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Database: UniProt
Entry: A0A0W1RII2_9EURY
LinkDB: A0A0W1RII2_9EURY
Original site: A0A0W1RII2_9EURY 
ID   A0A0W1RII2_9EURY        Unreviewed;      1033 AA.
AC   A0A0W1RII2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
DE   Flags: Fragment;
GN   ORFNames=AUR66_19465 {ECO:0000313|EMBL:KTG13387.1};
OS   Haloferax profundi.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=1544718 {ECO:0000313|EMBL:KTG13387.1, ECO:0000313|Proteomes:UP000053157};
RN   [1] {ECO:0000313|EMBL:KTG13387.1, ECO:0000313|Proteomes:UP000053157}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB29 {ECO:0000313|EMBL:KTG13387.1,
RC   ECO:0000313|Proteomes:UP000053157};
RA   Zhang G., Stingl U., Rashid M.;
RT   "Haloferax profundi sp. nov. isolated from the Discovery deep brine-
RT   seawater interface in the Red Sea.";
RL   Submitted (DEC-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:KTG13387.1}.
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DR   EMBL; LOPV01000599; KTG13387.1; -; Genomic_DNA.
DR   RefSeq; WP_058573447.1; NZ_LOPV01000599.1.
DR   AlphaFoldDB; A0A0W1RII2; -.
DR   OrthoDB; 45790at2157; -.
DR   Proteomes; UP000053157; 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   GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR   GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
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; IPR029063; SAM-dependent_MTases_sf.
DR   PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR   PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-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:0000256|ARBA:ARBA00022603};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          367..629
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   REGION          680..705
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        688..705
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KTG13387.1"
SQ   SEQUENCE   1033 AA;  116536 MW;  86BED31F96CF24F4 CRC64;
     LARAGDFRVL YVELSELTRT AERDFVQCLT HARLGTDWAT EDTFLAVFHA PDSTAWHLVT
     PFRTGVDDGR TGRPVLRRYT LGAGQTHRHV SDALAKIGAH DGQLADRIDE AFQVDTLTEE
     FYDDYKWAFE RLSDDLRESG VDTKDVHQYA HVTLTRLLCF YYLQRRGWTG GRTDFVRWFH
     DRYRASGEDE QFHETWLSAL FFSESDHPEG TSPFTSLPDE VEAARTECPP LNDGLFEPTD
     ADRSEWYFSD SALTSVICDF LERYTYTISE ESSYDVDVAV DPSMLGKIYE SFVAEEDRDE
     AGIFYTPRAE VDLMCRLALY EQFCDQIERP DTARKRALVE FLFSTPSGWD RTKIDIDDEL
     EAVLRNLRIV DPACGSGAFL VGMGQVLTEL FEKVGLTVDA ELKSRILDEA LYGADIKPWA
     VRVAAFRLWL WVVETEPEIP PEEFELLDFS FNLYTGDSVV GREGDGLDAA QEDGFDVVIT
     NPPYVDHQHI AQQNHPQTVS DQSPPADVRS SKAAYKTALV TYVQETFGIK PYRSSDLYLY
     FFFRAIDLLR DGGTLMFLTS NTWLDTAYGK RLQQGLLELT DIECIVDNRK RRSFERASVN
     TVLTVANRTS ERSLAGEVKF VALSDPYERV VSPPTMADIL VDSSEDEGTD EFALGSERGR
     IRRLDAIRVV RLDEPALWRL GGGTTQPRRE RGTGTSRTST PVCPGGTYTG TSWGRFLRAP
     SAYFDVLEAG ADIFTPLSSI ASVGSYLNTG GADGFFFVTL EEGDPQTDRH VTIRNRETDE
     TFTVESAFVV PFVESPRQVT HVDLSNDEFE SYLVSIPMGT DLSDTHVQRY VAWGERRGAY
     HTASGRRGKR EWWEIGTRGE TNTTVVWPNR QHDRHFVAYN PNRTVTHRFY RLAPHDAADV
     TPEELAALLN FSPTALFTEV LASTGLGLGV LDVTGRTLQQ IPVVDPAKLS KSSLETIRGA
     FRRMANRPMG SMHDELGATT AEQFDIDAVV SDRRTIDREL FEQYLDVAPS EQVPIYQAIL
     ETVNTRINKS RSL
//
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