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Database: UniProt
Entry: A0A1K2FMU8_9ACTN
LinkDB: A0A1K2FMU8_9ACTN
Original site: A0A1K2FMU8_9ACTN 
ID   A0A1K2FMU8_9ACTN        Unreviewed;       307 AA.
AC   A0A1K2FMU8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=STEPF1_01567 {ECO:0000313|EMBL:SFY48343.1};
OS   Streptomyces sp. F-1.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=463642 {ECO:0000313|EMBL:SFY48343.1, ECO:0000313|Proteomes:UP000095403};
RN   [1] {ECO:0000313|EMBL:SFY48343.1, ECO:0000313|Proteomes:UP000095403}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Streptomyces sp. F1 {ECO:0000313|EMBL:SFY48343.1};
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; FKJI03000003; SFY48343.1; -; Genomic_DNA.
DR   RefSeq; WP_070029862.1; NZ_FKJI03000003.1.
DR   AlphaFoldDB; A0A1K2FMU8; -.
DR   OrthoDB; 9795084at2; -.
DR   Proteomes; UP000095403; 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:UP000095403}.
FT   DOMAIN          53..182
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
FT   REGION          244..307
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        255..275
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        276..307
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   307 AA;  34030 MW;  6EC2402997FFD357 CRC64;
     MPRTIWSGAI SFGLVTVPIN VQSATEDHSI HFHQYHLADQ GRIRYRKVCE LEDREVSQDE
     IGKGYELTKT QVVPITDEDL SNLPLPTAKA IEIDAFVPLE SVDPLKIAEG YYLQPAGQVA
     AKPYKLLVEA LGRSAKVAVA KYAWSGRERL GLLRVKDDVL VLHAMRWPDE IRDPAELLPP
     PVEVSDDEIE GALALMDTMT VDALEGPDFH DRYTEAIAEI IEAKREEKPL PEAPEPEQPA
     QVLDLMAALQ ESVSKARASR DEPTEPAEVH ELPRPKKKAA TKKQPAKKAQ AKKTTAKKAS
     GRRSRSA
//
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