ID   KU70_SCHPO              Reviewed;         607 AA.
AC   O94395;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 138.
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=pku70; Synonyms=ku70; ORFNames=SPCC126.02c;
OS   Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC   Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC   Schizosaccharomyces.
OX   NCBI_TaxID=284812;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=972 / ATCC 24843;
RX   PubMed=11859360; DOI=10.1038/nature724;
RA   Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA   Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA   Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA   Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA   Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA   Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA   Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA   Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA   O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA   Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA   Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA   Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA   Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA   Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA   Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA   Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA   Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA   Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA   Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA   Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA   del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA   Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA   Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA   Nurse P.;
RT   "The genome sequence of Schizosaccharomyces pombe.";
RL   Nature 415:871-880(2002).
RN   [2]
RP   FUNCTION IN TELOMERE MAINTENANCE.
RX   PubMed=11029034; DOI=10.1091/mbc.11.10.3265;
RA   Baumann P., Cech T.R.;
RT   "Protection of telomeres by the Ku protein in fission yeast.";
RL   Mol. Biol. Cell 11:3265-3275(2000).
RN   [3]
RP   FUNCTION IN TELOMERE MAINTENANCE, INTERACTION WITH PKU80, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=12424244; DOI=10.1074/jbc.m208813200;
RA   Miyoshi T., Sadaie M., Kanoh J., Ishikawa F.;
RT   "Telomeric DNA ends are essential for the localization of Ku at telomeres
RT   in fission yeast.";
RL   J. Biol. Chem. 278:1924-1931(2003).
RN   [4]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=16823372; DOI=10.1038/nbt1222;
RA   Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA   Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA   Yoshida M.;
RT   "ORFeome cloning and global analysis of protein localization in the fission
RT   yeast Schizosaccharomyces pombe.";
RL   Nat. Biotechnol. 24:841-847(2006).
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. Required for mating-type switching (By
CC       similarity). Involved in telomere maintenance. Interacts with telomeric
CC       repeats and subtelomeric sequences thereby controlling telomere length
CC       and protecting against subtelomeric rearrangement. Maintains telomeric
CC       chromatin, which is involved in silencing the expression of genes
CC       located at the telomere. {ECO:0000250, ECO:0000269|PubMed:11029034,
CC       ECO:0000269|PubMed:12424244}.
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 pku70 and pku80.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Chromosome, telomere
CC       {ECO:0000269|PubMed:12424244}.
CC   -!- SIMILARITY: Belongs to the ku70 family. {ECO:0000305}.
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DR   EMBL; CU329672; CAA22471.1; -; Genomic_DNA.
DR   PIR; T40906; T40906.
DR   RefSeq; NP_588445.1; NM_001023436.2.
DR   AlphaFoldDB; O94395; -.
DR   SMR; O94395; -.
DR   BioGRID; 275662; 32.
DR   STRING; 4896.SPCC126.02c.1; -.
DR   MaxQB; O94395; -.
DR   PaxDb; O94395; -.
DR   EnsemblFungi; SPCC126.02c.1; SPCC126.02c.1:pep; SPCC126.02c.
DR   PomBase; SPCC126.02c; pku70.
DR   VEuPathDB; FungiDB:SPCC126.02c; -.
DR   eggNOG; KOG2327; Eukaryota.
DR   HOGENOM; CLU_014815_3_0_1; -.
DR   InParanoid; O94395; -.
DR   OMA; PNDMMGI; -.
DR   PhylomeDB; O94395; -.
DR   Reactome; R-SPO-6798695; Neutrophil degranulation.
DR   PRO; PR:O94395; -.
DR   Proteomes; UP000002485; Chromosome III.
DR   GO; GO:0099115; C:chromosome, subtelomeric region; IDA:PomBase.
DR   GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR   GO; GO:0000792; C:heterochromatin; IDA:PomBase.
DR   GO; GO:0043564; C:Ku70:Ku80 complex; ISO:PomBase.
DR   GO; GO:0005634; C:nucleus; IDA:PomBase.
DR   GO; GO:0005721; C:pericentric heterochromatin; IDA:PomBase.
DR   GO; GO:0035861; C:site of double-strand break; IDA:PomBase.
DR   GO; GO:0043138; F:3'-5' DNA helicase activity; ISS:PomBase.
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:0042162; F:telomeric DNA binding; IDA:PomBase.
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; IMP:PomBase.
DR   GO; GO:0032208; P:negative regulation of telomere maintenance via recombination; IGI:PomBase.
DR   GO; GO:0031297; P:replication fork processing; IMP:PomBase.
DR   GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IMP:PomBase.
DR   GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
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; 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; PF02037; SAP; 1.
DR   PIRSF; PIRSF003033; Ku70; 1.
DR   SMART; SM00559; Ku78; 1.
DR   SMART; SM00513; SAP; 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   1: Evidence at protein level;
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..607
FT                   /note="ATP-dependent DNA helicase II subunit 1"
FT                   /id="PRO_0000255455"
FT   DOMAIN          241..452
FT                   /note="Ku"
FT   DOMAIN          570..604
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
SQ   SEQUENCE   607 AA;  69100 MW;  2C0DD5378E16118F CRC64;
     MENDEQIDET ENFAIGKYAI LFVIEVSPSM LDPVDEFTPS SLQMALICAY QLAAQRVITN
     PSDIMGVLLY GTESSTGRFA NQMMLLDIDP PDAERIKSLQ SFEKDFQFSK EKFKPCSCQV
     SLSSVLYHCS VIFTTKAENF EKRLFLITDN DHPAWDATER DIILQRAKDL RDLDIQVHPV
     FLDPPTHSFR INIFYSDFLY IVYGRQDVSN LVNRGQAQLQ HMLNMITALQ KPKRAHFHLK
     MDLGNDVRIG VEAFILLKRL ESAKTNWVYA KGERFAVAVP QSKQVSFATK KELKKDEIRR
     SYSYGGSSVV FGSDELNKVR SFEPPTLRII GFRDFSTLKP WHCLKPAVFL RPKDDEIIGS
     GAVFSAIHKK LLASNKIGIA WFVSRPNANP CFVAMLATPG SIHIRDDFEL PLGIFLVQLP
     TADDIRSLPP INPNPISMPS NLIETMQRIL RGMELRSYQP GKYNNPSLQW HYKVLQALAL
     DEEIPTDFVD NTLPKYKAIQ KRVGEYMGDV NNIVAEYRND ISDKNGIKEE EEDQGPIVKK
     ARIEKSGKPI FAEDDRLKQL YIEGVLDKEI KALKVSQLKD ILRDRGLRVS GKKADLLDNL
     TNYVKKL