ID L0CRV0_DROME Unreviewed; 699 AA.
AC L0CRV0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 22-FEB-2023, entry version 50.
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=ku80 {ECO:0000313|EMBL:AGA18896.1};
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227 {ECO:0000313|EMBL:AGA18896.1};
RN [1] {ECO:0000313|EMBL:AGA18896.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=3852 {ECO:0000313|EMBL:AGA18896.1};
RX PubMed=22997235; DOI=10.1534/genetics.112.145714;
RA Lee Y.C., Langley C.H.;
RT "Long-term and short-term evolutionary impacts of transposable elements on
RT Drosophila.";
RL Genetics 192:1411-1432(2012).
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; KC116167; AGA18896.1; -; Genomic_DNA.
DR VEuPathDB; VectorBase:FBgn0041627; -.
DR HOGENOM; CLU_394457_0_0_1; -.
DR ExpressionAtlas; L0CRV0; baseline and differential.
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:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:InterPro.
DR GO; GO:0000723; P:telomere maintenance; IEA:InterPro.
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; 79798 MW; 62468075B33C35F2 CRC64;
MASNKECLII VLDVRTCAAE EVKLKSAKCV AEILKDKIVC DRKDYVSFVL VGCDTDEIKT
EDASHPNVLP FGEPRLCSWQ LLLEFFQFVN KTACEDGEWL NGLQAALELQ NVATTLRVAR
RRILLLFDFN DFPQDYEKFN EITDELLGEN IELIVGTHNI AYIDNAITSQ PQAIFNFSRK
CGPDELNNQK YALSLVPRCN ATLCSFKEAL HTVFKVTNRR PWVWNAKLNI GSKISISLQG
IIAMKNQTPV KLVKVWAEKD EIVIRETRHY IKGTEITPLP ENLITGYMLG GXXXXXDEAV
LEPKEPHPPG LHFFGFIKRN AVPDEYFCGE SLYLLVHQKH NQSAAVKLDA LVRALVSSDR
AILCWKIYST KFNRPQMVVL LPRLADDTHP ATSYMLEVSY TSQHHFWDFP ALRTTKTECS
EEQLNAIDQL IDSTDLECTL RDTQQPRPWA QNDLLPFDAL PSIFEQNVMD ILERKVIYDN
DKEDKMLKDK NFADVFWRVP DPLEEKSKRA AAIVKKLFPL RYSRAWQEKL LAKEQAENGV
AVKSEPAEKE IPLPSDGVGL IDPVSDFRRV LASVHTICNA TERDARFQAL AADTRVVIIT
LLQRRKQNIG QLGELITLYR QSCIDFNTFL EYDKFAEELK KIALAKNRSE FWQDVMVDKQ
LGPLVLGEPT LDDELALKAY YTIENWVESG ANDMEDVEM
//
