KU80_PHANO
ID KU80_PHANO Reviewed; 715 AA.
AC Q0U8L4;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 25-MAY-2022, entry version 92.
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; ORFNames=SNOG_11900;
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 ku80 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAT80944.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; CH445344; EAT80944.2; ALT_SEQ; Genomic_DNA.
DR RefSeq; XP_001802136.1; XM_001802084.1.
DR AlphaFoldDB; Q0U8L4; -.
DR STRING; 13684.SNOT_11900; -.
DR PRIDE; Q0U8L4; -.
DR GeneID; 5979044; -.
DR KEGG; pno:SNOG_11900; -.
DR eggNOG; KOG2326; Eukaryota.
DR InParanoid; Q0U8L4; -.
DR OMA; WAMQYVW; -.
DR OrthoDB; 598957at2759; -.
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 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; 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; PF08785; Ku_PK_bind; 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..715
FT /note="ATP-dependent DNA helicase II subunit 2"
FT /id="PRO_0000278355"
FT DOMAIN 217..468
FT /note="Ku"
FT REGION 254..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 264..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 715 AA; 79398 MW; 8631A7276309A1CD CRC64;
MAAIRLISIG LWSMFGIRLP TQVATGRKSA LMSVIGCRTD ETDLGGVMEE AEGYENLRVF
SELKQFLLGD IRTLQDQLRP SKTNDGDLLS ALALAVQMID GATQGKGGKP LKYDRRIIIV
TDGRGSIDTD DLEQIAAKIR DPEAPVDLVL LGVDFDDPDN GFKEEDKSSQ KAKNEVSLKG
FVEDCNGVFG TLAEAIDQLQ IPRLKETRPV PSFKGQLTLG DPGHYDATLT IDVERYPCTM
LAKPPTASSF ATRTDFGAGS AAGPSDESSH TMTGEEQPMT DLSAVRNQRV YQVDNEEEPG
MKKNVEMDEL ERGYEYGRTA VHISESDMNV VKLETTPMLS LIGFVKAEAF ERYLPLSRSN
FLVPQRGNQA AQLSLSSFIH ALYEADCYAV ARLVTKELKP PVIVLLVPRI EVEWEALVDV
ELPFEEDMRR YKFPPLDRKL TISGKVITEH KDLPTDELTD AMSKYVDAMD LSTFGRDEDG
NPAEYAKPED TFSPIVHRIG HIIRWRATHP DPSLPMPPPS DILTKYANPP ADLLDASTSQ
FEALKKAARV SKVPPKVKGR GKRNRAERDK PISGLDIDAL LGNPNRVKID PSNLVPSFKN
ALAASDDLET IKEAAQSMST EIRSLIRSSV GDSGYGRALE ALRVMRDELT ELEEPEIWNE
FIRGLKSDLL EGKLNGNRKD MWWKIRGNRY GLVDRKRSFV SDVTEEEASA FYNVA
