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Database: UniProt
Entry: A0A1L6HXJ7_9BURK
LinkDB: A0A1L6HXJ7_9BURK
Original site: A0A1L6HXJ7_9BURK 
ID   A0A1L6HXJ7_9BURK        Unreviewed;       336 AA.
AC   A0A1L6HXJ7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=BTO02_12440 {ECO:0000313|EMBL:APR36086.1};
OS   Paraburkholderia sp. SOS3.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1926494 {ECO:0000313|EMBL:APR36086.1, ECO:0000313|Proteomes:UP000184708};
RN   [1] {ECO:0000313|EMBL:APR36086.1, ECO:0000313|Proteomes:UP000184708}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SOS3 {ECO:0000313|EMBL:APR36086.1,
RC   ECO:0000313|Proteomes:UP000184708};
RA   Song W.-J., Kurnit D.M.;
RL   Submitted (DEC-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; CP018811; APR36086.1; -; Genomic_DNA.
DR   RefSeq; WP_075157290.1; NZ_CP018811.1.
DR   AlphaFoldDB; A0A1L6HXJ7; -.
DR   STRING; 1926494.BTO02_12440; -.
DR   KEGG; para:BTO02_12440; -.
DR   OrthoDB; 9795084at2; -.
DR   Proteomes; UP000184708; Chromosome 1.
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}.
FT   DOMAIN          53..181
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
FT   REGION          262..336
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..306
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   336 AA;  37087 MW;  0114EFF1135DC61F CRC64;
     MAHMIWKGAI SFGLVHVPVQ LYPATQSEKV GFNLLDKRSI DPIGYKQINK RTGKEVTREN
     IVRGFEYEKG KYVVMSDAEI RSANPESTQT VDILAFVEAP DISFLYLDTP YYLTPDRKGE
     KVYALLREAL KESGKIGIAN VVMHNKQHLA ALIPIGPVLA LNTLRWAGEV RSYDELKLPD
     ENRKKAGVTP RELEMAKKLI DDMSDAWDPS AYHDTFHDDI MALVDRKVSE GRTEEIGEVD
     EPADTRPSAD ILDLSELLKR SLGKGKAAGA RKSAAKADGK ATAKPARARA SRDEDAEQET
     GANTRRAPRR AAKSKATTRR SSGGASSTAV RKRRAA
//
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