ID A0A397I420_9EURO Unreviewed; 722 AA.
AC A0A397I420;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 22-FEB-2023, entry version 14.
DE RecName: Full=ATP-dependent DNA helicase II subunit 2 {ECO:0000256|ARBA:ARBA00021792, ECO:0000256|PIRNR:PIRNR016570};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551, ECO:0000256|PIRNR:PIRNR016570};
GN Name=KU80 {ECO:0000313|EMBL:RHZ68144.1};
GN ORFNames=CDV56_109013 {ECO:0000313|EMBL:RHZ68144.1};
OS Aspergillus thermomutatus.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=41047 {ECO:0000313|EMBL:RHZ68144.1, ECO:0000313|Proteomes:UP000215305};
RN [1] {ECO:0000313|EMBL:RHZ68144.1, ECO:0000313|Proteomes:UP000215305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMR AF 39 {ECO:0000313|EMBL:RHZ68144.1,
RC ECO:0000313|Proteomes:UP000215305};
RA Parent-Michaud M., Dufresne P.J., Fournier E., Martineau C., Moreira S.,
RA Perkins V., De Repentigny L., Dufresne S.F.;
RT "Draft genome sequence of azole-resistant Aspergillus thermomutatus
RT (Neosartorya pseudofischeri) strain HMR AF 39, isolated from a human nasal
RT aspirate.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00024890}.
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 Evidence={ECO:0000256|ARBA:ARBA00001665,
CC ECO:0000256|PIRNR:PIRNR016570};
CC -!- SUBUNIT: Heterodimer of Ku70 and Ku80. {ECO:0000256|ARBA:ARBA00011584}.
CC -!- SUBCELLULAR LOCATION: Chromosome, telomere
CC {ECO:0000256|ARBA:ARBA00004574}. Nucleus
CC {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR016570}.
CC -!- SIMILARITY: Belongs to the ku80 family. {ECO:0000256|ARBA:ARBA00007726,
CC ECO:0000256|PIRNR:PIRNR016570}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RHZ68144.1}.
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DR EMBL; NKHU02000003; RHZ68144.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A397I420; -.
DR STRING; 41047.A0A397I420; -.
DR VEuPathDB; FungiDB:CDV56_109013; -.
DR OrthoDB; 5884at2759; -.
DR Proteomes; UP000215305; 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-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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 CDD; cd00873; KU80; 1.
DR Gene3D; 1.10.1600.10; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 1.25.40.240; Ku, C-terminal domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 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 PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1.
DR PANTHER; PTHR12604:SF4; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 5; 1.
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; SSF101420; C-terminal domain of Ku80; 1.
DR SUPFAM; SSF100939; SPOC domain-like; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PIRNR:PIRNR016570};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|PIRNR:PIRNR016570};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|PIRNR:PIRNR016570};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|PIRNR:PIRNR016570};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR016570};
KW Helicase {ECO:0000256|ARBA:ARBA00022806, ECO:0000256|PIRNR:PIRNR016570};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PIRNR:PIRNR016570};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR016570};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR016570};
KW Reference proteome {ECO:0000313|Proteomes:UP000215305};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 6..164
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 265..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 519..539
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 265..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 722 AA; 81225 MW; 641EA4F0DDE3424E CRC64;
MAEKEATVYI VDVGRSMGEK RNGRSVTDLE WAMQYVWDRI TATVATGRKT ATIGVIGLKT
DGTSNELDDD PHFKHISVLS GIQQFLMPDI RRLAAVIKPS KTDKGDAISA IILAIQMIVT
YCKKLKYKRK IVLVTNGLGW MSNEDLDQIT KKIKEDNIEL VVLGTDFDDP DYGFKEEEKD
PQKAENEALL RGLVEDCDGA YGTLEQAVSE MDIPRVKKVR TVATFKGYLQ LGNPEEYDTA
LRIPVERYYR TYVAKPPSAS SFVLRSDVGA EQEQGESTGL AAPSQETPPE GGALTSVRNL
RTYEVPDENA PGGKIDVERE ELAKGYEYGR TAVHISETDE NITTLETYAV LELVGFIQSD
KYDRYMHMST TNIIIGQRGN DKATLALSSF IHALFELECY AVARLVVKEN KPPVMVLLAP
SIEPDYECLH EVQLPFAEDV RTYRFPPLDK VITVSGKVVT EHRNLPNKDL LDAMSEYVDS
MELVDIDEDG NPVEGLPIDD SFSPVLHRID SAIRYRAIHP NDPVPPPSEN LTRLSQPPPD
LVEKSKRYLE KLMAAADVKK VPPKVKGRKR VRESEKPLSG LDVDALLHQE KRARISPTNA
IPEFKQTLTQ AETIETIKDA VKQMTSIIED QIRNSLGDAN YDRVNEEMGV MRDELISFEE
PALYNDFLRQ LKDKLLKEEL GGDRQELWWL LRRSKLGLIS QRESDQSDVT EEQAKEFLSA
QS
//