ID H2V3E5_TAKRU Unreviewed; 608 AA.
AC H2V3E5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 17-JUN-2020, sequence version 3.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=X-ray repair cross complementing 6 {ECO:0000313|Ensembl:ENSTRUP00000043727.3};
GN Name=xrcc6 {ECO:0000313|Ensembl:ENSTRUP00000043727.3};
OS Takifugu rubripes (Japanese pufferfish) (Fugu rubripes).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
OX NCBI_TaxID=31033 {ECO:0000313|Ensembl:ENSTRUP00000043727.3, ECO:0000313|Proteomes:UP000005226};
RN [1] {ECO:0000313|Ensembl:ENSTRUP00000043727.3, ECO:0000313|Proteomes:UP000005226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551351;
RA Kai W., Kikuchi K., Tohari S., Chew A.K., Tay A., Fujiwara A., Hosoya S.,
RA Suetake H., Naruse K., Brenner S., Suzuki Y., Venkatesh B.;
RT "Integration of the genetic map and genome assembly of fugu facilitates
RT insights into distinct features of genome evolution in teleosts and
RT mammals.";
RL Genome Biol. Evol. 3:424-442(2011).
RN [2] {ECO:0000313|Ensembl:ENSTRUP00000043727.3}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the ku70 family.
CC {ECO:0000256|ARBA:ARBA00005240}.
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DR AlphaFoldDB; H2V3E5; -.
DR STRING; 31033.ENSTRUP00000068872; -.
DR Ensembl; ENSTRUT00000043873.3; ENSTRUP00000043727.3; ENSTRUG00000017070.3.
DR GeneTree; ENSGT00940000153239; -.
DR OrthoDB; 21093at2759; -.
DR Proteomes; UP000005226; Chromosome 1.
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 CDD; cd01458; vWA_ku; 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 NCBIfam; TIGR00578; ku70; 1.
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.
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 Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000005226}.
FT DOMAIN 304..450
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT DOMAIN 571..606
FT /note="SAP"
FT /evidence="ECO:0000259|SMART:SM00513"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..560
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 27
FT /note="Schiff-base intermediate with DNA; for 5'-
FT deoxyribose-5-phosphate lyase activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR003033-1"
SQ SEQUENCE 608 AA; 68648 MW; 57C2B823D9AF6AE4 CRC64;
MAQWNAYYHN DDEEEEQEDG EQFRDYKVTG RDSLVFLVDA SKEMFVKGED GQPSNFDLSM
QVVRSVYTSK IISSHRDLMA LVFYGTEQSK NPSNSFKHVY VYHNLDEPGA KRVQEVDALQ
GEKGARLMEK TMGSGETSLG DALWCCANLY SDIKLRLSFK RLMIFTCRDE PHGGDTAKDR
QARTKASDLK ETGVFIDLMH LMKPGGFDVS TFFCDIISPD SEGELGLQLE PCGKLEDLKK
RVRAKEQKKR AMSRLNLSLG EGLNLAVGIY AMAVPAKIPG SVKLYRETNK QVHSKPQTFD
TQTGRLLLPS EIKKAQVYGK KQIVMERDEV DSIKKFEDPG LYLIGFKPIK MLKIHHHIRP
AVFIYPEENM VKGSSCLFSA LLTKCSEKDV FALCRCILRR NCPPRFAALV PQKEELDEGK
VQITAPGFHL IYLPYADDIR TLDPPQFPSA SQIPVDKMKQ IVSKLRFKYR SDAFENPAIQ
KHFRNLEALA LDMMAPEDVE DLIMPKVDQI NQRLGPLAEE FKDLVYPANY NPESKPTTKR
KSADNGGGDE KKARVEVSEE ELRAHVQNGT LGKLTVPVLK EACKKMGFRT TGTKKQELID
ALIAQMGP
//
