ID A0A0P1BSX8_9BASI Unreviewed; 891 AA.
AC A0A0P1BSX8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 22-FEB-2023, entry version 28.
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};
OS Ceraceosorus bombacis.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Ceraceosorales; Ceraceosoraceae; Ceraceosorus.
OX NCBI_TaxID=401625 {ECO:0000313|EMBL:CEH19188.1, ECO:0000313|Proteomes:UP000054845};
RN [1] {ECO:0000313|EMBL:CEH19188.1, ECO:0000313|Proteomes:UP000054845}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Magalhaes I.L.F., Oliveira U., Santos F.R., Vidigal T.H.D.A.,
RA Brescovit A.D., Santos A.J.;
RL Submitted (SEP-2014) 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; CCYA01000277; CEH19188.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P1BSX8; -.
DR STRING; 401625.A0A0P1BSX8; -.
DR OrthoDB; 5884at2759; -.
DR Proteomes; UP000054845; 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:0016301; F:kinase 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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, ECO:0000313|EMBL:CEH19188.1};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Kinase {ECO:0000313|EMBL:CEH19188.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000054845};
KW Telomere {ECO:0000256|ARBA:ARBA00022895};
KW Transferase {ECO:0000313|EMBL:CEH19188.1}.
FT DOMAIN 410..550
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT REGION 675..768
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 696..712
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..728
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 891 AA; 99641 MW; 255AC718F0B6F32E CRC64;
MSLASTITTF LIDVSPSMGA LRIVAEDVED ANDQEEATRL DEGDRVRAED GMDGELNDAD
GSKRTLGEWK VRERETSNLQ WACEFVGRRV QTYVHAGLKT GKVCLITYGS ATTNNAVAGD
GTTKQEYLGI NEMFSPAQPD LNTCELVRAL RASKDSEEPH RADPLDALIA AICTLTDKDR
GGINSSSKNT WTRTIYLITD AMTKFNQDDS ALIQQRLEEE NIQLKVIGID FDDEEFGYVE
EDKPLTKAKN EQFWHDFLSR VPGSGIATAA DVIEQTHMPQ LAPKKSAAQN ATLTFGDPEE
QHLSHEVLGI AVVLYKATTL VRPMSAKKLS KIAQQSAAGK AEMERAAQMK IEPSSAPKLQ
PNQELEGSNP AFIDGEAHAM SYGVDMVRKY FILDEIRQLP KEEMDSAQPL PEGSEENFIK
AWKLGKSHIP VEQVQDVVFA TQAGLEIIQF HNREQLRRWF VMGETSYVLA SPGNGEAQLK
VSALVKAMIE LGKIALVRNV KKRDADPKLA ALIPIPKDPE SGSEADHFVY AEMPFANDFK
RLVFPPLEYV VDRNGVEHRE HHLLPTREMQ SAMDDLVDSM DLMEAYEEPD GSRSEWFSTE
DSFNPAIHRI KEAVEWRVFH PEDKELPKAH FELDKFLKRP ETVWNKSSTL AAQLKDLFEL
DYSPDANIQR QEMFREQKRK REEEAAANAK KQASNGAEGK VEKKKGDGDD EEGDKTLILD
ENDDSATDEE EAQSARPSKA TRAGSADRPT KTGAGPHRAQ GDVSIGTNDP VADFRRALQD
ARDPAVVIRA MCQRIRQLVS ESMASNSYGK ARDSMKVCRA EAAVEDEAEE WNEFVRKFKN
DLQQPTFGRR ARRDFWDGYV RGMMEVGLIT MQEDAGGRSR VDSKEAKDFV S
//
