KU80_ASPOR
ID KU80_ASPOR Reviewed; 725 AA.
AC Q2MHH2;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=ATP-dependent DNA helicase II subunit 2;
DE EC=3.6.4.12;
DE AltName: Full=ATP-dependent DNA helicase II subunit Ku80;
GN Name=ku80;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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.
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 ku80 family. {ECO:0000305}.
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; AB214651; BAE78503.1; -; Genomic_DNA.
DR EMBL; AP007159; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; Q2MHH2; -.
DR SMR; Q2MHH2; -.
DR STRING; 510516.Q2MHH2; -.
DR OMA; WAMQYVW; -.
DR Proteomes; UP000006564; Chromosome 3.
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 CDD; cd00873; KU80; 1.
DR Gene3D; 1.25.40.240; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 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; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF08785; Ku_PK_bind; 1.
DR PIRSF; PIRSF016570; Ku80; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF100939; SSF100939; 1.
DR SUPFAM; SSF101420; SSF101420; 1.
DR SUPFAM; SSF53300; SSF53300; 1.
PE 3: Inferred from homology;
KW ATP-binding; Chromosome; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Helicase; Hydrolase; Nucleotide-binding; Nucleus;
KW Reference proteome; Telomere.
FT CHAIN 1..725
FT /note="ATP-dependent DNA helicase II subunit 2"
FT /id="PRO_0000278349"
FT DOMAIN 229..481
FT /note="Ku"
FT REGION 259..298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 704..725
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 707..725
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 81742 MW; F4662B9A4F6383A4 CRC64;
MADKEATVYI VDVGRSMGEC RNGRSVTDLE WAMQYVWDRI TGTVATGRKT AMMGVIGLRT
DETSNELEDD VHFSHIAVLS NLKQFLMPDI RKLEDELKPS KTDKGDAISA IILAIQMIIT
HCKKLKYRRK IVLVTNGQGR MSDEDLGEIV KKVKEDNIEL VVMGIDFDDP EYGYKEEDKD
PHKAENETLL RTLVEDCDGV YGTFEQAVAE LDIPRVKSVR SVASFKGYLQ LGNPEEYDSA
LRIPVERYYR TYPAKPPTAS SFVLRSEPEA GQEEAESSEA AAATQKGSQS GDAGLTTVRT
MRTYQVEDKS APGGKIDIER DELAKGYEYG RTAVHISETD ENITILDTFA GLELMGFIQT
DQYQRYMHMS NTNIIIAQRA NDKAALALSS FIHALFELEC YAVARLVVKE NKPPVIVLLA
PSIEPEYECL LEVQLPFAED VRTYRFPPLD KVITVSGKVV TQHRNLPSDD LLDVMGKYVN
SMELVDADED GDPVETFPID DSYSPVLHRI DAAIRARAIH PDQPIPPPSE RLTKFSHPRE
DLIEKSQKHL EKLIEIADVK KVPPKAKGRK RTRETEKPLS GLDVDALLHH EKRVKISPNN
AIPEFKQTLA QAENIEAIKD ATKQMMVIVE DQIKHSLGNA NYDRVIEALG TMRDELVSYE
EPASYNDFLG QLKDKLLQEK LGGDRQELWW LVRRNKLGLV TQRESDQSRV TDTEAKEVSL
TKMKE
