ID A0A2T6AJE0_9RHOB Unreviewed; 303 AA.
AC A0A2T6AJE0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=C8N44_12320 {ECO:0000313|EMBL:PTX43922.1};
OS Allosediminivita pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Allosediminivita.
OX NCBI_TaxID=1267769 {ECO:0000313|EMBL:PTX43922.1, ECO:0000313|Proteomes:UP000244069};
RN [1] {ECO:0000313|EMBL:PTX43922.1, ECO:0000313|Proteomes:UP000244069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29329 {ECO:0000313|EMBL:PTX43922.1,
RC ECO:0000313|Proteomes:UP000244069};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (APR-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 -!- 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:PTX43922.1}.
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DR EMBL; QBKN01000023; PTX43922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T6AJE0; -.
DR OrthoDB; 9780854at2; -.
DR Proteomes; UP000244069; 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:UP000244069}.
FT DOMAIN 54..185
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT REGION 226..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..303
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 303 AA; 33378 MW; FC8B5A4AA67D8784 CRC64;
MASRAVWKGQ IRLSLVSIGI EIYPATTSGP RISFRQIHKP TGKRVRYEKT VKGVGPVDSD
DIVKGYETGK GEYVLFEPEE IEELKVETSK TLELVQFVET GEIPPLYFEK PYYVVPQDDL
AEDAYRVIRD ALRAERKTAL CQITLRGKER LAAIRPCGDG LLLETLRYAD EIREAEPMFS
EISDDEADEE MLDLARELIG RKTKSFDASA FSDSYHQALK ELIDARRKDK SAETAETEED
SEDDGDNVVD LMGALKKSLE KSEGGSSGKS KGGAKSKGTS KSSSKSSSSK SSAKGSGSRK
KAS
//
