GenomeNet

Database: UniProt
Entry: A0A3G3JV66_9BACL
LinkDB: A0A3G3JV66_9BACL
Original site: A0A3G3JV66_9BACL 
ID   A0A3G3JV66_9BACL        Unreviewed;       295 AA.
AC   A0A3G3JV66;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   13-SEP-2023, entry version 15.
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=EAV92_05840 {ECO:0000313|EMBL:AYQ72132.1};
OS   Cohnella candidum.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2674991 {ECO:0000313|EMBL:AYQ72132.1, ECO:0000313|Proteomes:UP000269097};
RN   [1] {ECO:0000313|EMBL:AYQ72132.1, ECO:0000313|Proteomes:UP000269097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=18JY8-7 {ECO:0000313|EMBL:AYQ72132.1,
RC   ECO:0000313|Proteomes:UP000269097};
RA   Srinivasan S., Kim M.K.;
RT   "Genome Sequence of Cohnella sp.";
RL   Submitted (OCT-2018) 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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP033433; AYQ72132.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G3JV66; -.
DR   KEGG; coh:EAV92_05840; -.
DR   Proteomes; UP000269097; Chromosome.
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:UP000269097}.
FT   DOMAIN          52..180
FT                   /note="Ku"
FT                   /evidence="ECO:0000259|SMART:SM00559"
FT   REGION          251..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..287
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  33148 MW;  99623176A73978E4 CRC64;
     MQTVWKGAVS FGLVNVPVKM FTATKDNDIP MKMLHRKYNE PIRYTRTCPK CEKDVEWSDI
     VKGYEYEPGH FVTFDKEELE AISSENSREI RILDFVDLEE IDPIYYQKTY YLGPGDTGSR
     AYQLLIKALE TTNKIGIANV TIRSKSSLAA IRVVDGVLSM VTMFYAEEVR PVSQIPNLPE
     NESVDDRELE MAKMLIDQLT SSFEPNKYED EYKARLKEAI DRKVEGKDVK LAPEEKPTNV
     IDLMEALKAS LSQAQGGAQA PAKKGKKAAA SAAKKGSDEE EKKPKPAKRP KKTGA
//
DBGET integrated database retrieval system