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Database: UniProt
Entry: B6A8E9_DROAE
LinkDB: B6A8E9_DROAE
Original site: B6A8E9_DROAE 
ID   B6A8E9_DROAE            Unreviewed;       615 AA.
AC   B6A8E9;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   08-NOV-2023, entry version 44.
DE   RecName: Full=Cell division control protein {ECO:0000256|PIRNR:PIRNR001767};
GN   Name=cdc6 {ECO:0000313|EMBL:ABI31381.1};
OS   Drosophila americana (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila.
OX   NCBI_TaxID=40366 {ECO:0000313|EMBL:ABI31381.1};
RN   [1] {ECO:0000313|EMBL:ABI31381.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ML5 {ECO:0000313|EMBL:ABI31381.1};
RA   Wiggins B.L., Malik H.S.;
RT   "Positive selection of Drosophila cdc6, an essential DNA replication-
RT   licensing gene, suggests an adaptive choice of replication origins.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the initiation of DNA replication. Also
CC       participates in checkpoint controls that ensure DNA replication is
CC       completed before mitosis is initiated. {ECO:0000256|PIRNR:PIRNR001767}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR001767}.
CC   -!- SIMILARITY: Belongs to the CDC6/cdc18 family.
CC       {ECO:0000256|ARBA:ARBA00006184, ECO:0000256|PIRNR:PIRNR001767}.
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DR   EMBL; DQ839665; ABI31381.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6A8E9; -.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-UniRule.
DR   GO; GO:0006270; P:DNA replication initiation; 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   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR016314; Cdc6/18.
DR   InterPro; IPR015163; Cdc6_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR10763:SF26; CELL DIVISION CONTROL PROTEIN 6 HOMOLOG; 1.
DR   PANTHER; PTHR10763; CELL DIVISION CONTROL PROTEIN 6-RELATED; 1.
DR   Pfam; PF13401; AAA_22; 1.
DR   Pfam; PF09079; Cdc6_C; 1.
DR   PIRSF; PIRSF001767; Cdc6; 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   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR001767}.
FT   DOMAIN          246..391
FT                   /note="AAA+ ATPase"
FT                   /evidence="ECO:0000259|SMART:SM00382"
FT   DOMAIN          517..597
FT                   /note="Cdc6 C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01074"
FT   REGION          1..109
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          123..210
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..33
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        61..76
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        81..99
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        170..202
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   615 AA;  69022 MW;  605B243AD611F7BA CRC64;
     MAAVRRSTRL SSINKSAATA TAALPQSPLP TTPRRSEIWR RRHSKQILDS EDEDQDDIIS
     VISENNENSN LLNQMDKAGK RKTAAAQKTH QEQLKTPRSS KKTTTKTTTE ALTTMAQRIE
     ANRRAAKLMD DSSSGSSEEE LDEAAHVSPP KQRKTQPLAQ HLISPSRLLD RLSIDEREEQ
     VEKPSKTETH TKKAERAESP KPSPPRNKYQ NARRVLNSAE TLNLPGREPQ LQELREFFTA
     HLESQTSGSL YVSGQPGTGK TACLSLLLRA PEFAKRLQRV YINCTSIASV GAVYKKLCAE
     LQLKPTGRTE RDHLAAIQRH LRTAKRMLLL VLDEIDQLCT TRQEVLYTIF EWPALPGARI
     LLVGIANSLD LTDRALMRLN ARCELKPRLM HFPPYTKPQI VEIFKSRLAE AQVMDVFPPV
     TLQLLAAKVS AVSGDVRRAL DIGRRVVEIA EQQKRAGDKE FNMKALDLEG QTTEANDTLK
     PVQVSQVAAV LNKVYGASQN LEEDIEAAFP LQQKLMLCSL VLMLRNERNK DISMGRLHEV
     YRRVCAKRNI LALDQAEFAG TVDLVETRGI LRIMRKKEPR LNKVVLQWDE EEVHAALSDK
     QLIASILSDT ACLAK
//
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