ID A0A0J8R9Z2_COCIT Unreviewed; 317 AA. AC A0A0J8R9Z2; DT 14-OCT-2015, integrated into UniProtKB/TrEMBL. DT 14-OCT-2015, sequence version 1. DT 25-MAY-2022, entry version 24. DE RecName: Full=DNA helicase {ECO:0000256|ARBA:ARBA00012551}; DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551}; GN ORFNames=CISG_09377 {ECO:0000313|EMBL:KMU81909.1}; OS Coccidioides immitis RMSCC 3703. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides. OX NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU81909.1, ECO:0000313|Proteomes:UP000054559}; RN [1] {ECO:0000313|Proteomes:UP000054559} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559}; 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. {ECO:0000256|ARBA:ARBA00024890}. 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 Evidence={ECO:0000256|ARBA:ARBA00001665}; CC -!- SUBUNIT: Heterodimer of Ku70 and Ku80. {ECO:0000256|ARBA:ARBA00011584}. CC -!- SUBCELLULAR LOCATION: Chromosome, telomere CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus CC {ECO:0000256|ARBA:ARBA00004123}. 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; DS268208; KMU81909.1; -; Genomic_DNA. DR STRING; 454286.A0A0J8R9Z2; -. DR EnsemblFungi; KMU81909; KMU81909; CISG_09377. DR Proteomes; UP000054559; Unassembled WGS sequence. DR GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell. DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC. 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 Gene3D; 2.40.290.10; -; 1. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom. DR InterPro; IPR005161; Ku_N. 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 SUPFAM; SSF100939; SSF100939; 1. DR SUPFAM; SSF53300; SSF53300; 1. DR PROSITE; PS50234; VWFA; 1. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Chromosome {ECO:0000256|ARBA:ARBA00022454}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW Helicase {ECO:0000256|ARBA:ARBA00022806}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleus {ECO:0000256|ARBA:ARBA00023242}; KW Reference proteome {ECO:0000313|Proteomes:UP000054559}; KW Telomere {ECO:0000256|ARBA:ARBA00022895}. FT DOMAIN 1..137 FT /note="VWFA" FT /evidence="ECO:0000259|PROSITE:PS50234" SQ SEQUENCE 317 AA; 34965 MW; EA088B5A6B9E2D19 CRC64; MAEKEATVYI VDVSTGRKTA TVGVVGLRTD GSSNPLWEKD EEESYAHLSV FQEIGQMLMP DIRKLRDLVK PSNTNQGDAI SSIILAIDMI VRYCKRLKYK RKIVLVTDGR STMDSDGIDS IVSKIKEEGI ELVILGVDFD DPDYGFKEED KDPFKVNTCR REMTTPRIKV VRGIPSFRGD LRLGDPSQYS TGLTIQVERY YRTYVARPPA ASAFALSIAP PKGQSTAESS VTLQNGDSTV ETASASNNLS GVRNARSYQV IDENAPGGKK EVEQDDLAKG YEYGRTAVHI SESDEVITKL DTTAALEFIG FIQSENV //