GenomeNet

Database: UniProt
Entry: B6A8E6_DROAE
LinkDB: B6A8E6_DROAE
Original site: B6A8E6_DROAE 
ID   B6A8E6_DROAE            Unreviewed;       615 AA.
AC   B6A8E6;
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:ABI31378.1};
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:ABI31378.1};
RN   [1] {ECO:0000313|EMBL:ABI31378.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=LP7 {ECO:0000313|EMBL:ABI31378.1};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQ839662; ABI31378.1; -; Genomic_DNA.
DR   AlphaFoldDB; B6A8E6; -.
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..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        100..116
FT                   /note="Polar 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;  69185 MW;  55064D0EA2DE8D02 CRC64;
     MAAVRRSTRL SSINKSAATA TAALPQSPLP TTPRRSEIWR RRHSKQILDS EDEDQDDIIS
     VISENNENSN LLNQMDKAGK RKTAAAQKTH QEQLKTPRSS KKTTTKTTTE ALTTMAQRIE
     VNRRAAKLMD DSSSSSSEEE LDEAAHVSPP KQRKTQPLPQ HLISPSRLLD RLSIDEREEQ
     VEKPSKTETH TKKAERAESP KPSPPRNKYQ NARRVLNSAE TLNLPGREPQ LQELREFFTE
     HLESQTSGSL YVSGQPGTGK TACLSLLLRA PKFAKRLQRV YINCTSIASV GAVYKKLCAE
     LQLKPTGRTE RDHLAAIQRH LRTAKRMLLL VLDEIDQLCT TRQEVLYTIF EWPALPGARI
     LLVGIANSLD LTDRALMRLN ARCELKPRLM RFPPYTKPQI VEIFKSRLAE AQVMDVFPPV
     TLQLLAAKVS AVSGDVRRAL DIGRRVVEIA EQQMRAGDKE FNMKALDLEG QTTEANDTLK
     PVQVSQVAAV LNKVYGASQN LEEDIEAAFP LQQKLMLCSL VLMLRNERNK DISMGRLHEV
     YRRVCAKRNI LALDQAEFAG TVDLVETRGI LRIMRKKEPR LNKVVLQWDE EEVHAALSDK
     QLIASILSDT ACLAK
//
DBGET integrated database retrieval system