ID A0A0N1JTQ8_9NEIS Unreviewed; 399 AA.
AC A0A0N1JTQ8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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=ykoV {ECO:0000313|EMBL:KPC54779.1};
GN Synonyms=ku {ECO:0000256|HAMAP-Rule:MF_01875};
GN ORFNames=WG78_04380 {ECO:0000313|EMBL:KPC54779.1};
OS Amantichitinum ursilacus.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Chitinibacteraceae; Amantichitinum.
OX NCBI_TaxID=857265 {ECO:0000313|EMBL:KPC54779.1, ECO:0000313|Proteomes:UP000037939};
RN [1] {ECO:0000313|EMBL:KPC54779.1, ECO:0000313|Proteomes:UP000037939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IGB-41 {ECO:0000313|EMBL:KPC54779.1,
RC ECO:0000313|Proteomes:UP000037939};
RA Kirstahler P., Guenther M., Grumaz C., Rupp S., Zibek S., Sohn K.;
RT "Draft genome sequence of the Amantichitinum ursilacus IGB-41, a new
RT chitin-degrading bacterium.";
RL Submitted (JUL-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:KPC54779.1}.
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DR EMBL; LAQT01000002; KPC54779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1JTQ8; -.
DR STRING; 857265.WG78_04380; -.
DR PATRIC; fig|857265.3.peg.898; -.
DR OrthoDB; 9795084at2; -.
DR Proteomes; UP000037939; 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:UP000037939}.
FT DOMAIN 53..181
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT REGION 278..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..393
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 399 AA; 42748 MW; EBEBADA2DA359983 CRC64;
MARALWSGAI SFGLIFIPVS LNSAESPDEL DLTLLDKRDF SKVGYKRVNK TTGKEVTWAD
IIKGYEYQPG EYVALGDEDF KHANVKATQT IDLLAFVDQD EIDPVYFEKP YYLSPGKRGE
KVYGLLREAL KKSGKVGVAQ IVIRVKQHLA VVAAVGDALV LNTLRYPEEI KDVDELGLPQ
TAVKPGLSSK EVDMAVQLVE GMSDDWHPDQ YHDQYREDLL KLIDRKIKAR QTHTVNAPME
DEDQPVPGSA NVLDLMALLK KSLPAAKGKA GKLKRAEADV ADNDDADEDQ AEQAAPQRKA
TRTAKAPAKA SATAAKTGAK AATRVSAARP ASKKIATATA KPAAKPAAKP AAKPAAKPAA
KPAVKPAATA ARAASKPKAT AQPATQRKTA TASTKRKAA
//
