ID   KU70_KLULA              Reviewed;         592 AA.
AC   Q6CUB4;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=KLLA0C06226g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR   EMBL; CR382123; CAH01326.1; -; Genomic_DNA.
DR   RefSeq; XP_452475.1; XM_452475.1.
DR   AlphaFoldDB; Q6CUB4; -.
DR   SMR; Q6CUB4; -.
DR   STRING; 28985.XP_452475.1; -.
DR   EnsemblFungi; CAH01326; CAH01326; KLLA0_C06226g.
DR   GeneID; 2892291; -.
DR   KEGG; kla:KLLA0_C06226g; -.
DR   eggNOG; KOG2327; Eukaryota.
DR   HOGENOM; CLU_024202_0_0_1; -.
DR   InParanoid; Q6CUB4; -.
DR   OMA; PNDMMGI; -.
DR   Proteomes; UP000000598; Chromosome C.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043564; C:Ku70:Ku80 complex; IEA:EnsemblFungi.
DR   GO; GO:0005635; C:nuclear envelope; IEA:EnsemblFungi.
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:0070034; F:telomerase RNA binding; IEA:EnsemblFungi.
DR   GO; GO:0042162; F:telomeric DNA binding; IEA:InterPro.
DR   GO; GO:0000727; P:double-strand break repair via break-induced replication; IEA:EnsemblFungi.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   GO; GO:0097695; P:establishment of protein-containing complex localization to telomere; IEA:EnsemblFungi.
DR   GO; GO:0097552; P:mitochondrial double-strand break repair via homologous recombination; IEA:EnsemblFungi.
DR   GO; GO:0030466; P:silent mating-type cassette heterochromatin assembly; IEA:EnsemblFungi.
DR   GO; GO:0031509; P:subtelomeric heterochromatin assembly; IEA:EnsemblFungi.
DR   GO; GO:0000723; P:telomere maintenance; IEA:EnsemblFungi.
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..592
FT                   /note="ATP-dependent DNA helicase II subunit 1"
FT                   /id="PRO_0000278344"
FT   DOMAIN          280..485
FT                   /note="Ku"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   592 AA;  68666 MW;  8342375A40641E26 CRC64;
     MSFEQPDFLK SQLTQTRDDD KESDHKKWRR YEAHDGIVFC IQLTPTMYLS NPDLGGKIQL
     LEILDSLNDL MSQLVVVMPS TAVGCYIYNC SHPNAEDNVY ELIPLRDVNY KNMKRVSDLL
     EDIEQDRILL KDEIPIADPN NPIELSPVLI KVRETFLQPI EGQKQLTNKK IFFFTDDDKP
     AEFLNVDSRS RLRKVVDDLY DYYINFVTFF IGSEDKPFDD SMYADILKWG SKINEAQSWL
     SSHGPSTNPI NASYIKSKVK RTKEIKRIKF RCPLMLDERA DLVVSVNGYT IVSHEIPGSK
     YKLVYANGSV RREAYSHREY LDAETGEAVD NSQLSKVYTF GDEIIELTED ENLKIQSGYS
     EHESFLKLIG FRSTEQCLHY YDNIDVPAFV VPNEEDYAGS IKTLASLYRT MLFKKKSAMV
     WGKLRPNSPP SMFVLTPSSK KDYNQGFYLY KVPFMEEVRK LPDFLNHSAL IESDDYKVMS
     KVTETLINFF NLKNGYRPSD FHNPALQKHF KILREYLLQI EVDKSKPEDE GDETLQKVKQ
     IYARIASSAK SDDVKQQRLV KYLKLWNSFY NRLSNLEVDT KPTKNKKAKL NL