ID A0A066YL27_9ACTN Unreviewed; 357 AA.
AC A0A066YL27;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 36.
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=KCH_76100 {ECO:0000313|EMBL:KDN80634.1};
OS Kitasatospora cheerisanensis KCTC 2395.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN80634.1, ECO:0000313|Proteomes:UP000027178};
RN [1] {ECO:0000313|EMBL:KDN80634.1, ECO:0000313|Proteomes:UP000027178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN80634.1,
RC ECO:0000313|Proteomes:UP000027178};
RA Nam D.H.;
RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL Submitted (MAY-2014) 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:KDN80634.1}.
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DR EMBL; JNBY01000168; KDN80634.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066YL27; -.
DR PATRIC; fig|1348663.4.peg.7359; -.
DR eggNOG; COG1273; Bacteria.
DR HOGENOM; CLU_048975_1_1_11; -.
DR Proteomes; UP000027178; 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 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:UP000027178}.
FT DOMAIN 49..179
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT REGION 254..316
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..298
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 357 AA; 39541 MW; 150EC2FA4EEBBA85 CRC64;
MWSGVLTFGL VTVPVALYTA TDSHSVRFHQ LQRGTGDRVR NKRVNERTGE EVPYQDIVKG
YEVTEGEYVV VEPEELEQIS PGRSRTIDIS GFVDLDQVDP IFFDKTYYLG PKGKEYAKVF
QLLTEALTRS NRAGIALFSM RGKEYLTAVR AEDGLLELHT MHWADELRDP RKEIGDLPDG
RAGYSRQELA TAEQLVDMLT VDWDPSDYRD TYEEQVEKLI EDKLAGRETA VSEGPPAEAT
NVVDLMAVLE RSLEGAKSGG KAPAAEAGQE SDGRRSGTSR ATPKKTGGKK TTGTDTSRKT
ATAKKRAGAK DDLSRLTKAE LYEKAARHDI ARRSTMTRDE LQEAVAKAER GHLRAAS
//
