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Database: UniProt
Entry: A0A078A0N2_STYLE
LinkDB: A0A078A0N2_STYLE
Original site: A0A078A0N2_STYLE 
ID   A0A078A0N2_STYLE        Unreviewed;       734 AA.
AC   A0A078A0N2;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   28-JUN-2023, entry version 35.
DE   SubName: Full=Atp-dependent dna helicase {ECO:0000313|EMBL:CDW74323.1};
GN   Name=Contig3961.g4240 {ECO:0000313|EMBL:CDW74323.1};
GN   ORFNames=STYLEM_3318 {ECO:0000313|EMBL:CDW74323.1};
OS   Stylonychia lemnae (Ciliate).
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Stylonychinae; Stylonychia.
OX   NCBI_TaxID=5949 {ECO:0000313|EMBL:CDW74323.1, ECO:0000313|Proteomes:UP000039865};
RN   [1] {ECO:0000313|EMBL:CDW74323.1, ECO:0000313|Proteomes:UP000039865}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=130c {ECO:0000313|EMBL:CDW74323.1,
RC   ECO:0000313|Proteomes:UP000039865};
RA   Swart Estienne;
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC   -!- SIMILARITY: Belongs to the ku80 family.
CC       {ECO:0000256|ARBA:ARBA00007726}.
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DR   EMBL; CCKQ01003213; CDW74323.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A078A0N2; -.
DR   EnsemblProtists; CDW74323; CDW74323; STYLEM_3318.
DR   InParanoid; A0A078A0N2; -.
DR   OMA; WAMQYVW; -.
DR   OrthoDB; 178937at2759; -.
DR   Proteomes; UP000039865; Unassembled WGS sequence.
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:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 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; 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   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.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
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, ECO:0000313|EMBL:CDW74323.1};
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:UP000039865}.
FT   DOMAIN          294..438
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
FT   REGION          165..196
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          711..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          545..575
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        174..196
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   734 AA;  85228 MW;  874183BF9A3D4CB8 CRC64;
     MNKLFGGDNT KQTRFQVAKE SVKMLIESKL LYATSHEIGI VLIGTQKSSN FLNDQYEDQY
     KHVTTFRQID KLDLESFRHL ENITCEKAPI KDNGGDLLDG LIVGMDMMVR HCGEKKYKKR
     VFLITDGERE TKYDPRELKQ IITTLNERDT RLNIITLDFC NELAEDDEDD DEEESKKDSK
     KKESAADETE SQNKNKEFLM ELTDKVKGAI FPAKVAMEIY KQFKKREVMA RVKYRGNLDL
     AKDLKLNVSI YSRTREEVFP SLKKHSTIAN ESTSAKESLV KLERQFAEVD DPDQQPVDTD
     QQIKAYNYGK QLVPVSKENE HILKYKPPKQ DDEHDPANDM DVKVQNQSKV PRHHFIAGVD
     VILPVKGSKN ERAFAALVFA MIETHRVLIA RIVERKNVDP KLVVLYPHIS KKKPLLYMAQ
     IPTNEEIRDY QFPSLIPATK PQKTAAKQLI KALDLVDQEA EEEKLKPEIT FNPALQYFSQ
     VVVHRITEPA QQELPQLNQQ IAEYVKPDKK LFQQAEDEIS AFEEAFELKY NNEDENKKKK
     RVYWRDIIRK EEEKVANEEQ KLEEEEQIAR QKIGDKDMDD KEDKIKEISS MNPIEDFKNM
     VNDRKVDRVS DAIDQMQKLI IRFVTNSLAG DLYSRALDCL IALRESCINE DEGQKFNQFM
     EKLKQLFSKG TNKEFFQSII KHKISLITKD ESSISSVITA DEAKRFLEID KDDSGQMAQQ
     KKIKQEDEFM DEIE
//
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