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KU70_PHANO
ID   KU70_PHANO              Reviewed;         652 AA.
AC   Q0U5F2;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 92.
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; ORFNames=SNOG_13012;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(2007).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT79812.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; CH445348; EAT79812.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; XP_001803226.1; XM_001803174.1.
DR   AlphaFoldDB; Q0U5F2; -.
DR   SMR; Q0U5F2; -.
DR   STRING; 13684.SNOT_13012; -.
DR   PRIDE; Q0U5F2; -.
DR   GeneID; 5980138; -.
DR   KEGG; pno:SNOG_13012; -.
DR   eggNOG; KOG2327; Eukaryota.
DR   InParanoid; Q0U5F2; -.
DR   OMA; PNDMMGI; -.
DR   OrthoDB; 402798at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0000781; C:chromosome, telomeric region; IEA:UniProtKB-SubCell.
DR   GO; GO:0043564; C:Ku70:Ku80 complex; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0071480; P:cellular response to gamma radiation; IBA:GO_Central.
DR   GO; GO:0071481; P:cellular response to X-ray; IBA:GO_Central.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IBA:GO_Central.
DR   GO; GO:0000723; P:telomere maintenance; IBA:GO_Central.
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;
KW   Reference proteome; Telomere.
FT   CHAIN           1..652
FT                   /note="ATP-dependent DNA helicase II subunit 1"
FT                   /id="PRO_0000278346"
FT   DOMAIN          274..486
FT                   /note="Ku"
FT   DOMAIN          613..647
FT                   /note="SAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00186"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          38..59
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          565..612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        43..58
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..594
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   652 AA;  72705 MW;  B4062F9323EB5179 CRC64;
     MADTQDNRPG EEEDDDEEID ESAYKTMKDA VLFAIDVSPS MLERPPKTED KKADRDSPTS
     AALKCAYQLM QQRIISNPND MMGILLFGTE KTDLKDGDST FQHCYLLADL DVPSAQDVKR
     LRDLVEDEEE AEQILKPAKD GASIATVLFC ANQIFTTKAP NFSSRRLFLV TDNDYPVNVK
     ADKDTAVTRA RDLYDLGCTI DLFPISQPDQ TFDRSRFYDD LVYPTSPSDP DAPIAVATTT
     KVAKSGEGIT LLKQLISSIN SKATPRRALF SLPLELGPDL RIGVKGYILI KRQEHAKSCY
     VWVGGDKPQI VSSSTSHMAD DTARVVEKTE LRKAYKFGGD AITFTPDEII KIRQAFGDPI
     IRIIGFKPIS CLPIWTNTNK ATFIYPSEAD FIGSTRVFSA LQQKLLKSKK MGLVWFIARR
     NAAPILSALI PAEEQTNEDG EQAMPPGLWL VPLPWADDIR QFPSPAADVL KTTDALTDKM
     RIIIEQLQLP KGVYDPAKYP NPDLQWFYRI LQAMALEEEL PEKPDDKTMP KFRQIDKRCG
     EYITEYGAEF EAAFAQLAVS TFPHRGKRAS ADPGDDKPAP KRVKKEPKVK EEGEDDEGLT
     DEQMATVNNK GQISKQTVAV LKAWLSQRGE STSGKKADLV ERVQGYLEGK GL
 
 
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