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KU80_NEUCR
ID   KU80_NEUCR              Reviewed;         725 AA.
AC   Q7RX73;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 2.
DT   25-MAY-2022, entry version 111.
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;
DE   AltName: Full=Protein mus-52;
GN   Name=mus-52; Synonyms=ku80; ORFNames=NCU00077;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=15299145; DOI=10.1073/pnas.0402780101;
RA   Ninomiya Y., Suzuki K., Ishii C., Inoue H.;
RT   "Highly efficient gene replacements in Neurospora strains deficient for
RT   nonhomologous end-joining.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:12248-12253(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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 mus-51/ku70 and mus-52/ku80. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, telomere
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD16623.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=EAA27151.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AB177395; BAD16623.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002238; EAA27151.3; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_956387.3; XM_951294.3.
DR   AlphaFoldDB; Q7RX73; -.
DR   SMR; Q7RX73; -.
DR   STRING; 5141.EFNCRP00000000459; -.
DR   EnsemblFungi; EAA27151; EAA27151; NCU00077.
DR   GeneID; 3872525; -.
DR   KEGG; ncr:NCU00077; -.
DR   HOGENOM; CLU_010975_1_1_1; -.
DR   InParanoid; Q7RX73; -.
DR   Proteomes; UP000001805; Chromosome 3, Linkage Group III.
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   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_0000278354"
FT   DOMAIN          232..478
FT                   /note="Ku"
SQ   SEQUENCE   725 AA;  80976 MW;  D182541223DFC8C0 CRC64;
     MADKEATVYV IDLGESMADC HNGRNESDLE FGMRYIWDKI TTTVAASRKT WNVGVVGLNT
     DETNNNENRE EYQGYENISV LQELGPMTMA SLRALKSKIE PSSTSSADAI SAIVVALRMI
     QTFTKKLKYK RKIIVVTNGE SPIDDDQSEE VANMLNDVGI ELIVLGVDFD DAEYGFKEED
     KPRHKEQNEK ILKTLVDHCE SGAFGTMAQA VEELATPRIK SVRPFKAYDG PLTLGDPQKY
     PSALSIQVER YFKTKRATPP SASNVANPNG PPQTQVWNED DGVPFSGVGL QPVKQLRTYR
     IEDSKAAGGK KDVDMEDLAK AYQYGRTVVP FGKSEEDYLK YETTKSFTII GFVPMSSYEP
     FLNMGETGLI VAQKVNEEAE LGLSALIHAL HELESYAVAR YVNKDKAPPQ ILLLKPNPAI
     EDDIECLYDI PLPFAEDVRS YQFPPLDKVL TITGNVLTEH RLLPNNDLQQ AMSDYVDAMD
     LTEYGQDDDG HPAEYAPIDD LYNPVIHHMN QAIRNRAVNP DAPLPPVAEI LTRFTHPPEP
     LLAKAKTEID GLIQAAEVKK VPPKVQGKRG RKDTVKPLSG LDIDALLSET RPRTKKTPII
     STENAIPEFK QILETAEDDE TIEIAAKQMG NIICKLVSDS FADVLYPRAA ENLRVMREEL
     INMEVPTLYN KYITKLKESL LSGNLNGDRR EMWFRWIVGG RLGLITQDES EVSEVSENEA
     KAFLK
 
 
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