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KU80_YARLI
ID   KU80_YARLI              Reviewed;         726 AA.
AC   Q6C7B9;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 100.
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;
GN   Name=KU80; OrderedLocusNames=YALI0E02068g;
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 ku80 family. {ECO:0000305}.
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DR   EMBL; CR382131; CAG79022.1; -; Genomic_DNA.
DR   RefSeq; XP_503443.1; XM_503443.1.
DR   AlphaFoldDB; Q6C7B9; -.
DR   SMR; Q6C7B9; -.
DR   STRING; 4952.CAG79022; -.
DR   EnsemblFungi; CAG79022; CAG79022; YALI0_E02068g.
DR   GeneID; 2912079; -.
DR   KEGG; yli:YALI0E02068g; -.
DR   VEuPathDB; FungiDB:YALI0_E02068g; -.
DR   HOGENOM; CLU_010975_1_1_1; -.
DR   InParanoid; Q6C7B9; -.
DR   OMA; WAMQYVW; -.
DR   Proteomes; UP000001300; Chromosome E.
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   CDD; cd00873; KU80; 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; IPR016194; SPOC-like_C_dom_sf.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF02735; Ku; 1.
DR   PIRSF; PIRSF016570; Ku80; 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..726
FT                   /note="ATP-dependent DNA helicase II subunit 2"
FT                   /id="PRO_0000278356"
FT   DOMAIN          248..475
FT                   /note="Ku"
FT   REGION          591..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   726 AA;  81612 MW;  EDF19A198B33B969 CRC64;
     MASKEATVYV VDLHESMGRE MARGHDSKEV TDLNWGLQYI YSEISNKILS GRKTDVVGLV
     GVHTDTTQNM FEEESGFEHI DIITPIQQFN LDTLLEAKKQ LVPNSDNKGD LISGIVVAVQ
     MIKLYTKALK YIRNIVVLTN GQGNMNLGDS GGIIKQLNEN RIILKVMGVD FDDEEVDYFE
     EDKPEHKREN ELKLKEFVDR CEDSVFATYK EARDSLDIPK VKAVNPVRAF QGNLVLSDPE
     QQPPQRVMSI GVEVFPCTRR ATAMTASSYA MSKIEPATIS TPSQNNLQAV KWDRQYYVND
     ESGIGGKKEL DRDTLENGYR YGSEIVYITK EEEEAIMFPT SASLQVIGFV NKKSVPPYML
     MGHTDYIIGQ RGNNRDAVAI SAFARALFET DNFGLARYVN KDGKDPQIVV LMPYIRAELE
     GLVFCQLPFA EDERKFILPS LTSLETRSGN KTVTTHSRLL PTKEMLDAMD DYVDAMDLSK
     LKGEDDEPWL TMEECFNPSI HHIRNVVKEC AVSQDYGKIP EPLPILTRFS QPAEELTEEA
     KPQLELLKHL FDIKEQFREA KKRKTEVTVG QTGLDLDALL EGELEVKLES SQTLSSNVKS
     EPGRQTASQS SQNSQQLSLD PENICPDFIR TLNKIDTKAT SDEEFRSGAT NLYKQTITLL
     EEKLESSKGN DAYNEIIGVL QTMREQADEM EIPDVFTAAK GQFVSKLERG DLGGQKNVLV
     AQINSI
 
 
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