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Database: UniProt
Entry: A0A1H7HB68_9ACTN
LinkDB: A0A1H7HB68_9ACTN
Original site: A0A1H7HB68_9ACTN 
ID   A0A1H7HB68_9ACTN        Unreviewed;       304 AA.
AC   A0A1H7HB68;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=SAMN05660976_00585 {ECO:0000313|EMBL:SEK45365.1};
OS   Nonomuraea pusilla.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=46177 {ECO:0000313|EMBL:SEK45365.1, ECO:0000313|Proteomes:UP000198953};
RN   [1] {ECO:0000313|EMBL:SEK45365.1, ECO:0000313|Proteomes:UP000198953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43357 {ECO:0000313|EMBL:SEK45365.1,
RC   ECO:0000313|Proteomes:UP000198953};
RA   de Groot N.N.;
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; FOBF01000001; SEK45365.1; -; Genomic_DNA.
DR   RefSeq; WP_055508481.1; NZ_FOBF01000001.1.
DR   AlphaFoldDB; A0A1H7HB68; -.
DR   STRING; 46177.SAMN05660976_00585; -.
DR   OrthoDB; 9795084at2; -.
DR   Proteomes; UP000198953; 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:UP000198953}.
FT   DOMAIN          52..180
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
FT   REGION          252..304
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..298
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   304 AA;  33945 MW;  929D49497B542694 CRC64;
     MRSIWKGAIS FGLVTIPVKL YSATEQKDVA FHQVHREDGG RIRYKRVCTV DGEEVAYADI
     AKGYELPTGE MVVLTDEDFE DLPLTTSRRI DVLQFTPAEQ IDPIYFAKTY YLEPDAQGSK
     PYVLLRDALE SSGQVAVVKV ALRQRESLAT LRVRDGIFVL ETMLWPDEIR APDFPFLEED
     IEVRPQELKM AESLISTMEA DFDPTEYHDA YREALQQVIE AKVAGKEVVA AREEEEAGPA
     VDLMAALRAS VEAAKRERAG ASAEPKPRKA AGKTGGRAAG RAQKEKEKEE EKAPAKQRKT
     RKSA
//
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