KU70_ASPSO
ID KU70_ASPSO Reviewed; 655 AA.
AC Q2MHH3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=ATP-dependent DNA helicase II subunit 1;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent DNA helicase II subunit Ku70;
GN Name=ku70;
OS Aspergillus sojae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41058;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 46250;
RX PubMed=16428831; DOI=10.1271/bbb.70.135;
RA Takahashi T., Masuda T., Koyama Y.;
RT "Identification and analysis of Ku70 and Ku80 homologs in the koji molds
RT Aspergillus sojae and Aspergillus oryzae.";
RL Biosci. Biotechnol. Biochem. 70:135-143(2006).
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 ku70 family. {ECO:0000305}.
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DR EMBL; AB214650; BAE78502.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2MHH3; -.
DR SMR; Q2MHH3; -.
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 Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR Gene3D; 4.10.970.10; -; 1.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR027388; Ku70_bridge/pillars_dom_sf.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR036361; SAP_dom_sf.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
DR PANTHER; PTHR12604:SF2; PTHR12604:SF2; 1.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF02037; SAP; 1.
DR PIRSF; PIRSF003033; Ku70; 1.
DR SMART; SM00559; Ku78; 1.
DR SMART; SM00513; SAP; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
DR SUPFAM; SSF68906; SSF68906; 1.
DR TIGRFAMs; TIGR00578; ku70; 1.
DR PROSITE; PS50800; SAP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chromosome; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus; Telomere.
FT CHAIN 1..655
FT /note="ATP-dependent DNA helicase II subunit 1"
FT /id="PRO_0000278339"
FT DOMAIN 284..493
FT /note="Ku"
FT DOMAIN 618..652
FT /note="SAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..21
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 655 AA; 73640 MW; 5A32EBCB1369039D CRC64;
MADEDQYRGD DQIDEEEEEI DESGYKTVKD AVLFAIEVSD SMLTPRPSSD SKKPAEESPT
TAALKCAYHL MQQRIISNPR DMIGVLLYGT QASKFYDEDE NSRGDLSYPH CYLFTDLDVP
SAQEVKNLRA LAQDGDESED VLKASGERVS MANVLFCANQ IFTSKAPNFL SRRLFIVTDN
DDPHGDNKSL RSAATVRAKD LYDLGVTIEL FPISRPDHEF DTARFYDDII YKASPSDPDA
PAYLQTDSKA SPATGDGISL LSTLLSSINS RSVPRRAQFS NIPLELGPNF KISVSGYLLF
KRQAPARNSF IWLGGEQPQI VKGVTTQIAD DTARTIEKWE IKKAYKFGGD QVAFTPEEMK
SLRNFGDPVI RIIGFKPLSA LPFWANIKHP SFIYPSEEDF VGSTRVFSAL HQTLLRDKKA
ALVWFIARKN ASPVLGAMVA GEEKLDESGV QKFPPGMWII PLPFADDVRQ NPETTLHVAP
EPLIDQMRYI VQQLQLPKAS YDPFKYPNPS LQWHYRILQA LALDEDLPEK PEDKTLPRYR
QIDKRTGDYV LSWADELEKQ YAKISAHGPK STLVERSAKD RTSEVEDAAP KPYKKVKVET
DEQGVEDVVR APYQKGSLSK LTVPVLKNFL KAHGRSAAGK KKELVERVEE YLEQK
