GenomeNet

Database: UniProt
Entry: B4NY83_DROYA
LinkDB: B4NY83_DROYA
Original site: B4NY83_DROYA 
ID   B4NY83_DROYA            Unreviewed;       699 AA.
AC   B4NY83;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=ATP-dependent DNA helicase II subunit 2 {ECO:0000256|PIRNR:PIRNR016570};
DE            EC=3.6.4.12 {ECO:0000256|PIRNR:PIRNR016570};
GN   Name=Dyak\GE19388 {ECO:0000313|EMBL:EDW89719.1};
GN   ORFNames=Dyak_GE19388 {ECO:0000313|EMBL:EDW89719.1};
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:EDW89719.1, ECO:0000313|Proteomes:UP000002282};
RN   [1] {ECO:0000313|EMBL:EDW89719.1, ECO:0000313|Proteomes:UP000002282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01
RC   {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   [2] {ECO:0000313|EMBL:EDW89719.1, ECO:0000313|Proteomes:UP000002282}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tai18E2 / Tucson 14021-0261.01
RC   {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).
CC   -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase.
CC       {ECO:0000256|PIRNR:PIRNR016570}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC         Evidence={ECO:0000256|PIRNR:PIRNR016570};
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123,
CC       ECO:0000256|PIRNR:PIRNR016570}.
CC   -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000256|ARBA:ARBA00007726,
CC       ECO:0000256|PIRNR:PIRNR016570}.
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DR   EMBL; CM000157; EDW89719.1; -; Genomic_DNA.
DR   RefSeq; XP_002090007.1; XM_002089971.2.
DR   AlphaFoldDB; B4NY83; -.
DR   EnsemblMetazoa; FBtr0265906; FBpp0264398; FBgn0236732.
DR   GeneID; 6528975; -.
DR   KEGG; dya:Dyak_GE19388; -.
DR   eggNOG; KOG1471; Eukaryota.
DR   HOGENOM; CLU_394457_0_0_1; -.
DR   OMA; MASNKEC; -.
DR   OrthoDB; 5884at2759; -.
DR   PhylomeDB; B4NY83; -.
DR   Proteomes; UP000002282; Chromosome 2L.
DR   GO; GO:0043564; C:Ku70:Ku80 complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042162; F:telomeric DNA binding; IEA:InterPro.
DR   GO; GO:0071480; P:cellular response to gamma radiation; IEA:EnsemblMetazoa.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblMetazoa.
DR   GO; GO:0045471; P:response to ethanol; IEA:EnsemblMetazoa.
DR   GO; GO:0000723; P:telomere maintenance; IEA:EnsemblMetazoa.
DR   CDD; cd00873; KU80; 1.
DR   CDD; cd00198; vWFA; 1.
DR   Gene3D; 1.10.1600.10; -; 1.
DR   Gene3D; 2.40.290.10; -; 1.
DR   Gene3D; 1.25.40.240; Ku, C-terminal domain; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR   InterPro; IPR024193; Ku80.
DR   InterPro; IPR036494; Ku_C_sf.
DR   InterPro; IPR005161; Ku_N.
DR   InterPro; IPR014893; Ku_PK_bind.
DR   InterPro; IPR016194; SPOC-like_C_dom_sf.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1.
DR   PANTHER; PTHR12604:SF4; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 5; 1.
DR   Pfam; PF02735; Ku; 1.
DR   Pfam; PF03731; Ku_N; 1.
DR   Pfam; PF08785; Ku_PK_bind; 1.
DR   PIRSF; PIRSF016570; Ku80; 1.
DR   SMART; SM00559; Ku78; 1.
DR   SUPFAM; SSF101420; C-terminal domain of Ku80; 1.
DR   SUPFAM; SSF100939; SPOC domain-like; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR016570};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR016570};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW   ECO:0000256|PIRNR:PIRNR016570};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR016570};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR016570};
KW   Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PIRNR:PIRNR016570};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR016570};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR016570};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR016570}.
FT   DOMAIN          275..415
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
SQ   SEQUENCE   699 AA;  79688 MW;  22CA83785E7C791F CRC64;
     MASNKECLII VLDVRTCAAE EVKLKSAKCV AEILKDKIVC DRKDYVSFVL VGSDTNEKKT
     DAASHPHVVP FGDPRLCSWQ LLLDFFQFVN KTACEEGEWL NGLQAALDLQ QTAASFRVAR
     RRILLLFDFN DFPQDYEKFN EITDELLTEN IELIVGTHNI AYVDNAETSQ PQSIFNFSRK
     CGPDELKNQK HVLSLVPRCN ATLCSFKEAL HTVFKVTNRR PWVWNAKLSI GSKISISLQG
     IIAMKNQTPV KLVKVWAEKD EIVIRETRHF IKGTEVTPLP ENLITGYMLG GTPVPYDEAV
     LESKDPHPPG LHFFGFIKRN AVPDEYFCGE SLYLLVHQKQ NQSAAVKLDA LVRALVCSDR
     AILCWKIFST KFNRPQMVVL LPRLADDTHP ATLYMLEVSY TSQHHFWDFP ALRTAKTECS
     KEQLDAIDQL IDSTDLECTL RDTQQPRPWA QNDLLPFDAL PSIFEQNVMD VLERKVIHNN
     NKDDVALKDK NFTDVFWRVP EPLEEKSKRA AATVKKLFSL RYSRAWQEKL LAKEQAANGV
     TVKPEPAQKE LPMPSDGMGL IEPCSDFKRV LASVCSLTNA TERDARFQGL AADTRVVIIT
     LLERKKHNIE QLGEIITLYR QSCIDFNTFL EYDKFAEELK KITLARNCSR FWQDVMVAKQ
     LGPLVLGELT LDDELTLKAY YTIENWAENE AAEMEDIEM
//
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