ID A0A238FDF0_9BASI Unreviewed; 740 AA.
AC A0A238FDF0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 03-MAY-2023, entry version 19.
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=BQ2448_1298 {ECO:0000313|EMBL:SCV69904.1};
OS Microbotryum intermedium.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Microbotryomycetes; Microbotryales; Microbotryaceae; Microbotryum.
OX NCBI_TaxID=269621 {ECO:0000313|EMBL:SCV69904.1, ECO:0000313|Proteomes:UP000198372};
RN [1] {ECO:0000313|Proteomes:UP000198372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jeantristanb JTB J.-T., Ricardo R.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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; FMSP01000005; SCV69904.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238FDF0; -.
DR STRING; 269621.A0A238FDF0; -.
DR OrthoDB; 21093at2759; -.
DR Proteomes; UP000198372; 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 Gene3D; 1.10.1600.10; -; 1.
DR Gene3D; 2.40.290.10; -; 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; IPR047087; KU70_core_dom.
DR InterPro; IPR005160; Ku_C.
DR InterPro; IPR005161; Ku_N.
DR InterPro; IPR003034; SAP_dom.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR036465; vWFA_dom_sf.
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 PIRSF; PIRSF003033; Ku70; 1.
DR SMART; SM00559; Ku78; 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:UP000198372};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 667..701
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 43..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 43..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..734
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 740 AA; 83286 MW; AC5B5D703CE3334D CRC64;
MVNMAYGWND GHVSEEEDDD VQEEIYHSSD ATLFLIEATP SMLEPFTPSS TDQPPPSTQT
REKLGWKDKP DATTKLQACL RSAYAMMRRK AQSAPRDRIG IMIFNTAKTE GVKGGSNAKK
HCQIVQDLAL VTAESLVKFK DLLADIEDDP GLLSQMYEVN RGVNALTEAI QGCTDLFRRN
ASSPRINKKI ILITDNDEPY PPRSKLRNAA NERRNAMALQ DLADMDYKIE PFFFSPPNHE
FDLENFYGKF ITMAREDNNN DDEDDELADY SDIPIPWPLV HHDIVQTLSE MVDNLRTKEA
MKRVQFQIPF TLAEGTTIGI KGHALVGVER LRLPTKVDLN TSHADAVLHK IFYKDAITGD
HLDVKTEIRK YFEIGKVDVD KGSRSAQIFF TEAEIRKVKV RPRRALLLPV TDKVTNPLMT
PQTLGRSPSM SLLGFVSRTD FLKYEETIKH SYFIRPDEDA FTGSMRTFVA LMESMIRKGV
IAYASFLSRI SGRPQIVILD AQEEVLNQKT GVVERPAGIN IYQLPFADDL RKHRLDKTPS
IKKPYVEGED EPEQPEIALA TAIVKKLTRV YDPNSYPNPA INFFQETLAA TALDDELPDP
IDKTIPAYGT IRDRAGDKIT QLKSLIKEDE LDPSLVRTSN KKRAHTPEPV GSVEDVQEFA
DKMTRLQNKI TVADLKEGLR LMGEPTGGTK QPLWDRAIAA LAKKGLWAEG DGEGDNASEA
LQKAKKKKRM TIEDDNDDDE
//
