ID A0A3A9YM77_9ACTN Unreviewed; 694 AA.
AC A0A3A9YM77;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=D7294_27500 {ECO:0000313|EMBL:RKN37488.1};
OS Streptomyces hoynatensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1141874 {ECO:0000313|EMBL:RKN37488.1, ECO:0000313|Proteomes:UP000272474};
RN [1] {ECO:0000313|EMBL:RKN37488.1, ECO:0000313|Proteomes:UP000272474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 29097 {ECO:0000313|EMBL:RKN37488.1,
RC ECO:0000313|Proteomes:UP000272474};
RX PubMed=24243968; DOI=10.1099/ijs.0.055640-0;
RA Veyisoglu A., Sahin N.;
RT "Streptomyces hoynatensis sp. nov., isolated from deep marine sediment.";
RL Int. J. Syst. Evol. Microbiol. 64:819-826(2014).
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 -!- SIMILARITY: Belongs to the type-I restriction system S methylase
CC family. {ECO:0000256|ARBA:ARBA00010923}.
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:RKN37488.1}.
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DR EMBL; RBAL01000024; RKN37488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A9YM77; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000272474; Unassembled WGS sequence.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004519; F:endonuclease activity; 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; cd16961; RMtype1_S_TRD-CR_like; 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; IPR000055; Restrct_endonuc_typeI_TRD.
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; PF01420; Methylase_S; 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 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Endonuclease {ECO:0000313|EMBL:RKN37488.1};
KW Hydrolase {ECO:0000313|EMBL:RKN37488.1};
KW Nuclease {ECO:0000313|EMBL:RKN37488.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000272474};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747}.
FT DOMAIN 136..439
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 518..674
FT /note="Type I restriction modification DNA specificity"
FT /evidence="ECO:0000259|Pfam:PF01420"
SQ SEQUENCE 694 AA; 75887 MW; 39B03502667C43D2 CRC64;
METESQAAHA AHVVDRLWRA YAPYQRGRNT SDDVASMLAI LVLAGFVESA GESGDTFVTL
WRRAVEEARI GLSPLKDLRT ALKSAGRHPR FPVRNARYFD AGVLGLDEGP EDAPWMAAFL
TALWRPPTVT EAGLPEVCEL LLERHAQEGT SSAGEFYTPR AVARLITALA SPRPGDRMLD
PACGSGSLLA AAAQRTRRAG RVDGDSYEAY ATDRGNPRLA MMNLAIHGVE GPVVHAADPV
SLFRSRGGSP ADRVVSNPPF NQRIEEVDIV RWPFGVPPRS NANFAWLQLA WARLSTDGIA
VLIMPPRAAW SEGSEAAIRA NMIRNGTLLS IISLPAHLFA HTAIPVHVWV LARDKSHHLP
ADARRSVLFI DASRLGTRAP RQRNTLTAAD VERISGRLHA WRRSPRSTPD EPGFSRSVSH
EEILRNEASL DPRLYVDAES AGPRTAPEMS RLLDELIRHD QTASGSSADL WQSLDKCAQL
VRDAVGLPRL PLRRIVEGPV GGDADDQTPG EFLAGPSGSL IRAEEYVDSG GIPVVMPKDL
TGDDFSTESI RYITEEKAHG LGRYRLRPGD VVLARRGELG RCAVVREEQV GWVCGTGCFV
LRPPAWLNAH YLVAYLRGRE ARTWLEAHST GSMTMKTISL KVLGELPVAL PDLGTQQAIA
RAMKQLDERE RLLREQLALT REIRGGAVHG LFSG
//