ID A0A2S1Z317_9ACTN Unreviewed; 791 AA.
AC A0A2S1Z317;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=DDQ41_19640 {ECO:0000313|EMBL:AWK10745.1};
OS Streptomyces spongiicola.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1690221 {ECO:0000313|EMBL:AWK10745.1, ECO:0000313|Proteomes:UP000245051};
RN [1] {ECO:0000313|EMBL:AWK10745.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HNM0071 {ECO:0000313|EMBL:AWK10745.1};
RA Zhou S., Huang X.;
RT "Complete genome sequence of the Type Strain of Streptomyces spongiicola
RT HNM0071, the producer of staurosporine.";
RL Submitted (MAY-2018) 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};
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DR EMBL; CP029254; AWK10745.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1Z317; -.
DR REBASE; 251918; M1.Ssp0071ORF19640P.
DR KEGG; sspo:DDQ41_19640; -.
DR OrthoDB; 9784823at2; -.
DR Proteomes; UP000245051; Chromosome.
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 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; 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; 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:AWK10745.1};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000313|EMBL:AWK10745.1}.
FT DOMAIN 184..395
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT REGION 387..427
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 547..612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..791
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 775..791
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 791 AA; 80534 MW; E92CB5181754ACDB CRC64;
MPETAAHVTA AEISRIAGVT RATVSNWRRR HADFPAPTAG TDTSPLYDLG AVRAWLGSRG
HTRVADPREE LRTAVRLHAS DPDGTTGRMA FVLTLARRPA DRTAALAGLE DAEVAGLTDA
ELAARASGEV AGLLASLPGP APASPLFSAS DGTALRALLR CVREAGAPAA LTVLAERELD
DSAATGVYGT PEPLARLVAA LLPAGAARVL DPACGSGALL AAAAGRGAGE LLGQDSVPVQ
ARRAAVGLSL AAPRAEVTVR IGDSLGADAF DGLTADAVVC NPPYGDRDWG HDRLAYDPRW
AYGVPGRSES ELAWVQHCLA HLVPGGRAVL ILPPATASRA SGRRIRAELV RSGAVRAVLA
LPPGAAPPLH VGLHLWVLSR PEPGGPERKS VLFADPAGAP PTDGGAPPSG TGARAAGMPR
TGTGPSRAPI DWAGLTARTL AHWEAFTADP DRFAAEPGTA RTVPVVDLLD DLVDLTPARR
VRTSHRDVDP AELSARTETG RRELAESARA LLDTAGLTGW TAPGGSVREW RTANASDLAR
GGALTLLRTV PDTKGPVPDT KAPVSDTKGP LRDTQTPEPD GSAAEPDGSA AEPDGSAAVS
DTQAPVPDGS AAAAPVLTGA DIARGTGPTG DPAELGPAAT TAPVIAAGDV LVRAIAGGGG
PMARVADDGD AGALLGPQVH LLRPDPARLD SWFLAGFVGS AENVAGASTG STVLHVAPGR
LRVPLLPLDE QRRYGEAFRH VHRLRARARR AARLAEETAA LLAGGLTGGA LLPAEGPPPA
APRPSPGTEP A
//
