ID A0A061HA24_9BASI Unreviewed; 678 AA.
AC A0A061HA24;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 03-MAY-2023, entry version 41.
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=PFL1_03074 {ECO:0000313|EMBL:EPQ29319.1};
OS Pseudozyma flocculosa PF-1.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Pseudozyma.
OX NCBI_TaxID=1277687 {ECO:0000313|EMBL:EPQ29319.1, ECO:0000313|Proteomes:UP000053664};
RN [1] {ECO:0000313|EMBL:EPQ29319.1, ECO:0000313|Proteomes:UP000053664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PF-1 {ECO:0000313|EMBL:EPQ29319.1,
RC ECO:0000313|Proteomes:UP000053664};
RX PubMed=23800965; DOI=10.1105/tpc.113.113969;
RA Lefebvre F., Joly D.L., Labbe C., Teichmann B., Linning R., Belzile F.,
RA Bakkeren G., Belanger R.R.;
RT "The transition from a phytopathogenic smut ancestor to an anamorphic
RT biocontrol agent deciphered by comparative whole-genome analysis.";
RL Plant Cell 25:1946-1959(2013).
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; KE361631; EPQ29319.1; -; Genomic_DNA.
DR RefSeq; XP_007878781.1; XM_007880590.1.
DR AlphaFoldDB; A0A061HA24; -.
DR GeneID; 19317185; -.
DR KEGG; pfp:PFL1_03074; -.
DR eggNOG; KOG2327; Eukaryota.
DR HOGENOM; CLU_014815_3_0_1; -.
DR OrthoDB; 21093at2759; -.
DR Proteomes; UP000053664; 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; 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 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:UP000053664};
KW Telomere {ECO:0000256|ARBA:ARBA00022895}.
FT DOMAIN 639..673
FT /note="SAP"
FT /evidence="ECO:0000259|PROSITE:PS50800"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 678 AA; 76347 MW; C631D60BD64AD82D CRC64;
MPPKAKFVNK REAERDDSED ELEELDLNAT YQKDMVLFCI DAGPSMHQIN PSSGTSNLYV
ALRAAASLME KKLISSPHDH VGVMVFNTSD TVFKSAQPGE YYRGSHELLT VRQVNVPDTF
NIKSLLKQAE ADPDHLRNAF PPAEKQMRID WALANAGVGI VAAANAGSKR VFYITDNDDP
HPFATDPKST RARKSSLEKM AEFRKLGIRI ETFFIGTEES PFQVNKFYAD IFEQYDDDDD
DDAEGGLQAP KVPKGFHAST EDLKGQEVRR HLWDSAIRFN ELESDVSTRE TPKRVVFSIR
FELGTIGSGI TTENGIMRSN VWQIGIKGYS LISKTTKGNP VKVLVDEECG ELKEVVTHQH
YIDPTTEKTL TKEQIVPAFQ FGKTASLRGQ VRFQGDELKR IKSLGMLPSL KLLGFKDRSE
LKFQDNVKHA YFIYPSDIEY RGSKKVFAGL LDSMVRKDKI GLGLFMPRQN VTPVFVAILP
QAEEVVKGQQ VAAPGMHLIT LPFADDVREV PDAVFNNPPA EAELHQVDAA KAVIERFHKS
KPFNPDHYPN PALNHHYAVL KATAFQEPLP ETMDDHTLPQ YDMIRKRTAH LISAFHDEID
KDDRVRHASD TATATSSGTR ERTFENDKEI LKMYKAGKLS SYTVVDLKGV CDFYRLDKKG
KKADLVDRIS AHIEKMRK
//
