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Database: UniProt
Entry: A0A091DRV8_FUKDA
LinkDB: A0A091DRV8_FUKDA
Original site: A0A091DRV8_FUKDA 
ID   A0A091DRV8_FUKDA        Unreviewed;       689 AA.
AC   A0A091DRV8;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Cell division control protein {ECO:0000256|PIRNR:PIRNR001767};
GN   ORFNames=H920_03581 {ECO:0000313|EMBL:KFO34879.1};
OS   Fukomys damarensis (Damaraland mole rat) (Cryptomys damarensis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Fukomys.
OX   NCBI_TaxID=885580 {ECO:0000313|EMBL:KFO34879.1, ECO:0000313|Proteomes:UP000028990};
RN   [1] {ECO:0000313|EMBL:KFO34879.1, ECO:0000313|Proteomes:UP000028990}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   TISSUE=Liver {ECO:0000313|EMBL:KFO34879.1};
RA   Gladyshev V.N., Fang X.;
RT   "The Damaraland mole rat (Fukomys damarensis) genome and evolution of
RT   African mole rats.";
RL   Submitted (NOV-2013) 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; KN121896; KFO34879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A091DRV8; -.
DR   STRING; 885580.ENSFDAP00000002700; -.
DR   eggNOG; KOG2227; Eukaryota.
DR   Proteomes; UP000028990; Unassembled WGS sequence.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:InterPro.
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   CDD; cd22077; WH2_WAS_WASL-2_3; 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; IPR041083; AAA_lid_10.
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; IPR003124; WH2_dom.
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; PF17872; AAA_lid_10; 1.
DR   Pfam; PF09079; Cdc6_C; 1.
DR   Pfam; PF02205; WH2; 1.
DR   PIRSF; PIRSF001767; Cdc6; 1.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM01074; Cdc6_C; 1.
DR   SMART; SM00246; WH2; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51082; WH2; 1.
PE   3: Inferred from homology;
KW   Cell cycle {ECO:0000313|EMBL:KFO34879.1};
KW   Cell division {ECO:0000313|EMBL:KFO34879.1};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   Nucleus {ECO:0000256|PIRNR:PIRNR001767};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028990}.
FT   DOMAIN          35..52
FT                   /note="WH2"
FT                   /evidence="ECO:0000259|PROSITE:PS51082"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          140..166
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          188..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..228
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        240..261
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   689 AA;  74904 MW;  4C9C68F3046AC4A9 CRC64;
     MPIPPPPPPP PGPPPPTFNQ ANTEQPKLSR DEQRGRNALL QDICRGAKLK KVTNVSDRSA
     PVLEKPKGSC GGGGYGSGAA ALQPKGGLFQ GGVPKLRPVG AKDGAGHVLL GVGEKPIRPF
     PPVALGILAS IMPRTRSQAQ TTISFPKKKF SQTLDKTQNS KNAKLVPTNV QATPCPAEIL
     PLSPRKRLGE DNLCNTPHLA PCSPPKQGRK ENGPPRSRTP KGRRLVFDDQ PAVKSPGKSK
     QARAQRNRVG SSVQKGQESP GSREQRCLPE TEPTCLRLFK RAGTCYQQAK LVLNTAVPDR
     LPAREAEMAV IGSFLRKHIC GRKAGSLYLS GAPGTGKTAC LSRTLQDLQK EVKGFRTIML
     NCMSLRSAQA VFPAIAQELG QEEAARPAGK DIMRRLEKQM TSEKGPMIVL VLDELDQLDS
     KGQDVLYTLF EWPWLSNSRL VLIGIANTLD LTDRILPRLE AREHCKPQLL NFPPYTRSQI
     AAILQDRLHQ VSADHILDGA ALQFCARKIS AVSGDVRKAL DVCRRAIEIV ESDVKSQTIL
     KPLSECKPAS ESWVPTRVGL AHIARVISEV DGSRVTLGSV GAQDSFPLQQ KVLVCSLLLL
     TRQLKVREVT LGKLYEAYSS VCRKQQVAAV DQSECLSLSG LLESRGIVGL KKNKETRFTK
     VSLKIEEKEI EHALKDKALI GNILATGLP
//
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