ID A0A0V1I7R1_9BILA Unreviewed; 1671 AA.
AC A0A0V1I7R1;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=CLIP-associating protein 1-A {ECO:0000313|EMBL:KRZ18881.1};
GN Name=XRCC6 {ECO:0000313|EMBL:KRZ18881.1};
GN ORFNames=T11_6100 {ECO:0000313|EMBL:KRZ18881.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ18881.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ18881.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ18881.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ku70 family.
CC {ECO:0000256|ARBA:ARBA00005240}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ18881.1}.
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DR EMBL; JYDP01000002; KRZ18881.1; -; Genomic_DNA.
DR STRING; 268475.A0A0V1I7R1; -.
DR Proteomes; UP000055024; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0043564; C:Ku70:Ku80 complex; IEA:InterPro.
DR GO; GO:0005819; C:spindle; IEA:UniProt.
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:0015631; F:tubulin 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:0000226; P:microtubule cytoskeleton organization; IEA:UniProt.
DR GO; GO:0000278; P:mitotic cell cycle; IEA:UniProt.
DR GO; GO:0031110; P:regulation of microtubule polymerization or depolymerization; IEA:UniProt.
DR GO; GO:1902903; P:regulation of supramolecular fiber organization; IEA:UniProt.
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; 1.25.10.10; Leucine-rich Repeat Variant; 4.
DR Gene3D; 1.10.720.30; SAP domain; 1.
DR Gene3D; 3.40.50.410; von Willebrand factor, type A domain; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR024395; CLASP_N_dom.
DR InterPro; IPR021133; HEAT_type_2.
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; IPR036361; SAP_dom_sf.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
DR InterPro; IPR034085; TOG.
DR InterPro; IPR002035; VWF_A.
DR InterPro; IPR036465; vWFA_dom_sf.
DR InterPro; IPR048491; XMAP215_CLASP_TOG.
DR NCBIfam; TIGR00578; ku70; 1.
DR PANTHER; PTHR21567; CLASP; 1.
DR PANTHER; PTHR21567:SF9; CLIP-ASSOCIATING PROTEIN; 1.
DR Pfam; PF12348; CLASP_N; 1.
DR Pfam; PF02735; Ku; 1.
DR Pfam; PF03730; Ku_C; 1.
DR Pfam; PF03731; Ku_N; 1.
DR Pfam; PF21041; XMAP215_CLASP_TOG; 1.
DR SMART; SM00559; Ku78; 1.
DR SMART; SM01349; TOG; 3.
DR SUPFAM; SSF48371; ARM repeat; 1.
DR SUPFAM; SSF100939; SPOC domain-like; 1.
DR SUPFAM; SSF53300; vWA-like; 1.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
DR PROSITE; PS50234; VWFA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
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:UP000055024};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT REPEAT 162..199
FT /note="HEAT"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00103"
FT DOMAIN 1121..1321
FT /note="VWFA"
FT /evidence="ECO:0000259|PROSITE:PS50234"
FT REGION 635..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 635..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1671 AA; 186870 MW; 31FC5F023C7CBD6E CRC64;
MGNFSELLNK NSTDPKTRVE LGQQLLDLIQ REGVPNDANN LTLFMDVMVQ WLNGTNFKVA
LLALEILSLS LEVSGATISH IVLDNASTIM ERLGDNREQV RQDAVGLLLK LMNTPGCTPQ
GVLDRVVEGL SHKQWLVRIG VMIVLQQILR SYGPSCLQLG RLVPSICRLL ADPMNQVRDV
ATETLVEMYV FLGDKLAMDI QRKQLVPNAR AAALFSRFED VKRNGLVGNS CSNGTVGSAL
ESVTDFTDAT PTAHRQISSV STTLKKPLLT AVKQSEVSNF TGKRATSAPP VKRLQTTSRY
AGNAGAVDEE SFYAAFEDVP KVEIFSAKEL SIQLQQIRTI VMNTNGDWEK RIDSLKRLRS
LLISGASQYD EFFVELRSLE VPMQIAGKDL RSQVVREVCI TVAYLAERLG PKFDHFAEII
LPLLISLIQN SAKVVSTSGL ISCRFIIKNT HAPRIVPVIT GSLESKSKEI RRCCCDFIAM
MCQQWSSHEL EKNVGALQGA IRRGLSDADP EARAFSRKAY WSFSDHFRDQ AEMLFQSLDP
GKQRQLLGEV SQSSSSHSLY NDLRTSQESV KCSTASQYGA SRAGGTIPCL RSASEIDTGA
VRRAVAMKQA NAGKAFLGVA SSSNMNSLPR PMKMLLSTSG NYPKLESSTP RSPTSTSNKS
VSQRRKLDDV GSESPPCFFG ERSFRGSESS ENSNSMMDVL RSCSSTVWIE RKEGLLCLQS
FFRSGGRLAA GELKKACDLF ARLFVDPHHK MFTVFLDTVI EFLQAHGSDI QDWLFVLLCR
LLSKQSNELL PSVQSKLLKT MDVVRAVFPI EAQFQALTRY LVDPTQTPNV KMKLNVLNYL
NALIYSMQSC HMTDTADMRM AISRIVQWTG EPKSTEVRRT AQATLLALFS LNTPMFSQIL
SSFSKAYQDT VSRILNTHIR HFPDLSTLCI HDSAEQSSKV IERNSDVQDS LRRTSEEIMR
YPFSSDCKTT GSNGSTVLDT KNGSSGQGAR LGLLSNGVST DEERQEEIIG EILTELSNHN
ASTRQPQRFQ DYAELTILKL LDAHKDPERK VTRAAEDCAA VLALHLAPLV CLRVLTPVIV
NDQGPALLAA IKMTTKVIEQ MDTDELLRIL KELPTWAGRK CFIFLVDCDS AMFTEAAACT
AFQESITAIR DIYCHNSVTG ERDYLATVLY NTKKAENSHR FNGISVLHNL SLPSVEKVKQ
LESLCNGPPF NYFNENYGTG QSNIDEVFWL SAMIKVQNQR RTIFLFTNND SPHQGDAELR
KRGRKKIKDL KEKNVTVEVI AVGTTKFVLD NFYKVALADE HACQDDNLTL ANRADDLFSR
IVKKTRTRRG FATLNFSLGP GIDISVTLYN NISTANLPQS VMLDGRTNGE VKLISNLFDP
ETGEKLHRFN LVKYQEYGRR RIAMTEKELE QMSSFTSPVL LGFQPLNRLK VYHHLRPAFF
ISPNENIIKG STVLLNALMR KCSEKEMTMI CRLTARKNTS PRLVALVAQI ESEEAVQSAK
CRRFHGIYLP YEDDLRDLQA VIASAPKIQV DNHQLVDLWK KVIKRMQIQY TVGSIQNPVL
QKHYRTLEAV VLDREKIGHF VDQTMNLKWI DNEVGMLLQQ IKEHLNFADQ KESSSNCTDA
EFDLEAEARN GLLGKRTVVQ LRNALRSKGV VIASNTRKPE IIKRILDLYA L
//
