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Database: UniProt
Entry: A0A2K5IF44_COLAP
LinkDB: A0A2K5IF44_COLAP
Original site: A0A2K5IF44_COLAP 
ID   A0A2K5IF44_COLAP        Unreviewed;       559 AA.
AC   A0A2K5IF44;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=SAP domain-containing protein {ECO:0000259|PROSITE:PS50800};
OS   Colobus angolensis palliatus (Peters' Angolan colobus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Colobus.
OX   NCBI_TaxID=336983 {ECO:0000313|Ensembl:ENSCANP00000015235.1, ECO:0000313|Proteomes:UP000233080};
RN   [1] {ECO:0000313|Ensembl:ENSCANP00000015235.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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   RefSeq; XP_011800482.1; XM_011945092.1.
DR   AlphaFoldDB; A0A2K5IF44; -.
DR   SMR; A0A2K5IF44; -.
DR   Ensembl; ENSCANT00000038168.1; ENSCANP00000015235.1; ENSCANG00000031032.1.
DR   GeneID; 105514005; -.
DR   CTD; 2547; -.
DR   OrthoDB; 21093at2759; -.
DR   Proteomes; UP000233080; 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: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:0010558; P:negative regulation of macromolecule biosynthetic process; IEA:UniProt.
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   Host-virus interaction {ECO:0000256|ARBA:ARBA00022581};
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:UP000233080}.
FT   DOMAIN          523..557
FT                   /note="SAP"
FT                   /evidence="ECO:0000259|PROSITE:PS50800"
FT   REGION          486..513
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..513
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   559 AA;  64253 MW;  D4031A674DF6516B CRC64;
     MKKQKKNKKR TLKQVCIQSV YISKIISSDR DLLAVVFYGT EKDKNSVNFK NIYVLQELDN
     PGAKRILELD QFKGQQGQKR FQDLMGHGSD YSLSEVLWVC ANLFSDVQFK MSHKRIMLFT
     NEDNPHGNDS AKASRARTKA GDLRDTGIFL DLMHLKKPGG FDISLFYRDI ISIAEDEDLR
     VHFEESSKLE DLLRKVRAKE TRKRALSRLK LKLNKDIVIS VGVYNLVQKA LKPPPIKLYR
     ETNEPVKTKT RTFNTSTGGL LLPSDTKRSQ IYGSRQIILE KEETEELKRF DDPGLMLMGF
     KPLVLLKKHH YLRPSLFVYP EESLVIGSST LFSALLIKCL EKEVAALCRY TPRRNIPPYF
     VALVPQDEEL DDQKIQVTPP GFQLVFLPFA DDKRKMPFTE KIMATPEQVD KMKAIVEKLR
     FTYRSDSFEN PVLQQHFRNL EALALDLMEP EQAVDLTLPK VEAMNKRLGS LVDEFKELVY
     PPDYNPEGKV TKRKHDNDGS GSKRPKVEYS EEELKTHISK GTLGKFTVPM LKEACRAYGL
     KSGLKKQELL EALTKHFQD
//
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