ID A0A1I8HKG1_9PLAT Unreviewed; 1326 AA.
AC A0A1I8HKG1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Ku domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0006726-snap-gene-0.7-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0006726-snap-gene-0.7-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0006726-snap-gene-0.7-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the DEF8 family.
CC {ECO:0000256|ARBA:ARBA00029450}.
CC -!- SIMILARITY: Belongs to the ku80 family.
CC {ECO:0000256|ARBA:ARBA00007726}.
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DR WBParaSite; maker-uti_cns_0006726-snap-gene-0.7-mRNA-1; maker-uti_cns_0006726-snap-gene-0.7-mRNA-1; maker-uti_cns_0006726-snap-gene-0.7.
DR Proteomes; UP000095280; Unplaced.
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:0046872; F:metal ion binding; 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; cd00029; C1; 1.
DR CDD; cd00873; KU80; 1.
DR Gene3D; 1.10.1600.10; -; 1.
DR Gene3D; 2.40.290.10; -; 1.
DR Gene3D; 3.30.60.20; -; 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; IPR046349; C1-like_sf.
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; IPR002219; PE/DAG-bd.
DR InterPro; IPR025258; RH_dom.
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 Pfam; PF13901; RH_dom; 1.
DR SMART; SM00109; C1; 1.
DR SMART; SM01175; DUF4206; 1.
DR SMART; SM00559; Ku78; 1.
DR SUPFAM; SSF101420; C-terminal domain of Ku80; 1.
DR SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR SUPFAM; SSF100939; SPOC domain-like; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50234; VWFA; 1.
DR PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 5..222
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT DOMAIN 1061..1115
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT REGION 169..212
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..594
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 733..798
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 878..917
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 776..798
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..904
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1326 AA; 143855 MW; 3ED60828535CC311 CRC64;
LQAESIAIIL DIGPHMRRGP PGYARPIELA LDCLKMLLQR KLFQQSKDEV AVVLAGTEMS
DNPLADDDGN FANISLAREL STIDWDIVQF FNDNIRTSDS ISADIIDGLI VGVDHLVKKT
QGRRGKTNKR AVIVSNLAGE MNTDELERIV RNLKKADVQV LLIGASISEN DDNDDNGDGE
DGAPDHLGGA GAGSGNSDSE RKPKTQRQLD NEAALRPLLE AVDGYSYSFN DAIPALSYFQ
LRSVQQRPWK ANLELGELSL PVCGYTKVKP AKPPSMTTVY AGDASAQVST ARATTLNDEQ
ETEIDEDDVV RGYRYGSTLV PFSEADREAM KQPEDKSLTI VCFTHRQNIL RHHMLGDGVS
LFVGDPSAPP EVHRALSALG EALLLRGGVV IVRRVYSRAS SPRLGVLLPK RKSTASGAEF
IVFEYIELAF REDIRTYTFP PLPLDDDIVR EVPSLAKLQP TQIQLEAAAA FVDAMDAGDD
ARLQMSEKLN PYVQHWYSCV TDRALHPDNP LPQPSAAVMA SLEAPAELRP EARQAEVHDR
LEQLRQACPI VPRQTSKRQE GKTGADVFGD DPLAGAGADN GADGPAKKRA KLETGETSDD
IAAALLRPRV TEVGAVTPLE DFDALIAQGQ TDAAFSGMQR RVVQLVSDSF GDAYFPKAGA
CLRALRATAR TTPGRGAAFN AFLRDWLPSL RRDRPAFLTQ HLATEQGRRA MGFLSKDETA
DSDLTAEQCA ELLASSSGGA DSGAAGKGED GAEEEEDDIP LTAASLDVDA DVDANADANA
DNRRQIEQRQ RDEESPLPEV AADLGDVWSS SPLADAGDST SLSTAAATVT LTTTMTATAA
SMSAGQRNRS LSSSLEAERV NPFNIVGAGL LLGLGHWRQR SDSERRATPP PSSSTPPPPS
QLPPSSLSSS SINSNHHQHQ LLAAADGLVE DHYAPERRRQ PDDYQSRADL QAEISRLQAE
FLAENVAEQA DSEVDDERQE RRRQLYERLI ELKFRLHRLS DSVRLATGKT GAATAGAAAA
AASDIVAADD DSEAREDLTI TPAASSVDEV GRDDEPRVIL SHAFVTSTGK PSGQCDVCAK
ELLKLGFILA GQFSRCCRCG LLAHPACLDR MVRPCIADEL ESGRLKLEWT KLYMFPSLRE
QDYACKGCSR SLTQLSEARL CHYTGLLYCH ACHWGDAVPL PSFILGRLDA TPQPVCRRAL
EVLRFSRTRP AIDLASPLAT VFVSVAGRQL PAARDFDQLR ARLSRLVPLL SACQGFRRLG
LAKLLPEHRL HFLNNHNMYS YQDLLDLVVA GTLRDDLARL LALVDGHIDT CSACNESSQT
LSTASG
//
