KU80_SCHPO
ID KU80_SCHPO Reviewed; 695 AA.
AC Q9HGM8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=ATP-dependent DNA helicase II subunit 2;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent DNA helicase II subunit Ku80;
DE AltName: Full=Pombe Ku80;
GN Name=pku80; Synonyms=ku80; ORFNames=SPBC543.03c;
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, INTERACTION WITH PKU70, 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 [3]
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. 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, 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. Chromosome, telomere.
CC -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000305}.
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DR EMBL; CU329671; CAC05245.1; -; Genomic_DNA.
DR RefSeq; NP_596791.1; NM_001023811.2.
DR AlphaFoldDB; Q9HGM8; -.
DR SMR; Q9HGM8; -.
DR BioGRID; 277560; 42.
DR STRING; 4896.SPBC543.03c.1; -.
DR MaxQB; Q9HGM8; -.
DR PaxDb; Q9HGM8; -.
DR PRIDE; Q9HGM8; -.
DR EnsemblFungi; SPBC543.03c.1; SPBC543.03c.1:pep; SPBC543.03c.
DR GeneID; 2541045; -.
DR KEGG; spo:SPBC543.03c; -.
DR PomBase; SPBC543.03c; pku80.
DR VEuPathDB; FungiDB:SPBC543.03c; -.
DR eggNOG; KOG2326; Eukaryota.
DR HOGENOM; CLU_010975_1_1_1; -.
DR InParanoid; Q9HGM8; -.
DR OMA; WAMQYVW; -.
DR PhylomeDB; Q9HGM8; -.
DR Reactome; R-SPO-6798695; Neutrophil degranulation.
DR PRO; PR:Q9HGM8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0043564; C:Ku70:Ku80 complex; ISO:PomBase.
DR GO; GO:0005634; C:nucleus; HDA: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:0000723; P:telomere maintenance; IMP:PomBase.
DR CDD; cd00873; KU80; 1.
DR Gene3D; 1.25.40.240; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR024193; Ku80.
DR InterPro; IPR036494; Ku_C_sf.
DR InterPro; IPR014893; Ku_PK_bind.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF08785; Ku_PK_bind; 1.
DR PIRSF; PIRSF016570; Ku80; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF101420; SSF101420; 1.
DR SUPFAM; SSF53300; SSF53300; 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..695
FT /note="ATP-dependent DNA helicase II subunit 2"
FT /id="PRO_0000255456"
FT DOMAIN 229..461
FT /note="Ku"
SQ SEQUENCE 695 AA; 79871 MW; 2FA77B1FD1401CAA CRC64;
MSDKECTVFV LDLGKDMGTC HHGRSHSDLE WTLSYFHDEL SHKFLANRKT DVVGIVGYKC
DDTKNDLAEQ EAYWNISVLY PIQTALFSKL QSVSQTLKPS NTMQGDLISA IVVSFDLMAR
HCKKNKWKKK MIVLTAARGI IDFSDYIGIA EQLLQHDVFL GVYGVDFDQE DINYSEPLKE
SQKKENEVRI QEFVESCHGQ YCTFQQIYNN IGKPWVRKVR PVAIFRGTFS IGNRDSKDTS
ISIQVERYPR TRLTKPPTSS AFYENDMSKN YECLNIENSN VENKSMESDA VSTVRSYMVR
DPKTNDSFEV KREDLESGYS YGRTIVPISR SDEDVLALDT IPGYEILGFI PKSSLPIYYT
ISDTNIIVPK DDFESKLNFS AFVQSLEREH RYALARFVSK DKGVPVLLVL MPYVEFKRHY
LVDIQLPFAE DVRPYSFSEF EKLSNEEDMR QIDFAVSNYI DNMDLDSSDC GFNPPFEPEN
TFSMIPHRLQ QAISYYANSP EGDLPQPNIY LTRYTNPPKS LLDNCILDLK LIKEKLTVNV
PVKPKYSSQE TAFDTGAPIS EEQIEELLNS GLDEQEGEKL LVLHVSEKDP VGTFTEVLKN
PFGLEDALTE MEKVIKNLID KSKYDLALQS LQSLRLHSIL EDEVERFNEY LTRLKKDVMQ
NNKPKENELI NKIRSSGLDI ILHDELTRHD NFNNI
