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Database: UniProt
Entry: A0A1H3DFS2_9PSED
LinkDB: A0A1H3DFS2_9PSED
Original site: A0A1H3DFS2_9PSED 
ID   A0A1H3DFS2_9PSED        Unreviewed;       311 AA.
AC   A0A1H3DFS2;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Non-homologous end joining protein Ku {ECO:0000256|HAMAP-Rule:MF_01875};
GN   Name=ku {ECO:0000256|HAMAP-Rule:MF_01875};
GN   ORFNames=SAMN05216287_3406 {ECO:0000313|EMBL:SDX65170.1};
OS   Pseudomonas kuykendallii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1007099 {ECO:0000313|EMBL:SDX65170.1, ECO:0000313|Proteomes:UP000243778};
RN   [1] {ECO:0000313|Proteomes:UP000243778}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-59562 {ECO:0000313|Proteomes:UP000243778};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: With LigD forms a non-homologous end joining (NHEJ) DNA
CC       repair enzyme, which repairs dsDNA breaks with reduced fidelity. Binds
CC       linear dsDNA with 5'- and 3'- overhangs but not closed circular dsDNA
CC       nor ssDNA. Recruits and stimulates the ligase activity of LigD.
CC       {ECO:0000256|HAMAP-Rule:MF_01875}.
CC   -!- SUBUNIT: Homodimer. Interacts with LigD. {ECO:0000256|HAMAP-
CC       Rule:MF_01875}.
CC   -!- SIMILARITY: Belongs to the prokaryotic Ku family. {ECO:0000256|HAMAP-
CC       Rule:MF_01875}.
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DR   EMBL; FNNU01000005; SDX65170.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3DFS2; -.
DR   STRING; 1007099.SAMN05216287_3406; -.
DR   OrthoDB; 9795084at2; -.
DR   Proteomes; UP000243778; Unassembled WGS sequence.
DR   GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:UniProtKB-UniRule.
DR   CDD; cd00789; KU_like; 1.
DR   Gene3D; 2.40.290.10; -; 1.
DR   HAMAP; MF_01875; Prokaryotic_Ku; 1.
DR   InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR   InterPro; IPR009187; Prok_Ku.
DR   InterPro; IPR016194; SPOC-like_C_dom_sf.
DR   NCBIfam; TIGR02772; Ku_bact; 1.
DR   PANTHER; PTHR41251; NON-HOMOLOGOUS END JOINING PROTEIN KU; 1.
DR   PANTHER; PTHR41251:SF1; NON-HOMOLOGOUS END JOINING PROTEIN KU; 1.
DR   Pfam; PF02735; Ku; 1.
DR   PIRSF; PIRSF006493; Prok_Ku; 1.
DR   SMART; SM00559; Ku78; 1.
DR   SUPFAM; SSF100939; SPOC domain-like; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_01875};
KW   DNA recombination {ECO:0000256|HAMAP-Rule:MF_01875};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_01875};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|HAMAP-
KW   Rule:MF_01875}; Reference proteome {ECO:0000313|Proteomes:UP000243778}.
FT   DOMAIN          53..181
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
FT   REGION          227..311
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        227..253
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        274..293
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   311 AA;  34452 MW;  ED2168156AA296DE CRC64;
     MPRVIWKGAV SFGLVHIPVA LVPATTRQGV DFDWLDKRSM DPVGYKRINK VTGKDIEKEN
     IVKGVELEKG NYVVISEEEI RAAHPKVTQT VDIVAFVDAE KIPFLFIDTP YYLTPDRRGE
     KVYALLREAL VATGKVGLAN VVLHTKQHLA VVMPLGEALV LNTLRWADEV RGIEALELKD
     EAIKPDLAKR ELDMATRLIE EMSEDWQPEQ YKDTFQEQIM ALVEQKAKEG KVEAVSEPDD
     DGGERRSADV IDLTELLKRS LGAKPAASKP AAKAAPKKTE KIEKAEKPAR KPAAKTATKP
     AAGRTTKKKA S
//
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