KU70_DICDI
ID KU70_DICDI Reviewed; 909 AA.
AC Q54MA9;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=ATP-dependent DNA helicase ku70;
DE EC=3.6.4.12;
GN Name=ku70; ORFNames=DDB_G0286069;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Involved in non-homologous end joining (NHEJ) DNA double
CC strand break repair. {ECO:0000250}.
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 -!- SUBUNIT: Heterodimer of ku70 and ku80. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
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DR EMBL; AAFI02000085; EAL64413.1; -; Genomic_DNA.
DR RefSeq; XP_637925.1; XM_632833.1.
DR AlphaFoldDB; Q54MA9; -.
DR SMR; Q54MA9; -.
DR STRING; 44689.DDB0232001; -.
DR PaxDb; Q54MA9; -.
DR EnsemblProtists; EAL64413; EAL64413; DDB_G0286069.
DR GeneID; 8625436; -.
DR KEGG; ddi:DDB_G0286069; -.
DR dictyBase; DDB_G0286069; ku70.
DR eggNOG; KOG2327; Eukaryota.
DR HOGENOM; CLU_014815_2_0_1; -.
DR InParanoid; Q54MA9; -.
DR OMA; FNTNTCS; -.
DR PhylomeDB; Q54MA9; -.
DR Reactome; R-DDI-5693571; Nonhomologous End-Joining (NHEJ).
DR Reactome; R-DDI-6798695; Neutrophil degranulation.
DR PRO; PR:Q54MA9; -.
DR Proteomes; UP000002195; Chromosome 4.
DR GO; GO:0000785; C:chromatin; IC:dictyBase.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IDA:dictyBase.
DR GO; GO:0005634; C:nucleus; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0003690; F:double-stranded DNA binding; ISS:dictyBase.
DR GO; GO:0042162; F:telomeric DNA binding; IBA:GO_Central.
DR GO; GO:0071480; P:cellular response to gamma radiation; IBA:GO_Central.
DR GO; GO:0071481; P:cellular response to X-ray; IBA:GO_Central.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:dictyBase.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:dictyBase.
DR GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR Gene3D; 4.10.970.10; -; 1.
DR InterPro; IPR019406; APLF_PBZ.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR027388; Ku70_bridge/pillars_dom_sf.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12604:SF2; PTHR12604:SF2; 1.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF10283; zf-CCHH; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR TIGRFAMs; TIGR00578; ku70; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Helicase; Hydrolase; Nucleotide-binding; Nucleus; Reference proteome.
FT CHAIN 1..909
FT /note="ATP-dependent DNA helicase ku70"
FT /id="PRO_0000376871"
FT DOMAIN 321..587
FT /note="Ku"
FT DOMAIN 697..733
FT /note="SAP"
FT REGION 494..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 663..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..859
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..798
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 812..830
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 909 AA; 102003 MW; 143DF762FC65BDF2 CRC64;
MSGTNSWLNN NNNNSNTTLT NTNTIGGTNF GINQFDGDDW DNIFDGNNGD GDGDLDGDSY
KSYQNPYSYR DCIIFLIDAS KAMFEPNENN EIPFHNAVKC LIQTITDKII TSDSDLIGVC
FYNTNKKKNI NDFENIYVLS DLDIPDPKII LTLEEMLENS NFTTNGLGNC QGEMPFCDAL
WTCSTMFSNI KQSGSSSGEN SNNNNFKRIF LFTNEDNPNA YNDSIRNSSI QRSKDLSDLN
IQIELFSMNK SVNDKFDFSL FYQHILIFAD EENYLDPTQF DASSKFSDLR FKLKRKEFKK
RSLGKLPLYI GNLNNNNNNS NSLDSQVIIS TQLYNLFSHA HKSSPTLLDP KTNLPVKQLI
KNVCANTQAT LLPSQIKLCY HYGGEPVIFT KDEMQTIKSI DRIGFTLLGF KPLENIKPYH
SIKHSQFIFP DDQSIKGSVL AFNALVEQML KSGKAAICRF TPRSSSSPRM VALIPQEEIL
QSESEFNNQQ LLNSLSSQQQ QQQSSQQSSS SQQQQQQQQQ QQQQQQQQQQ QQLPSSSQQS
NNNRKIQIRP RGMHVIYLPF ADDIRYPNNI GVKSDGLEIK QENIDKAKNI IKMMKIKFDE
KKFVNPGLQK HYASLQAIAL ERDKVEETVD NIQPDRKLIE KVIDTTQDFS DGIFPVGYAS
TVSSATSSTS SSSAKRLRDG KDLSTMDWPD MVKSGEIIKL TVDDLKSFLS NQNIKPSSKA
KKADLIDLIS NLISGGNFKP DKLHLLKKDS PPLSDNTITT NGGDDDDNNR PSKKVKSTST
STTASKNTSS SSPPLVSAAT MNKKAPPKKS FSVKDKNSSN NSSGGSSKAN VNDEFDIDFK
NSDQDDDTDN ESDVNNKATT STTTITTTTA APKKNNFVNN GMFDTRELCK YGKNCYRTNK
QHLDEYRHQ
