ID A0A395HK49_ASPHC Unreviewed; 654 AA.
AC A0A395HK49;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=ATP-dependent DNA helicase II subunit 1 {ECO:0000256|ARBA:ARBA00021796};
DE EC=3.6.4.12 {ECO:0000256|ARBA:ARBA00012551};
DE AltName: Full=ATP-dependent DNA helicase II subunit Ku70 {ECO:0000256|ARBA:ARBA00031811};
GN ORFNames=BO97DRAFT_473316 {ECO:0000313|EMBL:RAL07986.1};
OS Aspergillus homomorphus (strain CBS 101889).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450537 {ECO:0000313|EMBL:RAL07986.1, ECO:0000313|Proteomes:UP000248961};
RN [1] {ECO:0000313|EMBL:RAL07986.1, ECO:0000313|Proteomes:UP000248961}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101889 {ECO:0000313|EMBL:RAL07986.1,
RC ECO:0000313|Proteomes:UP000248961};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (FEB-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 -!- 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}.
CC -!- SIMILARITY: Belongs to the ku70 family.
CC {ECO:0000256|ARBA:ARBA00005240}.
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DR EMBL; KZ824321; RAL07986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395HK49; -.
DR STRING; 1450537.A0A395HK49; -.
DR VEuPathDB; FungiDB:BO97DRAFT_473316; -.
DR OrthoDB; 21093at2759; -.
DR Proteomes; UP000248961; 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:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase 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; cd00788; KU70; 1.
DR CDD; cd01458; vWA_ku; 1.
DR Gene3D; 1.10.1600.10; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 4.10.970.10; Ku70, bridge and pillars; 1.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR006165; Ku70.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR027388; Ku70_bridge/pillars_dom_sf.
DR InterPro; IPR047087; KU70_core_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 NCBIfam; TIGR00578; ku70; 1.
DR PANTHER; PTHR12604; KU AUTOANTIGEN DNA HELICASE; 1.
DR PANTHER; PTHR12604:SF2; X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 6; 1.
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; SSF68906; SAP domain; 1.
DR SUPFAM; SSF100939; SPOC domain-like; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50800; SAP; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Helicase {ECO:0000256|ARBA:ARBA00022806};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000248961};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 618..652
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..603
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 26
FT /note="Schiff-base intermediate with DNA; for 5'-
FT deoxyribose-5-phosphate lyase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003033-1"
SQ SEQUENCE 654 AA; 73809 MW; C5480E37889A5D7E CRC64;
MADSNPPRDD EVGEEEEEEI DETNYKTVKD AVLFAIEVSD SMLKPRPSSD PKKPVEESPA
TAALKCAYHL MQQRIISNPQ DMMGVLLYGT QASKFYDEDE GSRGDLSYPN CYLFTDLDIP
SAQEVKDLRA LVEDEGKARE ILVPAEKPVS MANVLFCANQ IFTSKAPNFL SRRLFIVTDN
DNPHSEDKAL RSAATVRAKD LYDLGVTIEL FPISQPDREF DSSKFYDDII YKTSPNDPEA
PAYLQLDSKA STATGDGISL LNTLLSSVNS RSVPRRTHFS NMPLEFGPNL KISVSGYILF
RKQAPARNCY VWLGGEKPEI VKGTTTQIAD DTARTVEKWE IRKAYKFGGD QVLFTPEEQK
ELKNFGDPVI RIIGFKPASA LPFWANMKHP YFIYPSEEDY VGSTRVFSAL HQTLLRQKKL
ALVWFIPRRA ANPVLGAMIA GEEKVDENGV QKYPPGMWIL PLPYADDVRQ NPETTLNVAP
EPLIDQMRVI IQQLQLPKAC YEPSKYPNPS LQWHYRILQA LALDEDLPEK PEDKTVPKYR
QIDKRAGDYV LSWADELEKQ YAKVAVEKPA HSTVVKRGAR DKGPDNDEES SKPAKRVKVE
ADNNLEDEVR RHYQKGNLSR LTVNILKDFL TSHGRSGVGK KADLIDRVVQ FLES
//
