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Database: UniProt
Entry: Q6BXN4_DEBHA
LinkDB: Q6BXN4_DEBHA
Original site: Q6BXN4_DEBHA 
ID   Q6BXN4_DEBHA            Unreviewed;       723 AA.
AC   Q6BXN4;
DT   16-AUG-2004, integrated into UniProtKB/TrEMBL.
DT   04-NOV-2008, sequence version 2.
DT   24-JAN-2024, entry version 94.
DE   RecName: Full=ATP-dependent DNA helicase II subunit 2 {ECO:0000256|ARBA:ARBA00021792};
DE            EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE   AltName: Full=ATP-dependent DNA helicase II subunit Ku80 {ECO:0000256|ARBA:ARBA00031847};
GN   OrderedLocusNames=DEHA2B01584g {ECO:0000313|EMBL:CAG85021.2};
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592 {ECO:0000313|EMBL:CAG85021.2, ECO:0000313|Proteomes:UP000000599};
RN   [1] {ECO:0000313|EMBL:CAG85021.2, ECO:0000313|Proteomes:UP000000599}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC
RC   2968 {ECO:0000313|Proteomes:UP000000599};
RX   PubMed=15229592; DOI=10.1038/nature02579;
RG   Genolevures;
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., Straub M.L.,
RA   Suleau A., Swennene D., Tekaia F., Wesolowski-Louvel M., Westhof E.,
RA   Wirth B., Zeniou-Meyer M., Zivanovic I., Bolotin-Fukuhara M., Thierry A.,
RA   Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J.,
RA   Wincker P., Souciet J.L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC       {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC       {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ku80 family.
CC       {ECO:0000256|ARBA:ARBA00007726}.
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DR   EMBL; CR382134; CAG85021.2; -; Genomic_DNA.
DR   RefSeq; XP_457035.2; XM_457035.1.
DR   AlphaFoldDB; Q6BXN4; -.
DR   STRING; 284592.Q6BXN4; -.
DR   GeneID; 2913188; -.
DR   KEGG; dha:DEHA2B01584g; -.
DR   VEuPathDB; FungiDB:DEHA2B01584g; -.
DR   eggNOG; KOG2326; Eukaryota.
DR   HOGENOM; CLU_023247_0_0_1; -.
DR   InParanoid; Q6BXN4; -.
DR   OMA; DIRGFMD; -.
DR   OrthoDB; 2056550at2759; -.
DR   Proteomes; UP000000599; Chromosome B.
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:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; 2.40.290.10; -; 1.
DR   Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR   InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR   InterPro; IPR024193; Ku80.
DR   InterPro; IPR005161; Ku_N.
DR   InterPro; IPR016194; SPOC-like_C_dom_sf.
DR   InterPro; IPR036465; vWFA_dom_sf.
DR   PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1.
DR   PANTHER; PTHR12604:SF4; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 5; 1.
DR   Pfam; PF02735; Ku; 1.
DR   Pfam; PF03731; Ku_N; 1.
DR   SMART; SM00559; Ku78; 1.
DR   SUPFAM; SSF100939; SPOC domain-like; 1.
DR   SUPFAM; SSF53300; vWA-like; 1.
PE   3: Inferred from homology;
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:UP000000599};
KW   Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT   DOMAIN          337..480
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
FT   REGION          305..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        319..335
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   723 AA;  81574 MW;  C4B4DBE5BF0C06FA CRC64;
     MASKEVTTFI VDLSPSMANK SNGRNISDLE YGLKYFYDIV TNKILRGRKT DYISVITCHS
     NRTENPFSSE DSFKNIEVVS NKIAPTYDDL RKYKELLCPN KTEITEDEGD CFESMLVGIG
     LLKDTQKLKF VRNVVVITNA ESKIKSFETK VADATRNAIN EMNINVVLNG IDFDVDGLKY
     PDKSPEKAKN ESGWASVFHT YKTSEVYTTA QIVESILHNP PLKKVKPMRA FKGQLRFGSD
     HCNQNENSDY APELDQTCIS LNVELYPALK AEKLASGHQY TIDPANGSVD KTKYVKDYFI
     KSVSSKDEDG KDDDEEVQKR RYDDDDDDED KDGDLETVSI DANEWTDGFK YSNYDLLTLD
     EDLLNSAKLA SDPGMDILGF IKMDDLPYAY LTGESYYLLP EVSCSYKNLV GFNGLCQSLV
     DLEGLALIRY VQKPNDEIKV CILIPSKIKV NESFVYAFIL VRLPFREDEK IGKFPLLTSI
     MTTSGKSFTS NTDSPDENPI KQENDEESSN ETNLPNAATN SLMESFILSR DLDTKGKNKD
     NESNDSDTFF VENNKVTLSN DSLISFPKLS HFGVSSRLLV SSPAIHKFNL NIKKIIIKSL
     EDGNLHEYLN NPNFIRDNLI SNENDNSGPS TNLFNLSNVL KINSTTNDEW LTDVNKNSKN
     VAKKLIKELD TKYVKQEVEA KKKRKMLNNN NLNDIFMMKN AQGNYGAGEG EYEALPDIND
     LLN
//
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