ID D4GQB1_HALVD Unreviewed; 1088 AA.
AC D4GQB1; L9UUU7;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 65.
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=HVO_A0079 {ECO:0000313|EMBL:ADE01706.1};
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OG Plasmid pHV4 {ECO:0000313|EMBL:ADE01706.1,
OG ECO:0000313|Proteomes:UP000008243}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE01706.1, ECO:0000313|Proteomes:UP000008243};
RN [1] {ECO:0000313|EMBL:ADE01706.1, ECO:0000313|Proteomes:UP000008243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
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; CP001955; ADE01706.1; -; Genomic_DNA.
DR RefSeq; WP_004043359.1; NZ_AOHU01000086.1.
DR AlphaFoldDB; D4GQB1; -.
DR REBASE; 25098; HvoDSORF79P.
DR PaxDb; 309800-C498_10871; -.
DR EnsemblBacteria; ADE01706; ADE01706; HVO_A0079.
DR GeneID; 8923789; -.
DR KEGG; hvo:HVO_A0079; -.
DR PATRIC; fig|309800.29.peg.2085; -.
DR eggNOG; arCOG02634; Archaea.
DR eggNOG; arCOG02635; Archaea.
DR eggNOG; arCOG02636; Archaea.
DR HOGENOM; CLU_002539_1_2_2; -.
DR OrthoDB; 293790at2157; -.
DR Proteomes; UP000008243; Plasmid pHV4.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; 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:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 3.90.220.20; DNA methylase specificity domains; 1.
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; IPR011639; MethylTrfase_TaqI-like_dom.
DR InterPro; IPR044946; Restrct_endonuc_typeI_TRD_sf.
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; PF07669; Eco57I; 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 3: Inferred from homology;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Hydrolase {ECO:0000313|EMBL:ADE01706.1};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603,
KW ECO:0000313|EMBL:ADE01706.1}; Plasmid {ECO:0000313|EMBL:ADE01706.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008243};
KW Restriction system {ECO:0000256|ARBA:ARBA00022747};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ADE01706.1}.
FT DOMAIN 374..480
FT /note="DNA methylase adenine-specific"
FT /evidence="ECO:0000259|Pfam:PF02384"
FT DOMAIN 595..667
FT /note="Type II methyltransferase M.TaqI-like"
FT /evidence="ECO:0000259|Pfam:PF07669"
SQ SEQUENCE 1088 AA; 123885 MW; ADDFF3E0E23DF644 CRC64;
MVEIPSGIKR NQGGNDWYEA HLVDENGDGI IRYIELEASG DSPAFSDLKR HLKRHGSPIN
ELFTVIAYRK SDEGPLTSPL NDDITFLHIE EQFSSEDVEV TFDLNYFTVK RFGVEPAYLD
YLDDLSVDSG QGRASLEGDV EEVFSIREIT RSFYQDFGEI FREDLQDAIH GLKDPEENLN
AYTRTVVNRV LFLLFIEEKK WLDGDVDYVE NKYEEVAEDP DMHVYEDFFE PLFFEALSEE
GTTESDTLGR IPFLNGGLFE RKDIEKNVEI DEVFFDKLLS PEKNSSGNPE GLLRRYKISL
RESNPSEQEL VVDPEFIGRI FEMFMQKDDR ADLGAFYTPK PITSYMTKNA LKQHLLGQTD
ITNEEAVSLV TDHTTPESLS DSQIEAIDEA LRSATVLDPA VGSGAFIIAM LEELVAVSEA
LDSSRGDDRS RFQLKKEFIA DTLYGVDIDA AGIEMCKFRV WLHLMQDLKH VSHEEFLEAN
QKFALPNLGF KFFVGNSLVG EYDPTRVDVS SYQETLTGGL NSTLNEIHKT RKEFQTAHGK
NKDRLSDQLE KLTTELETQL AVKEKGGWMT EAAEAADSTF TWTTNIPEVI LDGGFDIVIG
NPPYEGQEGA EYKGELGDFY SEKEGFRYYS KTDLFQFFVH RGYELANSDG VFTYIMSDTF
FTQINKTDVR STLLDELDEL TRVNPDAFDA SVETAIFSLS KSGNKSNEVR LNDSYDVDIK
SYPQLLTPID YDESYSVSIG EVSYETKRSN LGEHTIYQLN RELYRKSINN SFFTPTELNT
EIFGEFIAPF NSVYDRWQNE IADTSNLEKS LPEVESLIQE TSPGEILPFG LLTVGGQGIS
MRTNKDFIHV LEGTKKAKRI EEEDSYSRSK LYKTVKEEKV IHDASQLSEE EKLHGVANDA
NRTFVKVTRE SKSRDLYFCP TDEFVDWSRD NVDKLKDQGV PRNDQYYLNQ GIATKQGGGV
RNLECRMIEP SVFTNTNLVF FSIDEEKADL KYMMAILNST FSGYIAKNFL NRIGLSTRDV
RRLPIKIPDD DEKEKIVGLV EDAIQIQKKR PDVLDDPDMD AIEEIDRELD EAVAELYGVD
LERLENGI
//
