ID G0HZ23_HALHT Unreviewed; 1455 AA.
AC G0HZ23;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
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=HAH_4403 {ECO:0000313|EMBL:AEM59074.1};
OS Haloarcula hispanica (strain ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182
OS / NCIMB 2187 / VKM B-1755).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=634497 {ECO:0000313|EMBL:AEM59074.1, ECO:0000313|Proteomes:UP000005629};
RN [1] {ECO:0000313|EMBL:AEM59074.1, ECO:0000313|Proteomes:UP000005629}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33960 / DSM 4426 / JCM 8911 / NBRC 102182 / NCIMB 2187 /
RC VKM B-1755 {ECO:0000313|Proteomes:UP000005629};
RX PubMed=21994921; DOI=10.1128/JB.05953-11;
RA Liu H., Wu Z., Li M., Zhang F., Zheng H., Han J., Liu J., Zhou J., Wang S.,
RA Xiang H.;
RT "Complete genome sequence of Haloarcula hispanica, a model haloarchaeon for
RT studying genetics, metabolism, and virus-host interaction.";
RL J. Bacteriol. 193:6086-6087(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; CP002922; AEM59074.1; -; Genomic_DNA.
DR RefSeq; WP_014030938.1; NC_015943.1.
DR STRING; 634497.HAH_4403; -.
DR GeneID; 23802777; -.
DR KEGG; hhi:HAH_4403; -.
DR eggNOG; arCOG02634; Archaea.
DR HOGENOM; CLU_251831_0_0_2; -.
DR OrthoDB; 45790at2157; -.
DR Proteomes; UP000005629; Chromosome 2.
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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 1.
DR InterPro; IPR047939; BREX_1_PglX.
DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS.
DR InterPro; IPR046816; MmeI_Mtase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; NF033452; BREX_1_MTaseX; 1.
DR NCBIfam; NF033454; BREX_5_MTaseX; 1.
DR PANTHER; PTHR33841:SF1; ADENINE-SPECIFIC METHYLTRANSFERASE PGLX; 1.
DR PANTHER; PTHR33841; DNA METHYLTRANSFERASE YEEA-RELATED; 1.
DR Pfam; PF20473; MmeI_Mtase; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
DR PROSITE; PS00092; N6_MTASE; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 325..390
FT /note="MmeI-like DNA-methyltransferase"
FT /evidence="ECO:0000259|Pfam:PF20473"
FT REGION 41..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 279..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 991..1011
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1158..1178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 150..177
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 281..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 995..1009
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1455 AA; 165096 MW; 52EF2DB012A37A80 CRC64;
MDGQSTHPRK AQLDKEEREH LEAVVTEMRD RVEANVRYQL EDEYGLDEKP DTVGASADES
SLAAAREDGD ASLSETQENL VEAIELEAAD GHDWEAAHEQ YITGVGYTIV NRLAALRCME
VRDFIDDEVT SFRDDGLTPA ADRLVTEEFM LEEEAVLEAY RNECDALADE IEILFDRSTA
YSLIDPDDDT YEDLCGMLDE VPDEVWRADD VLGWVYEYYN VKLLDDLRRK GDREGLEPED
VPAANQFYTP HWVVRMLTDN SLGKLYLEDN GTLQETVEAQ DALTPDERKN RPLSPDESPD
LADFCTYLVP SEEEGEPPAF DGPEDIRVID PACGSGHFLL YAFDVLERIW RAETDLDHAE
IPREILRHNL HGVDLDMRAC QLAAFNLYLK GRTRAEAEGA TGFDMPEVGI VCADAKVADI
EGVEEVFDEV AGGKSDVKDA LRQILDAFEG VHGLGSLLDV RGTLDELFED KIDQESVQIT
LEDDPRDDHT LGQILHSLRD AVDEHRQGDS FLAQDLRSFI RLLDVLAQDY DVALMNPPYG
SRNRMPPSVK EYIDDHYRYP AEFYVNFFEV CDDITKNHGR IGMLVPRTFM FKARAEQFRS
DFIGGEGSFD FLAEFGLGVL DNATVRTAGT VVRSGVEPDP SGEFIRLYDL EASSKEEKFV
EVLSGDEPDV QRLFEVDLDS FSKVPGNTIC YSTPEEVRDL HDTELRLDCE VSDIDGESIG
YARQGIATTN DFRFMRFHWE TDDFDTFNPI ATGGSDAWIL PQIVEVVRWR DQGTRIKRYS
GTVRTPNEFL YGREGLVWTR SKETGRRFGY YPSDGLFSQT GYLFVPKDSD LLWQLLASLN
SDLYHSLFLS LTVERDWVGG IVGRAPWITA FEGEEKLESL AKEQLSIMAS TKTSDPVSPY
YISPDILPIT GDRGYFYQHP HSKKIDLVSE AKEQSPPKEE SIIEAAKTAK TEGISTRQRL
ETLAENINSL VYDLAGISGN TQKQIEEEIR LRTGKNQNSE SNETVSETPD NLEEQVKDLI
HHFAVEAVRE ENDGVIPLKS ADDQPDMLDR IVDRFHDAYG EYAENRLVEV DDILGAESAA
DEAYPNLRAF IDDDLFEYHV ETMENTPIIW KLSTERLLAD AKGEGFACFV DYHQLDASLF
DRLSNQYLEP RKAELRERRA AANQRQNDES LSTSERAEAT EEFEFCSSAL EQIAEFEEVM
QELGSTSERD FDEDDRELVE ELAPKVAAFR EETAKRIETL EQLREMNGEE WFQDTFSDNF
WEAVNEWSDE WLEALDELEN ACEEYAKPSD EPVEAHLADL FDYFNWRLKG SDHYSSTGIL
FMTYYFEREG SKLLNGEGEP FDTLTEDEEM LASLATGVND ASVLDEEYLQ QMADVEDVDD
IDDLPPLAEF KALAEEINDR CQTVDKQIPS DWSDRALSEI TTAGYQPNQN HGVIINITPL
TEKNVVPEVV EDKVL
//
