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Database: UniProt
Entry: A0A101UQG1_9ACTN
LinkDB: A0A101UQG1_9ACTN
Original site: A0A101UQG1_9ACTN 
ID   A0A101UQG1_9ACTN        Unreviewed;      1156 AA.
AC   A0A101UQG1;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, 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=AQJ91_44050 {ECO:0000313|EMBL:KUO14943.1};
OS   Streptomyces dysideae.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=909626 {ECO:0000313|EMBL:KUO14943.1, ECO:0000313|Proteomes:UP000053260};
RN   [1] {ECO:0000313|EMBL:KUO14943.1, ECO:0000313|Proteomes:UP000053260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RV15 {ECO:0000313|EMBL:KUO14943.1,
RC   ECO:0000313|Proteomes:UP000053260};
RA   Ruckert C., Abdelmohsen U.R., Winkler A., Hentschel U., Kalinowski J.,
RA   Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces sp. RV15, isolated from a marine
RT   sponge.";
RL   Submitted (OCT-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:KUO14943.1}.
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DR   EMBL; LMXB01000127; KUO14943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101UQG1; -.
DR   STRING; 909626.AQJ91_44050; -.
DR   OrthoDB; 9776021at2; -.
DR   Proteomes; UP000053260; 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:0006306; P:DNA methylation; IEA:InterPro.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR041635; Type_ISP_LLaBIII_C.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR   PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   Pfam; PF18135; Type_ISP_C; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:KUO14943.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053260};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          318..502
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   DOMAIN          696..1045
FT                   /note="Type ISP restriction-modification enzyme LLaBIII C-
FT                   terminal specificity"
FT                   /evidence="ECO:0000259|Pfam:PF18135"
FT   REGION          1088..1156
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1124..1147
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1156 AA;  130860 MW;  CEACCCD853FB52D7 CRC64;
     MPEEWIRALV ADFGSECRER LRVSDTEASI SLPVAKLVET FGARWRLSPR LHPEYPLPEA
     RVRPDYAVET SGRITGFLEL KAPGHDVTPD GFTKRDREQW ELMRRLPNVL YSNGHTWCLY
     RGGLRPLRTV RLEGDLYRSG SRLRTSEADG AAFRDLLREF LGWQPQRITT VGQLVSSIAP
     LCQYLREEVL EQLALERRTP DGPRSRRRAP KPFTALAHHW SKVLFPSTDG QDPDHLFADR
     YTQTIAFALL LARIENVPLA GRNFVDVARE LKAENTVMGR ALQLLTETVD AEFARRIDTL
     VQVIDAVDWE AIRARTPDAH VHLYEDFLQE YDRELRKRSG TYYTPPRLVK EMVRFTDAVL
     RTRLGCVEGF ADEQVTIVDP AMGTGTFLSE IIDRVAEERS RRGEGFRGEA VEQLAGRLIG
     FERQMAAYAV AQMRITQTLR KQVTDTQLGD LRLHLADTLA DPYERATLFT FLPDGDPLVE
     NTRKADWIKR EQKVTVMISN PPDRERAEGE GGWVEKGREG DDKAPLLDAF RLGGRNGVHE
     NKLKNLYVYF WRWATFKVFE QHRSESDRGI VAFISTAGFL SGPGFRGMRK YLRETCSEGW
     IIDLSPEGIQ PPLRTRLFEG VQQQLTIAVF VRSRADTEPA HIRYVALDGS TREEKYAQLE
     ALGPDSDQWR PVRQDAHAPF TPAALGAWDT YPALDDLLPW TVPGILPKRT WVYSSDPDTL
     RSRWRRLTAE TDIAEKRALF RETKGGRTVD RPVKPLPGSA QRRRSMLEAG PECPEPVPVA
     FRPFDRQWII PDNRVLDRCS PELWENRAEG QIHMVELHSE RFGDGPATLF TALMPDMHHF
     AGWGGGRVIP FLQKDGTPNA TPGLLQHLRN SFGGLAVSAE DLIAYIAAIT AHPGFRSRFD
     DELTTIGVRV PLTGDAALWS EALHIGRKVI WASTFGERLV DPVAGRPGGP QEVWATAQPA
     ITYRRQVGRD ELPESFVYDP DRLELHFGQG VFVSVTQQMR DYQVSGQNVL DGWLKRRTGP
     PSRRAVSQLD HIRPDRWQPA WSEELQHVLA VLWHLVELQS AQNELLDRVL TSPLVSVAEL
     QRRNVLPVPE TARRSAPAPI QTDPIPGTEG IEAREPHAVR PLTAEKSSSA TAPMARSRRS
     RNSGAAQSPR RKRQDP
//
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