ID Q18F84_HALWD Unreviewed; 455 AA.
AC Q18F84;
DT 25-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 25-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=site-specific DNA-methyltransferase (adenine-specific) {ECO:0000256|ARBA:ARBA00011900};
DE EC=2.1.1.72 {ECO:0000256|ARBA:ARBA00011900};
GN OrderedLocusNames=HQ_3277A {ECO:0000313|EMBL:CAJ53374.1};
OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloquadratum.
OX NCBI_TaxID=362976 {ECO:0000313|EMBL:CAJ53374.1, ECO:0000313|Proteomes:UP000001975};
RN [1] {ECO:0000313|EMBL:CAJ53374.1, ECO:0000313|Proteomes:UP000001975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16790 / HBSQ001 {ECO:0000313|Proteomes:UP000001975};
RX PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA Bolhuis H.H., Palm P.P., Wende A.W., Falb M.M., Rampp M.M.,
RA Rodriguez-Valera F.F., Pfeiffer F.F., Oesterhelt D.D.;
RT "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT limits of water activity.";
RL BMC Genomics 7:169-169(2006).
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 -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family.
CC {ECO:0000256|ARBA:ARBA00006594}.
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DR EMBL; AM180088; CAJ53374.1; -; Genomic_DNA.
DR AlphaFoldDB; Q18F84; -.
DR STRING; 362976.HQ_3277A; -.
DR REBASE; 13225; M.HwaORF3277P.
DR KEGG; hwa:HQ_3277A; -.
DR eggNOG; arCOG02636; Archaea.
DR HOGENOM; CLU_034179_0_0_2; -.
DR Proteomes; UP000001975; Chromosome.
DR GO; GO:0003676; F:nucleic acid binding; 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 CDD; cd02440; AdoMet_MTases; 1.
DR Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR PANTHER; PTHR33841:SF5; TYPE II METHYLTRANSFERASE M.HINDII; 1.
DR Pfam; PF07669; Eco57I; 1.
DR PRINTS; PR00507; N12N6MTFRASE.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:CAJ53374.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001975};
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:CAJ53374.1}.
FT DOMAIN 97..171
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 455 AA; 51618 MW; 4185D406B0ABCD40 CRC64;
MRGHVPTPDR LADKMVEKLF RDNPPEDGER ILYPGCGRGP FISAVHRYCD SNDFPVPEGV
AVEIDPELYE DARKRHKDKE VEFLERDFLT DSDGLDKFEY VLGNPPYIPI EGLEEDEKGR
YRREFETAEG RFDLYVLFFE QAIDLLSSGG RLCFVTPEKF EYTETTAALR RVLASSGVEE
IHHVDEDSFE GLVTYPTVTV IDADGRNETR VVGRDGEVRD VDLPDDGSSW AAAVRGGEPD
IETGVTLGDV CRRISCGVAT GADKVFVMDR EEAPPQLDDW TYPTTSGKQL RINDGPESGQ
VFVCPYDADG RLPSRDELGD FGDWASLYRE RLEDRSCYEK GKQVWYGWHE NPPMDDILQR
KLLCKDVTEE PHFWRDDSGE VVPRHSVYYL IPEEGVDIEE LQEYLNSGDA QAWLEANCQR
AANGFLRLQS TVMKQLPVPE QFGHHRQSTL TAETG
//
