ID A0A0C3CWD6_HEBCY Unreviewed; 824 AA.
AC A0A0C3CWD6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 22-FEB-2023, entry version 32.
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 ORFNames=M413DRAFT_22955 {ECO:0000313|EMBL:KIM48464.1};
OS Hebeloma cylindrosporum h7.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Agaricineae; Hymenogastraceae; Hebeloma.
OX NCBI_TaxID=686832 {ECO:0000313|EMBL:KIM48464.1, ECO:0000313|Proteomes:UP000053424};
RN [1] {ECO:0000313|EMBL:KIM48464.1, ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RA Kuo A., Gay G., Dore J., Kohler A., Nagy L.G., Floudas D., Copeland A.,
RA Barry K.W., Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A.,
RA Lipzen A., Lundell T., Morin E., Murat C., Sun H., Tunlid A., Henrissat B.,
RA Grigoriev I.V., Hibbett D.S., Martin F., Nordberg H.P., Cantor M.N.,
RA Hua S.X.;
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000053424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=h7 {ECO:0000313|Proteomes:UP000053424};
RG DOE Joint Genome Institute;
RG Mycorrhizal Genomics Consortium;
RA Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- 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; KN831769; KIM48464.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C3CWD6; -.
DR STRING; 686832.A0A0C3CWD6; -.
DR HOGENOM; CLU_010975_1_0_1; -.
DR OrthoDB; 5884at2759; -.
DR Proteomes; UP000053424; 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: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; 1.10.1600.10; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 1.25.40.240; Ku, C-terminal domain; 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; 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; 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 Pfam; PF08785; Ku_PK_bind; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF101420; C-terminal domain of Ku80; 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:UP000053424};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 346..481
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT REGION 306..341
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 801..824
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..341
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 824 AA; 92214 MW; DC6E7C05A8FB5923 CRC64;
MPAERAGYTV TMFLVDVSSS MGNVRTLEVE SSDGETHTVE MTNLAWGLQY VKLKIQDMIF
NNRKTEQCGV IIFGSEETKN VVNTANGGYE NVVEYIPIGQ PNASTMAKIN ALEASTTSGD
HRLPFSQTGR YLASKKTWTR KIVIVTDGES PIEVEDWEAT VQKMDSLNVS LTVVGIDFDD
ESFPYIEPGK SNIKAQNEKF YHTLTSSMQS GIVGTCAYAI QETTMPDVKQ VRSALMGTVL
RIGDVDARAD EAVELSVKAS KCNALQRPKG WKKFALREDK DEEMEEEEID PDKTVFAQLR
MRTEYYVDRN PEDDTDEDGD VKMKQEPGED ETLLESGEKD PDVQNLEKVE KEELVRGFKY
GTTYAPCPDG QFPKLQTRKG IDICGFFPRK NFRRELSMGE IQYIWAEPTS PQQQVALSSI
AQAMLEKECM AIARWVSRDG MDPKMGVLVP GEFEKVDCLL WSPMPFADDV RKYTFASLDH
LVNKKGEVLT EHPYLPTKEQ LEAMDNFVDA MDLMDAGEKD EEGNRTPWFN TLDSYSPAIH
RVKQAMFHCA VVNDITTNPL PPPHPELLKY FEPPKKVLKR SKEPLEECKN IFKVKEIPKK
VAKAKKDGHV HAQDEDDNML LLDHKRPLGA SASQMSIVEN SISAAAKGKA PAEESETEDE
EEEELLLNKK KATPPPKKGV PFPTPARSVS PHVDPGRAPG RIVGNTYPLK DFQKNISQGD
VVTKAVEDLA AVIAEVIMKP LAARRTQEML ECMEALRRTC LEEDEIDAWN LDLKKKCSSK
PGNPAFWEGV KEVGRDLSLI SNQEAKKQGG KSDVTENEAG EFLS
//
