ID Q06JX6_DROYA Unreviewed; 706 AA.
AC Q06JX6;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 24-JAN-2024, entry version 111.
DE RecName: Full=Cell division control protein {ECO:0000256|PIRNR:PIRNR001767};
GN Name=cdc6 {ECO:0000313|EMBL:ABI31786.1};
GN Synonyms=Dyak\GE21291 {ECO:0000313|EMBL:EDW93138.1};
GN ORFNames=Dyak_GE21291 {ECO:0000313|EMBL:EDW93138.1};
OS Drosophila yakuba (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7245 {ECO:0000313|EMBL:ABI31786.1};
RN [1] {ECO:0000313|EMBL:EDW93138.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW93138.1};
RG The Drosophila yakuba Sequencing Consortium;
RT "The Genome of Drosophila yakuba.";
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABI31786.1}
RP NUCLEOTIDE SEQUENCE.
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.
RN [3] {ECO:0000313|EMBL:EDW93138.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW93138.1}, and Tai18E2 / Tucson
RC 14021-0261.01 {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RA Clark A.G., Eisen M.B., Smith D.R., Bergman C.M., Oliver B., Markow T.A.,
RA Kaufman T.C., Kellis M., Gelbart W., Iyer V.N., Pollard D.A., Sackton T.B.,
RA Larracuente A.M., Singh N.D., Abad J.P., Abt D.N., Adryan B., Aguade M.,
RA Akashi H., Anderson W.W., Aquadro C.F., Ardell D.H., Arguello R.,
RA Artieri C.G., Barbash D.A., Barker D., Barsanti P., Batterham P.,
RA Batzoglou S., Begun D., Bhutkar A., Blanco E., Bosak S.A., Bradley R.K.,
RA Brand A.D., Brent M.R., Brooks A.N., Brown R.H., Butlin R.K., Caggese C.,
RA Calvi B.R., Bernardo de Carvalho A., Caspi A., Castrezana S.,
RA Celniker S.E., Chang J.L., Chapple C., Chatterji S., Chinwalla A.,
RA Civetta A., Clifton S.W., Comeron J.M., Costello J.C., Coyne J.A., Daub J.,
RA David R.G., Delcher A.L., Delehaunty K., Do C.B., Ebling H., Edwards K.,
RA Eickbush T., Evans J.D., Filipski A., Findeiss S., Freyhult E., Fulton L.,
RA Fulton R., Garcia A.C., Gardiner A., Garfield D.A., Garvin B.E., Gibson G.,
RA Gilbert D., Gnerre S., Godfrey J., Good R., Gotea V., Gravely B.,
RA Greenberg A.J., Griffiths-Jones S., Gross S., Guigo R., Gustafson E.A.,
RA Haerty W., Hahn M.W., Halligan D.L., Halpern A.L., Halter G.M., Han M.V.,
RA Heger A., Hillier L., Hinrichs A.S., Holmes I., Hoskins R.A., Hubisz M.J.,
RA Hultmark D., Huntley M.A., Jaffe D.B., Jagadeeshan S., Jeck W.R.,
RA Johnson J., Jones C.D., Jordan W.C., Karpen G.H., Kataoka E.,
RA Keightley P.D., Kheradpour P., Kirkness E.F., Koerich L.B., Kristiansen K.,
RA Kudrna D., Kulathinal R.J., Kumar S., Kwok R., Lander E., Langley C.H.,
RA Lapoint R., Lazzaro B.P., Lee S.J., Levesque L., Li R., Lin C.F., Lin M.F.,
RA Lindblad-Toh K., Llopart A., Long M., Low L., Lozovsky E., Lu J., Luo M.,
RA Machado C.A., Makalowski W., Marzo M., Matsuda M., Matzkin L.,
RA McAllister B., McBride C.S., McKernan B., McKernan K., Mendez-Lago M.,
RA Minx P., Mollenhauer M.U., Montooth K., Mount S.M., Mu X., Myers E.,
RA Negre B., Newfeld S., Nielsen R., Noor M.A., O'Grady P., Pachter L.,
RA Papaceit M., Parisi M.J., Parisi M., Parts L., Pedersen J.S., Pesole G.,
RA Phillippy A.M., Ponting C.P., Pop M., Porcelli D., Powell J.R.,
RA Prohaska S., Pruitt K., Puig M., Quesneville H., Ram K.R., Rand D.,
RA Rasmussen M.D., Reed L.K., Reenan R., Reily A., Remington K.A.,
RA Rieger T.T., Ritchie M.G., Robin C., Rogers Y.H., Rohde C., Rozas J.,
RA Rubenfield M.J., Ruiz A., Russo S., Salzberg S.L., Sanchez-Gracia A.,
RA Saranga D.J., Sato H., Schaeffer S.W., Schatz M.C., Schlenke T.,
RA Schwartz R., Segarra C., Singh R.S., Sirot L., Sirota M., Sisneros N.B.,
RA Smith C.D., Smith T.F., Spieth J., Stage D.E., Stark A., Stephan W.,
RA Strausberg R.L., Strempel S., Sturgill D., Sutton G., Sutton G.G., Tao W.,
RA Teichmann S., Tobari Y.N., Tomimura Y., Tsolas J.M., Valente V.L.,
RA Venter E., Venter J.C., Vicario S., Vieira F.G., Vilella A.J.,
RA Villasante A., Walenz B., Wang J., Wasserman M., Watts T., Wilson D.,
RA Wilson R.K., Wing R.A., Wolfner M.F., Wong A., Wong G.K., Wu C.I., Wu G.,
RA Yamamoto D., Yang H.P., Yang S.P., Yorke J.A., Yoshida K., Zdobnov E.,
RA Zhang P., Zhang Y., Zimin A.V., Baldwin J., Abdouelleil A., Abdulkadir J.,
RA Abebe A., Abera B., Abreu J., Acer S.C., Aftuck L., Alexander A., An P.,
RA Anderson E., Anderson S., Arachi H., Azer M., Bachantsang P., Barry A.,
RA Bayul T., Berlin A., Bessette D., Bloom T., Blye J., Boguslavskiy L.,
RA Bonnet C., Boukhgalter B., Bourzgui I., Brown A., Cahill P., Channer S.,
RA Cheshatsang Y., Chuda L., Citroen M., Collymore A., Cooke P., Costello M.,
RA D'Aco K., Daza R., De Haan G., DeGray S., DeMaso C., Dhargay N., Dooley K.,
RA Dooley E., Doricent M., Dorje P., Dorjee K., Dupes A., Elong R., Falk J.,
RA Farina A., Faro S., Ferguson D., Fisher S., Foley C.D., Franke A.,
RA Friedrich D., Gadbois L., Gearin G., Gearin C.R., Giannoukos G., Goode T.,
RA Graham J., Grandbois E., Grewal S., Gyaltsen K., Hafez N., Hagos B.,
RA Hall J., Henson C., Hollinger A., Honan T., Huard M.D., Hughes L.,
RA Hurhula B., Husby M.E., Kamat A., Kanga B., Kashin S., Khazanovich D.,
RA Kisner P., Lance K., Lara M., Lee W., Lennon N., Letendre F., LeVine R.,
RA Lipovsky A., Liu X., Liu J., Liu S., Lokyitsang T., Lokyitsang Y.,
RA Lubonja R., Lui A., MacDonald P., Magnisalis V., Maru K., Matthews C.,
RA McCusker W., McDonough S., Mehta T., Meldrim J., Meneus L., Mihai O.,
RA Mihalev A., Mihova T., Mittelman R., Mlenga V., Montmayeur A., Mulrain L.,
RA Navidi A., Naylor J., Negash T., Nguyen T., Nguyen N., Nicol R., Norbu C.,
RA Norbu N., Novod N., O'Neill B., Osman S., Markiewicz E., Oyono O.L.,
RA Patti C., Phunkhang P., Pierre F., Priest M., Raghuraman S., Rege F.,
RA Reyes R., Rise C., Rogov P., Ross K., Ryan E., Settipalli S., Shea T.,
RA Sherpa N., Shi L., Shih D., Sparrow T., Spaulding J., Stalker J.,
RA Stange-Thomann N., Stavropoulos S., Stone C., Strader C., Tesfaye S.,
RA Thomson T., Thoulutsang Y., Thoulutsang D., Topham K., Topping I.,
RA Tsamla T., Vassiliev H., Vo A., Wangchuk T., Wangdi T., Weiand M.,
RA Wilkinson J., Wilson A., Yadav S., Young G., Yu Q., Zembek L., Zhong D.,
RA Zimmer A., Zwirko Z., Jaffe D.B., Alvarez P., Brockman W., Butler J.,
RA Chin C., Gnerre S., Grabherr M., Kleber M., Mauceli E., MacCallum I.;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
RN [4] {ECO:0000313|EMBL:EDW93138.1, ECO:0000313|Proteomes:UP000002282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW93138.1}, and Tai18E2 / Tucson
RC 14021-0261.01 {ECO:0000313|Proteomes:UP000002282};
RX PubMed=17550304; DOI=10.1371/journal.pbio.0050152;
RA Ranz J.M., Maurin D., Chan Y.S., von Grotthuss M., Hillier L.W., Roote J.,
RA Ashburner M., Bergman C.M.;
RT "Principles of genome evolution in the Drosophila melanogaster species
RT group.";
RL PLoS Biol. 5:E152-E152(2007).
RN [5] {ECO:0000313|EMBL:EDW93138.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Tai18E2 {ECO:0000313|EMBL:EDW93138.1};
RG FlyBase;
RL Submitted (NOV-2015) 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; DQ839715; ABI31786.1; -; Genomic_DNA.
DR EMBL; CM000159; EDW93138.1; -; Genomic_DNA.
DR RefSeq; XP_002093426.1; XM_002093390.2.
DR AlphaFoldDB; Q06JX6; -.
DR SMR; Q06JX6; -.
DR EnsemblMetazoa; FBtr0267809; FBpp0266301; FBgn0238558.
DR GeneID; 6532682; -.
DR KEGG; dya:Dyak_GE21291; -.
DR eggNOG; KOG2227; Eukaryota.
DR HOGENOM; CLU_012774_3_1_1; -.
DR OMA; DHMEAIQ; -.
DR OrthoDB; 118994at2759; -.
DR Proteomes; UP000002282; Chromosome 3L.
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; 2.
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 333..478
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT DOMAIN 608..688
FT /note="Cdc6 C-terminal"
FT /evidence="ECO:0000259|SMART:SM01074"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 65..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 31..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 706 AA; 80385 MW; 1A508093B514CB00 CRC64;
MAAVRRSTRL SSISKSAAAS PLPQSTQTPR RSEVWKRRQP KKVLADSDEE EEVEVVTAIY
DLTSTVSENN ENRNVLNKMD KIPRRRNSQV QVAQVEHPKT PRSTKKTAQS AGSSRAKRMQ
ENREATARFL ESEQDLEEVD PLHGSPPKQR KLQPLPQHLI SPSRLLDRLS IDERQEEEEV
EAPIHKTDKA EQQQKHVAKD QPKPRPKQLE DPLALKQLEK PATKQQEKLP SKQQEKLPSK
QQEKPATKQQ EKPATKQQEK PATKQQNKTQ IKEQNQSETN EETLQNSQPS PSRNKYQNAR
RVLNSAETQN LPGRESQLQE LREFFSSHLE SQTSGSLYVS GQPGTGKTAC LSLLLRDPDF
SKRLQRVYIN CTSIASVGAV YKKLCTELQL KVSGRTERDH LEAIQRHLKT AKRMLLLVLD
EIDQLCTSRQ EVLYTIFEWP ALPSSRILLV GIANSLDLTD RALMRLNARC ELKPRLMHFP
PYSKQQIVEI FKSRLAEAEV LDVFPPVTLQ LLAAKVSAIS GDVRRALDIG RRVVEIAEQQ
KRDGEKEFNM KALQLEGKDA EEAREKQDTL KPVQVTQVAA VLNKVYGASQ NLEEDIEASF
PLQQKLMLCT LVLMLRNERN KDISMGRLHE VYRRVCAKRN ILALDQAEFT GTVDLVETRG
ILRIMRKKEP RLHKVLLQWD EEEVHAALSD KQLIASILSD TGCLSK
//