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Database: UniProt
Entry: A0A397I420_9EURO
LinkDB: A0A397I420_9EURO
Original site: A0A397I420_9EURO 
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
//
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