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Database: UniProt
Entry: A0A2G5CX97_AQUCA
LinkDB: A0A2G5CX97_AQUCA
Original site: A0A2G5CX97_AQUCA 
ID   A0A2G5CX97_AQUCA        Unreviewed;       640 AA.
AC   A0A2G5CX97;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=SAP domain-containing protein {ECO:0000259|PROSITE:PS50800};
GN   ORFNames=AQUCO_03400046v1 {ECO:0000313|EMBL:PIA35886.1};
OS   Aquilegia coerulea (Rocky mountain columbine).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Ranunculales; Ranunculaceae; Thalictroideae;
OC   Aquilegia.
OX   NCBI_TaxID=218851 {ECO:0000313|EMBL:PIA35886.1, ECO:0000313|Proteomes:UP000230069};
RN   [1] {ECO:0000313|EMBL:PIA35886.1, ECO:0000313|Proteomes:UP000230069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Goldsmith {ECO:0000313|Proteomes:UP000230069};
RA   Hodges S., Kramer E., Nordborg M., Tomkins J., Borevitz J., Derieg N.,
RA   Yan J., Mihaltcheva S., Hayes R.D., Rokhsar D.;
RT   "WGS assembly of Aquilegia coerulea Goldsmith.";
RL   Submitted (SEP-2017) 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}.
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DR   EMBL; KZ305051; PIA35886.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2G5CX97; -.
DR   STRING; 218851.A0A2G5CX97; -.
DR   InParanoid; A0A2G5CX97; -.
DR   OrthoDB; 21093at2759; -.
DR   Proteomes; UP000230069; 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: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.
DR   PROSITE; PS50800; SAP; 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:UP000230069}.
FT   DOMAIN          604..638
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..19
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   640 AA;  72183 MW;  5E88B9D5F046CB6E CRC64;
     MDLDPEDLFK DDEDDPENEF QGREYTKELV VYLVDASPQM FSPISTLDDN KGENHFGIAV
     NCISQSLKSQ IISRSYDEVA ICFFNTSKKK NLQDLNGVFV FNVAEREDLD RPTARLIKEF
     DSIEETFAKE IGSQYGIISG SRENSLYNAI WVAQALLRKG SAKTTDKRML LFTNNDDPFG
     DIRGATKADM IRTTLQRAKD AQDLGISIEL LPLCRPEEEF NVSLFYADLI GLDDEDLDQF
     IPSAGEKLED MKDELRKRMF KKRKVRRITF LISNGISIEL NTYALVRPTL PGQITWLDSV
     TNVPLKTERS FICADTGALL EEPSKRVQSY KGENVKFSTE ELTEIKRVST GQLRLLGFKP
     LSCLKDYYNL RPSTFVFPSD ESNDSVSVLR YNQEILGSSC IFIALHRSML RLRRFALAFY
     GSSSHPQLVA LVAQDEITSS CGQVEPPGMH MIYLPYSDDI RHVEELHVDV GSVAPRATDD
     KVKKADALMK RVDLKDFSVC QFANPALQRH YAVLQALALD EDEMPEVKDE TLPDEQGMSR
     QGVVNALEEF KISVYGENYD QEEADALSSK TSSEAAKKRK AIAECAVKEC ANYDWAELAD
     NGKLKDLTVV ELKYYLAAHS LTLTGKKDVL ISRILTHLGK
//
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