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Database: UniProt
Entry: A0A1M5ZEL8_9FIRM
LinkDB: A0A1M5ZEL8_9FIRM
Original site: A0A1M5ZEL8_9FIRM 
ID   A0A1M5ZEL8_9FIRM        Unreviewed;       273 AA.
AC   A0A1M5ZEL8;
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=SAMN02745823_03613 {ECO:0000313|EMBL:SHI22631.1};
OS   Sporobacter termitidis DSM 10068.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Sporobacter.
OX   NCBI_TaxID=1123282 {ECO:0000313|EMBL:SHI22631.1, ECO:0000313|Proteomes:UP000183995};
RN   [1] {ECO:0000313|EMBL:SHI22631.1, ECO:0000313|Proteomes:UP000183995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10068 {ECO:0000313|EMBL:SHI22631.1,
RC   ECO:0000313|Proteomes:UP000183995};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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; FQXV01000018; SHI22631.1; -; Genomic_DNA.
DR   RefSeq; WP_073082454.1; NZ_FQXV01000018.1.
DR   AlphaFoldDB; A0A1M5ZEL8; -.
DR   STRING; 1123282.SAMN02745823_03613; -.
DR   OrthoDB; 9795084at2; -.
DR   Proteomes; UP000183995; 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:UP000183995}.
FT   DOMAIN          52..180
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
FT   REGION          249..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        252..267
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   273 AA;  30813 MW;  4F106229A6C93A7C CRC64;
     MPVAHRTVIS FGLVAIPVSL YTATQDNDIH FNQLHKDDQG RVRYKKTCAH CGKELKSEDI
     IKGYEYDKDR YVVIADEEIE KIKTEKDKSI QILHFAQLNQ ISPVYYDKTY QAVPDTGGER
     AFELLRSALM KEQKIAIGKT VMGTKDTLMA IIPRENGVLI STMFYQDDIK ELQKSYQIPE
     PTEQELKMAQ VLIGSMDTPF DPAQYKDEYQ GKLKELVESK ISGKEIVAAK PEQAGNVINL
     MDALKASIDK QNAGKETPED KPPAKRTSRK KGA
//
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