KU70_CHAGB
ID KU70_CHAGB Reviewed; 622 AA.
AC Q2H0I3;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 90.
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=CHGG_04713;
OS Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 /
OS NRRL 1970) (Soil fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Chaetomium.
OX NCBI_TaxID=306901;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970;
RX PubMed=25720678; DOI=10.1128/genomea.00021-15;
RA Cuomo C.A., Untereiner W.A., Ma L.-J., Grabherr M., Birren B.W.;
RT "Draft genome sequence of the cellulolytic fungus Chaetomium globosum.";
RL Genome Announc. 3:E0002115-E0002115(2015).
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}.
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DR EMBL; CH408032; EAQ88094.1; -; Genomic_DNA.
DR RefSeq; XP_001223927.1; XM_001223926.1.
DR AlphaFoldDB; Q2H0I3; -.
DR SMR; Q2H0I3; -.
DR STRING; 38033.XP_001223927.1; -.
DR EnsemblFungi; EAQ88094; EAQ88094; CHGG_04713.
DR GeneID; 4392952; -.
DR eggNOG; KOG2327; Eukaryota.
DR HOGENOM; CLU_014815_3_0_1; -.
DR InParanoid; Q2H0I3; -.
DR OMA; PNDMMGI; -.
DR OrthoDB; 402798at2759; -.
DR Proteomes; UP000001056; Unassembled WGS sequence.
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 Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.40.50.410; -; 1.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
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; 2.
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 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..622
FT /note="ATP-dependent DNA helicase II subunit 1"
FT /id="PRO_0000278340"
FT DOMAIN 276..463
FT /note="Ku"
FT DOMAIN 584..618
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 537..572
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..558
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 622 AA; 68878 MW; 853F383DE2ED3482 CRC64;
MAWGGDDDRR PDADEGEEEL DETDYKTQKD AVLFAIDVSS SMLQQPPATD KKRADKDSAI
AAALKCAYQF MQQRIIAQPK DMMGILLFGT EKSRFRDEVG GRSSGYPHCY LFTDLDVPAA
EDVKSLKALV EEGEDPDEVL VPAKEPASMA NVLFCANQVF TTNAANFGSR RLFIITDNDA
PHGKDKAAKS AAAVRAKDLY DLGVVIELFP VSHEGKAFDV SKFYDDIIYR DPATEAISDE
VKTSKSGDGL SLLNSLISNI NSKQTPKRAY FSNLHFELAP NVTISVKGYM PLHRQQPART
CYVWLGGEQA QLAQSETIKV DSATRTVDKS EVKKAYKFGG EYIHFKPEEA ASLKNLGGKV
LRVIGFKPRS LLPTWASVKK SIFIFPSEEH FVGSTPRENA NPIMVAIIPS RAMDDETSET
PYLPAGLWLY PLPFADDVRN VDLAAPPRPA DELTDKMREI VQNLQLPKAM YNPLKYPNPS
LQWHYKVLQA MALDEDVPEA LDDATIPKYR QIDKRVGGYL AEWKEALTEK AGGLMKSRAM
KREAEDEDVS RPLAKRTKPA APKEAAGGHM SNAQLKAALE QDTLKKMTVA ELKDVLASKG
VSAVGKKAEL VDKLEQWIEE NV
