ID   KU_DESHD                Reviewed;         285 AA.
AC   B8FRH5;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Non-homologous end joining protein Ku {ECO:0000255|HAMAP-Rule:MF_01875};
GN   Name=ku {ECO:0000255|HAMAP-Rule:MF_01875}; OrderedLocusNames=Dhaf_3719;
OS   Desulfitobacterium hafniense (strain DSM 10664 / DCB-2).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=272564;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10664 / DCB-2;
RX   PubMed=22316246; DOI=10.1186/1471-2180-12-21;
RA   Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L.,
RA   Tiedje J.M.;
RT   "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive
RT   anaerobe capable of dehalogenation and metal reduction.";
RL   BMC Microbiol. 12:21-21(2012).
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:0000255|HAMAP-Rule:MF_01875}.
CC   -!- SUBUNIT: Homodimer. Interacts with LigD. {ECO:0000255|HAMAP-
CC       Rule:MF_01875}.
CC   -!- SIMILARITY: Belongs to the prokaryotic Ku family. {ECO:0000255|HAMAP-
CC       Rule:MF_01875}.
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DR   EMBL; CP001336; ACL21735.1; -; Genomic_DNA.
DR   RefSeq; WP_005813277.1; NC_011830.1.
DR   AlphaFoldDB; B8FRH5; -.
DR   SMR; B8FRH5; -.
DR   EnsemblBacteria; ACL21735; ACL21735; Dhaf_3719.
DR   KEGG; dhd:Dhaf_3719; -.
DR   HOGENOM; CLU_048975_1_0_9; -.
DR   OMA; IRYRKVC; -.
DR   Proteomes; UP000007726; Chromosome.
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   PANTHER; PTHR41251; PTHR41251; 1.
DR   Pfam; PF02735; Ku; 1.
DR   PIRSF; PIRSF006493; Prok_Ku; 1.
DR   SMART; SM00559; Ku78; 1.
DR   SUPFAM; SSF100939; SSF100939; 1.
DR   TIGRFAMs; TIGR02772; Ku_bact; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA recombination; DNA repair; DNA-binding.
FT   CHAIN           1..285
FT                   /note="Non-homologous end joining protein Ku"
FT                   /id="PRO_0000389182"
FT   DOMAIN          9..176
FT                   /note="Ku"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01875"
FT   REGION          250..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..274
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   285 AA;  32606 MW;  606EE3A011FBFE6F CRC64;
     MHTVWKGSIS FGLVNVPVKM HAATETHEFH FNYLHKDCHN RIRYIKKCPH CEVEVAAENI
     IKGYEYEKDH YVIMEEEDLA SLEAPLSRSI DILDFIDLSD IDPIYYQKSY YLSPEEAAHK
     AYKLLCQAMS DTGKVAIAKL TMRSKQHLAC LRIIDQSIMV LETMYYPAEI RHLEASWDNV
     SPTDTEIAMA RQLIENLAAP FAPEKYRDEL REQVKELIEK KVSGETYRVA AAPEPGKVVD
     LMEALRASIA MTDQKKQQNT AESETEEKPT KSTLTPRGRR KVKGA