ID A0A101U650_9ACTN Unreviewed; 354 AA.
AC A0A101U650;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=AQJ67_10785 {ECO:0000313|EMBL:KUO04694.1};
OS Streptomyces caeruleatus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=661399 {ECO:0000313|EMBL:KUO04694.1, ECO:0000313|Proteomes:UP000053429};
RN [1] {ECO:0000313|EMBL:KUO04694.1, ECO:0000313|Proteomes:UP000053429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-24802 {ECO:0000313|EMBL:KUO04694.1,
RC ECO:0000313|Proteomes:UP000053429};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces caeruleatus NRRL B-24802, type
RT strain for the species Streptomyces caeruleatus.";
RL Submitted (OCT-2015) 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:KUO04694.1}.
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DR EMBL; LMWY01000011; KUO04694.1; -; Genomic_DNA.
DR RefSeq; WP_062718544.1; NZ_KQ948926.1.
DR AlphaFoldDB; A0A101U650; -.
DR STRING; 661399.AQJ67_10785; -.
DR OrthoDB; 9795084at2; -.
DR Proteomes; UP000053429; 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:UP000053429}.
FT DOMAIN 52..181
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT REGION 251..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..342
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 354 AA; 38217 MW; F77C1954BFD2C6D8 CRC64;
MRSIWNGAIS FGLVSIPIKL VNATENRSIS FRQIHTEDGG RIRYRKVCEL EDREVTQGEI
GKGYEDADGT IIPITDEDLS HLPLPTAKTI EIVAFVPADR IDPLQMDSAY YLAAGGAPAA
KPYTLLREAL KRSQKVAIAK YALRGRERLG MLRVVEDAIA MHGLLWPDEV RAPEGVAPDT
HVTVNDKELD LADALMDTLG EIELDELHDA YREALEEVVA AKAAGEAPPE TPEPAKAGKV
LDLMAALENS VRAAKESRGE EPTAPEKKEA QVRRLPERKT SRAAPKQTAG KKSTATKKTA
AKKTASAKKS TAKTAQGAKK TAAKSTTKST AKSTAKSTAK KSTAKKTTAR KRTA
//
