ID A0A0L0KRJ7_9ACTN Unreviewed; 667 AA.
AC A0A0L0KRJ7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=IQ63_00300 {ECO:0000313|EMBL:KND40335.1};
OS Streptomyces acidiscabies.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=42234 {ECO:0000313|EMBL:KND40335.1, ECO:0000313|Proteomes:UP000037151};
RN [1] {ECO:0000313|Proteomes:UP000037151}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 4445 {ECO:0000313|Proteomes:UP000037151};
RA Harrison J., Sapp M., Thwaites R., Studholme D.J.;
RT "Genome sequencing of plant-pathogenic Streptomyces species.";
RL Submitted (JUL-2014) 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:KND40335.1}.
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DR EMBL; JPPY01000002; KND40335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L0KRJ7; -.
DR PATRIC; fig|42234.21.peg.66; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000037151; 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 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 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; 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:KND40335.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037151};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:KND40335.1}.
FT DOMAIN 153..371
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 491..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 491..508
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 667 AA; 69902 MW; 5C0ECAFD5F042E72 CRC64;
MTAAEISRLA GVTRATVSNW RRRHDDFPSP TGGTDSSPLY DWGSVRVWLA MRGHTAAANP
REEFRTALRL HAQGGVALLP VILVASRHTP EDLTALMDLT DADLATRVTA EAPDTAALEP
ADGAVLRALL RCVRDEGGRA ALGILAEREL EDSAASGVYR TPAPLADLAA RLLPQEACRV
LDPACGSGTL LEAAARYGAT ELYGQDVLPV QVQRSTVGLL LEDPDAEITI KSGDSLRSDA
FPGLMADAVL CNPPYGDRDW GHDELAYDPR WAYGVPARGE SELAWVQHAL AHLAPGGWAV
LILPPATATR VAGRRIRAEL VRGGAVRAVI ALPAGAAPPL HVGLQIWALQ RPEPGGAERK
SVLFVDTTEA GAEVALPHWR AFTASPDVFT GESGVARAVP VVDLLDDVVD LTPARRVRVS
RTDVDPAELA AVVDAGRREL AGAAESLVRG VGLTEWEAKG TSARGWRTAT ASDLARGGAL
TLLRTVPGTK GQTADSGAVL TSSDIGGGTA PSGDPAEVGV ENAPIVAAGD VLMRSVAGGT
GPMARVADES DVGALLGPNV HLLRPDPVRL DPWFLVGFLD SADNIAGAST GSTVLHVAPG
RLRIPLMPLE EQRRYGEAFR RLYVLRADAR RTAQLAEETA GLLAEGLTCG ALLPPSSARD
SPDVDSS
//