KU70_NEUCR
ID KU70_NEUCR Reviewed; 645 AA.
AC Q7SA95;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
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;
DE AltName: Full=Protein mus-51;
GN Name=mus-51; Synonyms=ku70; ORFNames=NCU08290;
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 ku70 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD16622.1; Type=Erroneous gene model prediction; Evidence={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; AB177394; BAD16622.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CM002239; EAA33267.3; -; Genomic_DNA.
DR RefSeq; XP_962503.3; XM_957410.3.
DR AlphaFoldDB; Q7SA95; -.
DR SMR; Q7SA95; -.
DR STRING; 5141.EFNCRP00000008414; -.
DR PRIDE; Q7SA95; -.
DR EnsemblFungi; EAA33267; EAA33267; NCU08290.
DR GeneID; 3878669; -.
DR KEGG; ncr:NCU08290; -.
DR VEuPathDB; FungiDB:NCU08290; -.
DR HOGENOM; CLU_014815_3_0_1; -.
DR InParanoid; Q7SA95; -.
DR Proteomes; UP000001805; Chromosome 4, Linkage Group IV.
DR GO; GO:0099115; C:chromosome, subtelomeric region; IEA:EnsemblFungi.
DR GO; GO:0140445; C:chromosome, telomeric repeat region; IEA:EnsemblFungi.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IEA:EnsemblFungi.
DR GO; GO:0035861; C:site of double-strand break; IEA:EnsemblFungi.
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:0003723; F:RNA binding; IEA:UniProtKB-KW.
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:0032208; P:negative regulation of telomere maintenance via recombination; IEA:EnsemblFungi.
DR GO; GO:0120290; P:stalled replication fork localization to nuclear periphery; IEA:EnsemblFungi.
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; RNA-binding; Telomere.
FT CHAIN 1..645
FT /note="ATP-dependent DNA helicase II subunit 1"
FT /id="PRO_0000278345"
FT DOMAIN 276..486
FT /note="Ku"
FT DOMAIN 607..641
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 565..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 565..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 645 AA; 72353 MW; B9DF6FCA28B4C46D CRC64;
MSWRKDQDER LDGDEGDEEL DENDYKTQKD AVLFAIDVSK SMLKPPQNTG DKKADKDSAL
TAALTCAYQI MQQRIISQPK DMMGVLLFGT EKSKFRDDSG NGTGYPHCYL LSDLDIPGAE
DVKKLKALIE DGDDEDEIMV PSKEPVIMSN MLFCANQVFT TNAANFGSRR LFIVTDNDDP
HAGDKQAKSS AAVRAKDLYD LGVVIELFPI SREDKKFDLS KFYDDIIYRN PAAEAGQSES
PKTSKSGDGL TLLNSLISNI NSKQTPKRSY FSNLPFELAP GLTISIKGYM PLNRQTPTRS
CYVYEGEEQA QVVQSETAQV DFAARTVEKS ELRKGYKFGG EHICFKPEEL AELKQMGKKT
LRIIGFKKRS KIPSWASVKK SIFIFPSEEQ YVGSTRVFSA LWQKLLKDDK VGIAWFVARE
NAHPVMVAIF PSGNPDDEEA NTPYLPAGLW LYPLPFADDV RSVDHVTAPP RPADELTDQM
RQVIQNLQLP KAMYDPRKYP NPSLQWHYKI LQAKALDEET PDAMDDVTLP KYRQIDKRVG
GYLAEWKEML AKKANDLQNT RAFKREFEED DERPAKRAKP SKKAASGGGG PANSNADLKK
AFEQGTLGKM TVAELKDIMA SKGISTAGRK AELVERLEQW VEENL
