ID   KU70_RHIAP              Reviewed;         600 AA.
AC   Q26228;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=ATP-dependent DNA helicase 2 subunit 1;
DE            EC=3.6.4.12;
DE   AltName: Full=ATP-dependent DNA helicase II 70 kDa subunit;
DE   AltName: Full=ATP-dependent DNA helicase II subunit Ku70;
DE   AltName: Full=Ku autoantigen protein p70 homolog;
GN   Name=ku70;
OS   Rhipicephalus appendiculatus (Brown ear tick).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC   Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Rhipicephalinae;
OC   Rhipicephalus; Rhipicephalus.
OX   NCBI_TaxID=34631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Salivary gland;
RX   PubMed=8597595; DOI=10.1016/0167-4781(95)00230-8;
RA   Paesen G.C., Zanotto P.M., Nuttall P.A.;
RT   "A tick homologue of the human DNA helicase II 70-kDa subunit.";
RL   Biochim. Biophys. Acta 1305:120-124(1996).
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 a 70 kDa and a 80 kDa subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
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DR   EMBL; L41356; AAC41612.1; -; mRNA.
DR   PIR; S65788; S65788.
DR   AlphaFoldDB; Q26228; -.
DR   SMR; Q26228; -.
DR   PRIDE; Q26228; -.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0043564; C:Ku70:Ku80 complex; IEA:InterPro.
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; 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   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; 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; IPR003034; SAP_dom.
DR   InterPro; IPR036361; SAP_dom_sf.
DR   InterPro; IPR016194; SPOC-like_C_dom_sf.
DR   InterPro; IPR002035; VWF_A.
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   SMART; SM00513; SAP; 1.
DR   SMART; SM00327; VWA; 1.
DR   SUPFAM; SSF100939; SSF100939; 1.
DR   SUPFAM; SSF53300; SSF53300; 1.
DR   SUPFAM; SSF68906; SSF68906; 1.
DR   TIGRFAMs; TIGR00578; ku70; 1.
DR   PROSITE; PS50800; SAP; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Chromosome; DNA damage; DNA recombination; DNA repair;
KW   DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus.
FT   CHAIN           1..600
FT                   /note="ATP-dependent DNA helicase 2 subunit 1"
FT                   /id="PRO_0000210182"
FT   DOMAIN          247..456
FT                   /note="Ku"
FT   DOMAIN          564..598
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   REGION          524..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   600 AA;  67405 MW;  29E7A24903B3D728 CRC64;
     MDQPWMRQDD DESDDESSTV DFGQAVDGIL FLIDATEGMF EEVDGDTAFM QCIKAAKSTM
     LNKITSSPKD LVGIILFGTD KDNNPNRFKN VYVLQDLESP GAESVLKLEK LIADGPKKFK
     QEYGHGNVNM ADVLWTCALM FSKSRAGQRR VLVLTNQDDP HKGSGDLDDK AVVKAKDLLQ
     SGIELDLVHL KPPGDKKFRP QILYKNLVTD KENYEDGFPE ASDKMEELLL RVRMKDHKKR
     RLMSLPFWLG PEVKMSVSLY NLVRPTGKPA TTRLARDNNE ELLSRRITYA MDSAEALMPG
     DISKTQEYGG RKAYFDICEV KQIKSMAPPG LQLLGFKPLS YLEKQPHVRP SHFVYPDEGS
     VRGSTRLFAA LLQSCLRHRV APICFWISRA AQAPKLVYLL AQEEERDPHG LQMVPPGFHV
     VQLPFSDDRR RLQALQEGTT KATPGLVALA REMAEKLRFT YHPDKFENPE LQGFWSCLEA
     LALDRDDAEH PKDYTRPDHE KMKAKAGEEM DAFLEAAFPD GCSATTAGSR KRTQAGEGGQ
     AKKARSENQG SNVDVREEAK RGKLASLTVS VLRDFCKQEG LRCPSKKAEI VDCIKKHLKL