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KU80_ASPSO
ID   KU80_ASPSO              Reviewed;         725 AA.
AC   Q2MHH1;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   25-MAY-2022, entry version 66.
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 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 ku80 family. {ECO:0000305}.
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DR   EMBL; AB214652; BAE78504.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2MHH1; -.
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; Telomere.
FT   CHAIN           1..725
FT                   /note="ATP-dependent DNA helicase II subunit 2"
FT                   /id="PRO_0000278350"
FT   DOMAIN          229..481
FT                   /note="Ku"
FT   REGION          259..294
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..294
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;  81784 MW;  0EBFD27AF6A3F512 CRC64;
     MADKEATVYI VDVGRSMGEC RNGRSVTDLE WAMQYVWDRI TGTVATGRKT ATMGVIGLRT
     DETSNELEDD VHFSHIAVLS NIKQFLMPDI RKLEDELKPS KTDKGDAISA IILAIQMIIT
     HCKKLKYRRK IALVTNGQGR MSDEDLGEIV KKVKEDNIEL VVMGIDFDDP EYGYKEEDKD
     PRKAENETLL RTLVEDCDGV YGTFEQAVAE LDIPRVKSVR SVASFKGYLQ LGNPEDYDSA
     LRIPVERYYR TYPAKPPTAS SFVLRSEPEA GQEEAESSEA AAATQKGSQS GDIGLTTVRT
     MRTYQVEDKS APGGKIDIER DDLAKGYEYG RTAVHISETD ENITILDTFA GLELMGFIQT
     DRYQRYMHMS NTNIIIAQRA NDKAALALSS FIHALFELEC YAVARLVVKE NKPPVIVLLA
     PSIEPDYECL LEVQLPFAED VRTYRFPPLD KVITVSGKVV TQHRNLPNDD LLDVMGKYVN
     SMELVDADED GDPVETFPID DSYSPVLHRI DAAIRARAIH PDQPIPPPSE RLTKFSHPRE
     DLIERSQKYL EKLIEIADVK KVPPKAKGRK RTRETEKPLS GLDVDALLHH EKRAKISPNN
     AIPEFKQTLA QAENIEAIKD ATKQMMVIVE DQIKHSLGNA NYDRVIEALG TMRDELVSYE
     EPASYNDFLG QLKDKLLQEK LGGDRQELWW LVRRNKLGLV TQRESDQSRV TDTEAKEVSL
     TKMKE
 
 
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