KU80_EMENI
ID KU80_EMENI Reviewed; 725 AA.
AC Q5B4H8; C8V875;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 100.
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=AN4552;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
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DR EMBL; AACD01000078; EAA60895.1; -; Genomic_DNA.
DR EMBL; BN001303; CBF77271.1; -; Genomic_DNA.
DR RefSeq; XP_662156.1; XM_657064.1.
DR AlphaFoldDB; Q5B4H8; -.
DR SMR; Q5B4H8; -.
DR STRING; 162425.CADANIAP00005886; -.
DR EnsemblFungi; CBF77271; CBF77271; ANIA_04552.
DR EnsemblFungi; EAA60895; EAA60895; AN4552.2.
DR GeneID; 2872348; -.
DR KEGG; ani:AN4552.2; -.
DR eggNOG; KOG2326; Eukaryota.
DR HOGENOM; CLU_010975_1_1_1; -.
DR InParanoid; Q5B4H8; -.
DR OMA; WAMQYVW; -.
DR OrthoDB; 598957at2759; -.
DR Proteomes; UP000000560; Chromosome III.
DR Proteomes; UP000005890; 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; 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_0000278353"
FT DOMAIN 235..484
FT /note="Ku"
FT REGION 277..299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 567..586
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 725 AA; 81561 MW; 96F4325158C4464B CRC64;
MADKEATVYI VDVGKSMGER RNGRDLTDLE WAMKYVWDCI TNTVATGRKT AMLGVIGLKT
DGTDNELGDE SHFSHISVLS EIKQFLMSDI RELGERIKPS SVDKGDAISA LILAIQMIIT
HCKKLKWKRK IVLITNGLGR MNSENLDDIV SKVKEDNIEL IILDLTGRRG PDFDDAEYGI
KEEDKDPHKA SNETLLRTIT ERCDGVFGTL EQAVEETEIP RVKPVRPVAS FKGFLQLGNP
EEYDTAVRIP VERYPRTMVA KPPTASQFVL RSDLAAGQEG PVSSTAVPET QPEDGSNLTN
VRNLRTYQVS DESAPGGKID VERDDLAKGY EYGRTAVHIS ETDENITRLE TTAAMELVGF
IQSERYDRYM HLSNTHIIIA NRANDKASLA LSSFIHALFE LESYAVARLV TKENKPPTLV
LLAPSIEPDY ECLLEVQLPF AEDVRTYRFP PLDHVVTVSG KVVTQHRNLP NDDLLDAMDK
YVDSMELKGT DEDGDLVNTP FPIDDSFSPV LHRVNAAIRS RAIHPNDPIP PPARILTQFS
QPPEHLLKNA ERHLKRLIEV ADVKKVPPKA KGRKRAREPE KPLSGLDVDS LLHQEKRVRI
SPNNAIPEFK QTLAQAENIE TMKDAVKQMR SILEDQIRHS LGDANYDRVT EGLGVVREEL
IAYEEPGLYN DLIRKLKEAL LKEKLGGDQR ELWWLLKRSK LGLIEQRESE LSEVTEEEAK
KFMSA
