ID A0A1Q5K731_9ACTN Unreviewed; 661 AA.
AC A0A1Q5K731;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=AMK31_28230 {ECO:0000313|EMBL:OKJ77319.1};
OS Streptomyces sp. TSRI0107.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703942 {ECO:0000313|EMBL:OKJ77319.1, ECO:0000313|Proteomes:UP000185813};
RN [1] {ECO:0000313|EMBL:OKJ77319.1, ECO:0000313|Proteomes:UP000185813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TSRI0107 {ECO:0000313|EMBL:OKJ77319.1,
RC ECO:0000313|Proteomes:UP000185813};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKJ77319.1}.
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DR EMBL; LIVZ01000011; OKJ77319.1; -; Genomic_DNA.
DR RefSeq; WP_073943568.1; NZ_LIVZ01000011.1.
DR AlphaFoldDB; A0A1Q5K731; -.
DR STRING; 1703942.AMK31_28230; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000185813; 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 CDD; cd02440; AdoMet_MTases; 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; IPR003356; DNA_methylase_A-5.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
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; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Methyltransferase {ECO:0000313|EMBL:OKJ77319.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185813};
KW Transferase {ECO:0000313|EMBL:OKJ77319.1}.
FT DOMAIN 132..372
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
SQ SEQUENCE 661 AA; 70301 MW; 9411D0F6681F5A2A CRC64;
MSTPDVVPVS LAEIARIAGV GRAAVSNWRR RHDSFPTRIG GTDVSPQFSL AEVEQWLRDN
GKLKDIGGRE LLWPRFEALG SRNESGLAVA EAARRMRSST AEITRPELSA QARELVAEAA
KLGRAGGPRE TFEFLLQRWL ETHVRQLSTT PPQLAALMAR IALAVRRGTG EGGLTVLDPA
CGTGHLAAAA TQEYDRPGLE LLACELDAAL AALASARLEF IAEDRDIRTR VATADALRED
PFAGTKADIV LCNPPFNERD WGYEELATDQ RWTHGLPPRT EPELAWVQHL LSHLKPGGAA
VVVLPPAVAS RKAGRRIRGS LLRTGVLRAV VSLPPGSAQP HSVSLQLWIL QAAADGFAAA
PASQDALLVD ATRFARPGSR EPSPDWDALG SFVLTAMATL NHPTQDLPEG AVCVPLLDLL
DDEVDVTPGR YTAAMTEPSP KELVAKWGEF GALLTDLADH AQHLSGLDFE AAAPQTTATV
GDLVKAGALT LRAGQQPLET VTPARGAAMP LLTIADLLHD GSPGGLLPTD SAHAIAEEGD
VVVAGVIRAF KAWVHEGPPV ALGPQLYALR VDPEKLDAHF LAGCLRAPAN GRQAGTHASS
SSRVDIRRLQ VLQLPLERQT VYAETFRRLK SFEALVIKAE SAGSGLVGDM SDRLAAGGLA
G
//