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Database: UniProt
Entry: G0LND3_HALWC
LinkDB: G0LND3_HALWC
Original site: G0LND3_HALWC 
ID   G0LND3_HALWC            Unreviewed;       500 AA.
AC   G0LND3;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE            EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN   Name=rmeM2 {ECO:0000313|EMBL:CCC41939.1};
GN   OrderedLocusNames=Hqrw_5066 {ECO:0000313|EMBL:CCC41939.1};
OS   Haloquadratum walsbyi (strain DSM 16854 / JCM 12705 / C23).
OG   Plasmid PL100 {ECO:0000313|EMBL:CCC41939.1,
OG   ECO:0000313|Proteomes:UP000007954}.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=768065 {ECO:0000313|EMBL:CCC41939.1, ECO:0000313|Proteomes:UP000007954};
RN   [1] {ECO:0000313|EMBL:CCC41939.1, ECO:0000313|Proteomes:UP000007954}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16854 / JCM 12705 / C23
RC   {ECO:0000313|Proteomes:UP000007954};
RC   PLASMID=Plasmid PL100 {ECO:0000313|Proteomes:UP000007954};
RX   PubMed=21701686; DOI=10.1371/journal.pone.0020968;
RA   Dyall-Smith M., Pfeiffer F., Klee K., Palm P., Gross K., Schuster S.C.,
RA   Rampp M., Oesterhelt D.;
RT   "Haloquadratum walsbyi: limited diversity in a global pond.";
RL   PLoS ONE 6:E20968-E20968(2011).
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; FR746100; CCC41939.1; -; Genomic_DNA.
DR   RefSeq; WP_014554928.1; NC_017457.1.
DR   AlphaFoldDB; G0LND3; -.
DR   REBASE; 38075; M.HwaC23ORF5066P.
DR   GeneID; 12445570; -.
DR   KEGG; hwc:Hqrw_5066; -.
DR   HOGENOM; CLU_013049_4_2_2; -.
DR   OrthoDB; 45790at2157; -.
DR   Proteomes; UP000007954; Plasmid PL100.
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; 1.20.1260.30; -; 1.
DR   Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR   InterPro; IPR022749; D12N6_MeTrfase_N.
DR   InterPro; IPR003356; DNA_methylase_A-5.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   InterPro; IPR038333; T1MK-like_N_sf.
DR   PANTHER; PTHR42933; SLR6095 PROTEIN; 1.
DR   PANTHER; PTHR42933:SF3; TYPE I RESTRICTION ENZYME MJAVIII METHYLASE SUBUNIT; 1.
DR   Pfam; PF12161; HsdM_N; 1.
DR   Pfam; PF02384; N6_Mtase; 1.
DR   PRINTS; PR00507; N12N6MTFRASE.
DR   SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW   ECO:0000313|EMBL:CCC41939.1}; Plasmid {ECO:0000313|EMBL:CCC41939.1};
KW   Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW   S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCC41939.1}.
FT   DOMAIN          8..131
FT                   /note="N6 adenine-specific DNA methyltransferase N-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12161"
FT   DOMAIN          145..465
FT                   /note="DNA methylase adenine-specific"
FT                   /evidence="ECO:0000259|Pfam:PF02384"
FT   COILED          469..496
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   500 AA;  57443 MW;  948DCB98639A4F73 CRC64;
     MSVSLDELDS QLFKCADIIR DAVDSTDYKE YILPLVYYKA ISDEFAKQYQ KNVTEYGEEF
     ARRENLYDVP VIPDGYMWDD VRAVSDNVDE ALNESFDALV EANPELRGVF RADYIDADAL
     GDDRLGRLVE HLSKYDLDTD SVPPDMLGEA YMDLVRHFAE EEGKSGGQFF TPPQIVNLCV
     RLVDEFEDGH TFHDPTVGSG GMLIEAARYY REEQNGDPQK FELTGQEINP DIAAIAKMNL
     SIHGLNGEIE REDSLAYPQF TDETDDSVAR FNRVLANFPF SADWAKDELQ DDPYDRFDWH
     EKLPRADRGD YAFIMHIAKQ LKTPEQDGEG GKASIVIPHG VLFRKHEQRY RKPMLENDMV
     EAIVGLPENL FQNNSIPSAV LVLNTDKPEE REGEVQFIHA ADEDFYDELS NQNQLTHEGL
     DHIIENFRGW TTEERVSRTV GMDEIRENDY NLNIALYVDT TEPEEDIDVE EELAKLRDLQ
     AERDDIESQM TQHMEALKYE
//
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