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Database: UniProt
Entry: M0N3D3_9EURY
LinkDB: M0N3D3_9EURY
Original site: M0N3D3_9EURY 
ID   M0N3D3_9EURY            Unreviewed;       915 AA.
AC   M0N3D3;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
GN   ORFNames=C450_10133 {ECO:0000313|EMBL:EMA52452.1};
OS   Halococcus salifodinae DSM 8989.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Halococcaceae; Halococcus.
OX   NCBI_TaxID=1227456 {ECO:0000313|EMBL:EMA52452.1, ECO:0000313|Proteomes:UP000011625};
RN   [1] {ECO:0000313|EMBL:EMA52452.1, ECO:0000313|Proteomes:UP000011625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8989 {ECO:0000313|EMBL:EMA52452.1,
RC   ECO:0000313|Proteomes:UP000011625};
RX   PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA   Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA   Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT   "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT   strategies for static and dynamic osmo-response.";
RL   PLoS Genet. 10:E1004784-E1004784(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|ARBA:ARBA00001665};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000256|ARBA:ARBA00001966};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family.
CC       {ECO:0000256|ARBA:ARBA00007913}.
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:EMA52452.1}.
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DR   EMBL; AOME01000054; EMA52452.1; -; Genomic_DNA.
DR   RefSeq; WP_005043140.1; NZ_AOME01000054.1.
DR   AlphaFoldDB; M0N3D3; -.
DR   STRING; 1227456.C450_10133; -.
DR   PATRIC; fig|1227456.3.peg.2048; -.
DR   OrthoDB; 45637at2157; -.
DR   Proteomes; UP000011625; Unassembled WGS sequence.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd18808; SF1_C_Upf1; 1.
DR   Gene3D; 2.40.30.270; -; 1.
DR   Gene3D; 3.90.320.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR   InterPro; IPR041679; DNA2/NAM7-like_C.
DR   InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR   InterPro; IPR014808; DNA_replication_fac_Dna2_N.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR011604; PDDEXK-like_dom_sf.
DR   InterPro; IPR047187; SF1_C_Upf1.
DR   PANTHER; PTHR43788; DNA2/NAM7 HELICASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR43788:SF8; HELICASE WITH ZINC FINGER 2; 1.
DR   Pfam; PF13086; AAA_11; 2.
DR   Pfam; PF13087; AAA_12; 1.
DR   Pfam; PF08696; Dna2; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022806};
KW   Iron {ECO:0000256|ARBA:ARBA00022485};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00022485};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022485};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT   DOMAIN          40..184
FT                   /note="DNA replication factor Dna2 N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08696"
FT   DOMAIN          511..602
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          611..676
FT                   /note="DNA2/NAM7 helicase helicase"
FT                   /evidence="ECO:0000259|Pfam:PF13086"
FT   DOMAIN          713..898
FT                   /note="DNA2/NAM7 helicase-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF13087"
SQ   SEQUENCE   915 AA;  99862 MW;  29C201B0205A9C80 CRC64;
     MAELRGPIVD VGETRSVSTQ YGERDLAELT LRPERGQAEP VTLTLWGKWS EIAEYAQTGM
     EVLALGVEHE EFRGEIQYAT AGDSRVVIEP DYLVNVTDVR SWVQCPRMHY LNTLSGVPLN
     YPVVKGTIVH EVFSDLLRGG EVEAAIDDRV AEVGLDLGLL DRDADEVRED VSDHARAIDG
     WLSQGTLDGG DEWRSEQTLI SERYGLKGRA DAVRRGAPVE LKTGKNTNSE PRFQDKVQVA
     CYALLLDERG EPPDTGTLLY TKNAALDRNE ESGDLSPTKD FSLNDGLLDY VLRERNHLAA
     MAVAGEIPTG YEANATCNYC FEQDTCMVIS GRLDQESKAG QIGEAIPEGE RAYFDRFYRA
     IEAERGAVHN EYAKLWTQTA TERADADRAL IDLEPAGEIE VDGRWELRAR CDDPVSKIRE
     GDVVLASDGH PVRGNAEMAR VVSMGEEIVV TADEPVELRR LDVYPSEIGA DRMLTALHDA
     LLAGDESQKD VLFDRRDPAF QDIEETFIDN NPAQDRAVRR AVGAEDCALI HGPPGTGKTY
     TIARTVRALV ERGERVLLSA FTNRAVDNAL DALRDQGFEE FVRVGTEHGV REDIQEHRLE
     SRGDPDERAA ELRNAPVVAA TTASCGSRIM REGSFDVAVI DEASQLTEPA TLAAVTLADR
     FVLVGDHQQL PPVVQSADAT GTVETTTATD GSGATAAKTM DGAGGATSGI ADLSRSLFER
     LIETHPEAAV LLDTQYRMAQ RIQAFSSDEF YDGRLRPASP AVAGQHVSDL PGVTSDALPD
     HLQERVTFVD PDGTVRGNTN PAEVEAVAEI VEAYASAGVA RTDIGVIAPF RAQAAAIRRE
     VPDVTVDTVD RFQGSAKEII IVSFVATGDL DSPIFEDFRR VNVALTRAKK GLVLVGDRAA
     LATDERYARM VEWAE
//
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