLTA
RAEKTAGELP VAVPEAEPFR YGPDDVSVLR ALLGCVREAG AQAAVDVLAE RELDEGAASG
VYQTPEGLAL LMARLLPAGA SRVLDPACGS GTLLAAAARQ GARELFGQDS LPVQGRRTAV
RLLLAAPEAE TAIRVGDSLR ADAFPDITVD AVLCNPPFAD RDWGHDELAY DPRWAYGLPP
RFESELAWVQ HALAHLEPGG HAVMLLPPAL AFRSSGRRVR AELIRSGALR AVVSLPARAA
YPLHIGLQIW VFQRPEPGGT DRTTVLFVDG EGEQRDGAAG TPSATDTATA GAGTRGGSRP
RRSGSSSSAA SSAPASSASS ASASSFDWAG LTDRVLGQWA AFTTAPDTYA DEPGVARAVP
LVDLLDDVVD VTPARHVRAT AADIDPDALA RRVHDLHEQL AEQVAALAAA SASGGLQPSG
ASAREWRTAT VSDLARGGAL TVLRAATPST RGSKGPAAPT GENRPVLTAQ DISAANPPSA
GAVDIHADAT QSVAAGDVLV RAVAGGGDAA AMTRVADDRD AGALLGPHIH LLRPDPARLD
PWFLAGFLGA EDNIASASTG STLVHVTPGR LRVPLLPLEE QQRYGAAFRR VYELRAAVRR
TADLAADTAA TLTTGLTAGV LLPPDTPDNR SA
//
