ID   KU80_COCIM              Reviewed;         731 AA.
AC   Q1E6K9; J3KKC6;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 91.
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; ORFNames=CIMG_01804;
OS   Coccidioides immitis (strain RS) (Valley fever fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=246410;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RS;
RX   PubMed=19717792; DOI=10.1101/gr.087551.108;
RA   Sharpton T.J., Stajich J.E., Rounsley S.D., Gardner M.J., Wortman J.R.,
RA   Jordar V.S., Maiti R., Kodira C.D., Neafsey D.E., Zeng Q., Hung C.-Y.,
RA   McMahan C., Muszewska A., Grynberg M., Mandel M.A., Kellner E.M.,
RA   Barker B.M., Galgiani J.N., Orbach M.J., Kirkland T.N., Cole G.T.,
RA   Henn M.R., Birren B.W., Taylor J.W.;
RT   "Comparative genomic analyses of the human fungal pathogens Coccidioides
RT   and their relatives.";
RL   Genome Res. 19:1722-1731(2009).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=RS;
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAS36450.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; GG704911; EAS36450.3; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001248033.2; XM_001248032.2.
DR   AlphaFoldDB; Q1E6K9; -.
DR   STRING; 246410.Q1E6K9; -.
DR   EnsemblFungi; EAS36450; EAS36450; CIMG_01804.
DR   GeneID; 4566627; -.
DR   KEGG; cim:CIMG_01804; -.
DR   InParanoid; Q1E6K9; -.
DR   OrthoDB; 598957at2759; -.
DR   Proteomes; UP000001261; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; 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   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; IPR005161; Ku_N.
DR   InterPro; IPR014893; Ku_PK_bind.
DR   InterPro; IPR016194; SPOC-like_C_dom_sf.
DR   InterPro; IPR002035; VWF_A.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   Pfam; PF02735; Ku; 1.
DR   Pfam; PF03731; Ku_N; 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   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..731
FT                   /note="ATP-dependent DNA helicase II subunit 2"
FT                   /id="PRO_0000278352"
FT   DOMAIN          238..486
FT                   /note="Ku"
SQ   SEQUENCE   731 AA;  82008 MW;  E580014E490FBEE8 CRC64;
     MAEKEATVYI VDVGHSMGKC RGGRTISDLD WMMLYVWDRI TTTVSTGRKT ATVGVVGLRT
     DGSSNPLWEK DEEESYAHLS VFQEIGQMLM PDIRKLRDLV KPSNTNQGDA ISSIILAIDM
     IVRYCKRLKY KRKIVLVTDG RSTMDSDGID SIVSKIKEEG IELVILGVDF DDPDYGFKEE
     DKDPFKTKNE SVLKILADDA DGAYGTLAQA VEEMTTPRIK VVRGIPSFRG DLRLGDPSQY
     STGLTIQVER YYRTYVARPP AASAFALSIA PPKGQSTAES SVTLQNGDST VETANASNNL
     SGVRNARSYQ VIDENAPGGK KEVERDDLAK GYEYGRTAVH ISESDEVITK LDTTAALEFI
     GFIQSENYER YMNMSTSNVI IAQKINDKAI LALSSMIHAL FELEYYAIGR LVTKDGKPPL
     MVLLAPLIET DFECLLEVQL PFAEDTRSYR FPPLDKIVTV SGKVVKEHRN LPSDDLLETM
     GKYVEDMDLS EFDENGDPFQ SLALEDCYSP LVHRIDQAIR WRAVHPTKPL PPVPKVLEKL
     SHWPEELVKK SHDSLRDLIS ISAVKKVPPK AKGRKRRREA DKPLSGLNVD DLLRGEKRLK
     ISPENPIPEF KQTLANTEDI SAISDAVKQM SAIIEDQIRQ SLGDINYDRA IEGIGTMREE
     LIAYEEPGLY NDFIRGLKEK LLDDKLGGDR REMWWLIRKS RLGLIDQKAL DISDITEEQA
     REFLSSRPTT V