ID L7KRJ1_9ACTN Unreviewed; 327 AA.
AC L7KRJ1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=GOACH_23_00480 {ECO:0000313|EMBL:GAC50338.1};
OS Gordonia aichiensis NBRC 108223.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1220583 {ECO:0000313|EMBL:GAC50338.1, ECO:0000313|Proteomes:UP000010988};
RN [1] {ECO:0000313|EMBL:GAC50338.1, ECO:0000313|Proteomes:UP000010988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108223 {ECO:0000313|EMBL:GAC50338.1,
RC ECO:0000313|Proteomes:UP000010988};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia aichiensis NBRC 108223.";
RL Submitted (DEC-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAC50338.1}.
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DR EMBL; BANR01000023; GAC50338.1; -; Genomic_DNA.
DR RefSeq; WP_005177974.1; NZ_BANR01000023.1.
DR AlphaFoldDB; L7KRJ1; -.
DR STRING; 1220583.GOACH_23_00480; -.
DR eggNOG; COG1273; Bacteria.
DR OrthoDB; 9795084at2; -.
DR Proteomes; UP000010988; 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; 2.
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:UP000010988}.
FT DOMAIN 55..184
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT REGION 259..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..279
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..320
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 327 AA; 36245 MW; FA4E50D388888DA1 CRC64;
MVRMRSIWKG DLSFGLVNVP VKVYSATESH DRKSYQVDSS DGARIRYRRV REGTDTEVDY
SDIANAYETD SGDSVILTKE DLASLPVQKS PEISIVEFVP VDQVDPIYFD KPYYLEPSSK
SPKAYVLLAK ALQETDRLAI ASFTLRNRTR MAALRVIEPG VMTLQTLLWP DEVRKPDFDF
LGEDVQIRDQ ELKMASSLID SMATDYDPDE FSDTYQDELS KLIEAKAEGG EAFPEAEEKE
TVDEDSEVAD LLAALRASVK DSSTAKDSAS ENSSATPRKA PAKKTAAKKE PAKKTAAKKT
ATKKTTAEKT TAEKTTAKKT TRKRAAS
//
