ID   KU70_YARLI              Reviewed;         585 AA.
AC   Q6CCK2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=ATP-dependent DNA helicase II subunit 1;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent DNA helicase II subunit Ku70;
GN   Name=KU70; OrderedLocusNames=YALI0C08701g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase.
CC       Involved in non-homologous end joining (NHEJ) DNA double strand break
CC       repair. DNA-binding is sequence-independent but has a high affinity to
CC       nicks in double-stranded DNA and to the ends of duplex DNA. Binds to
CC       naturally occurring chromosomal ends, and therefore provides
CC       chromosomal end protection. Required also for telomere recombination to
CC       repair telomeric ends in the absence of telomerase. KU70, of the
CC       KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA
CC       component of telomerase. Involved in telomere maintenance. Interacts
CC       with telomeric repeats and subtelomeric sequences thereby controlling
CC       telomere length and protecting against subtelomeric rearrangement.
CC       Maintains telomeric chromatin, which is involved in silencing the
CC       expression of genes located at the telomere. Required for mating-type
CC       switching (By similarity). {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}. Chromosome, telomere
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
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; CR382129; CAG81913.1; -; Genomic_DNA.
DR   RefSeq; XP_501610.1; XM_501610.1.
DR   AlphaFoldDB; Q6CCK2; -.
DR   SMR; Q6CCK2; -.
DR   STRING; 4952.CAG81913; -.
DR   EnsemblFungi; CAG81913; CAG81913; YALI0_C08701g.
DR   GeneID; 2910012; -.
DR   KEGG; yli:YALI0C08701g; -.
DR   VEuPathDB; FungiDB:YALI0_C08701g; -.
DR   HOGENOM; CLU_014815_3_0_1; -.
DR   InParanoid; Q6CCK2; -.
DR   OMA; PNDMMGI; -.
DR   Proteomes; UP000001300; Chromosome C.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043564; C:Ku70:Ku80 complex; IBA:GO_Central.
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: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:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
DR   Gene3D; 2.40.290.10; -; 1.
DR   Gene3D; 3.40.50.410; -; 1.
DR   Gene3D; 4.10.970.10; -; 1.
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; 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   PIRSF; PIRSF003033; Ku70; 1.
DR   SMART; SM00559; Ku78; 1.
DR   SUPFAM; SSF100939; SSF100939; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Chromosome; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW   Reference proteome; Telomere.
FT   CHAIN           1..585
FT                   /note="ATP-dependent DNA helicase II subunit 1"
FT                   /id="PRO_0000278347"
FT   DOMAIN          239..444
FT                   /note="Ku"
FT   REGION          514..537
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        515..529
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   585 AA;  66611 MW;  44EEC5BD7C15E4ED CRC64;
     MEWISHLEND DDVLEIEDYK VRKDALLIAI QVTQNAINNG TLHKALEAAF DAVTDRIVIS
     PQDYTGVMLF GASMQSEDDG DEFDDESDTH FILKLGLPTA AQIKRLKRLA EDPDLGERFK
     VQEEPHLMDV FFDMNRHFIN MAPNFASRRI IYITDDDTPT TNEDDINKTR VRIEDLSHLK
     VKVEPLLINP SEDKTFDSSK FYALVFNEDT SVEPVEAIDL KQFINKRNVL NRSLFNVKME
     IGEGLVVGVR GYLLYAEQKA TSTTRKAWVY TGGEKPEIAK LESQAVTIES GRSVDKADLR
     KTFKFGNDYV PFTEEQLTQI RYFGEPIIRI LGFHNSSDFS ELFIHSVRSS MFLYPTDEKL
     VGSIRAFSAL YQSLKNKDKM ALAWVIVRKG AKPILALLIP STKEIEGLHM VFLPFTDDIR
     QEPKTELVSA APELVDATKN IFTRLRMPGG FESQRYPNPR LQWHYRVVRA MALQEEVPKV
     PEDKTTPKYR SIDTRVGDAI EEWNKVLQSS SKRPAEDICK AEKKVKSSDA GPPSNEQMQN
     MVENDIVGKL TVAELRAWGA ANNVEPNGSK LKKDWVEVVK KYYGK