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Database: UniProt
Entry: M0D1F2_9EURY
LinkDB: M0D1F2_9EURY
Original site: M0D1F2_9EURY 
ID   M0D1F2_9EURY            Unreviewed;       591 AA.
AC   M0D1F2;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=ORC1-type DNA replication protein {ECO:0000256|HAMAP-Rule:MF_01407};
GN   ORFNames=C475_03979 {ECO:0000313|EMBL:ELZ29346.1};
OS   Halosimplex carlsbadense 2-9-1.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC   Haloarculaceae; Halosimplex.
OX   NCBI_TaxID=797114 {ECO:0000313|EMBL:ELZ29346.1, ECO:0000313|Proteomes:UP000011626};
RN   [1] {ECO:0000313|EMBL:ELZ29346.1, ECO:0000313|Proteomes:UP000011626}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2-9-1 {ECO:0000313|EMBL:ELZ29346.1,
RC   ECO:0000313|Proteomes:UP000011626};
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   -!- FUNCTION: Involved in regulation of DNA replication.
CC       {ECO:0000256|HAMAP-Rule:MF_01407}.
CC   -!- SIMILARITY: Belongs to the CDC6/cdc18 family. {ECO:0000256|HAMAP-
CC       Rule:MF_01407}.
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:ELZ29346.1}.
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DR   EMBL; AOIU01000008; ELZ29346.1; -; Genomic_DNA.
DR   RefSeq; WP_006882468.1; NZ_AOIU01000008.1.
DR   AlphaFoldDB; M0D1F2; -.
DR   STRING; 797114.C475_03979; -.
DR   PATRIC; fig|797114.5.peg.810; -.
DR   eggNOG; arCOG00467; Archaea.
DR   Proteomes; UP000011626; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd00009; AAA; 1.
DR   CDD; cd08768; Cdc6_C; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR   HAMAP; MF_01407; ORC1_type_DNA_replic_protein; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR041664; AAA_16.
DR   InterPro; IPR015163; Cdc6_C.
DR   InterPro; IPR014277; Orc1/Cdc6_arc.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   NCBIfam; TIGR02928; orc1/cdc6 family replication initiation protein; 1.
DR   PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR   PANTHER; PTHR10763:SF22; ORC1-TYPE DNA REPLICATION PROTEIN 3; 1.
DR   Pfam; PF13191; AAA_16; 1.
DR   Pfam; PF09079; Cdc6_C; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01074; Cdc6_C; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_01407}; Cell cycle {ECO:0000313|EMBL:ELZ29346.1};
KW   Cell division {ECO:0000313|EMBL:ELZ29346.1};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP-
KW   Rule:MF_01407};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_01407}; Reference proteome {ECO:0000313|Proteomes:UP000011626}.
FT   DOMAIN          180..390
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          484..566
FT                   /note="Cdc6 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01074"
FT   REGION          1..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          241..297
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        44..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        64..78
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..93
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         192..196
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01407"
FT   BINDING         389
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01407"
FT   BINDING         401
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01407"
SQ   SEQUENCE   591 AA;  65736 MW;  986EAB94FA6DA33F CRC64;
     MNGDDTDQDT TLDSQRFVDG ADGDDEQLPP STGDQGAQSE RAAEGQSGDR EQRTTREDEA
     SAAGDQDPTD DESDPETAST VDTDSSSTVR GGVGSSGVDF DSESDDADSS VLDDVMLDDV
     GSEEPEEASQ GLFDDLLAGD PIFENKEVLR PSYTPRKLPH REEQINNMAT ILVTALRGDS
     PSNILIYGKT GTGKTASAKF VSTELESTSQ KYEVPCEVEY INCEVTDTQY RVLAQLANKF
     VEKNEAVIDE ELDDLESLRE RAHENPTVLA ETEYDSVAAV EDRIEQLEDD RESFEQVPMT
     GWPTDRVYST FFDAVDYHER VVVIMLDEID KLVEKSGDDT LYNLSRMNSE LERSRVSIMG
     ISNDLKFTDF LDPRVKSSLG EEEIVFPPYD ANQLRDILEH RAEVAFEGDA LTDDVIPLCA
     AFAAQEHGDA RRALDLLRTA GELAERDQTD DVDEDHVRKA QEKIELDRVV EVVRTLPTQS
     KLVLFAIIML EKNGVHNINT GEVYNVYQRL CEEIDVDTLT QRRVTDLISE LDMLGIVNAV
     VVSKGRYGRT KEISLSVPID ETEAVLLSDS RLSDIEDTQP FVQTRFDSDS N
//
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