ID KU_BPMCO Reviewed; 284 AA.
AC Q856K7;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Protein Ku;
DE AltName: Full=Cd-Ku;
DE AltName: Full=Gp87;
GN Name=87;
OS Mycobacterium phage Corndog (Mycobacteriophage Corndog).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Corndogvirus.
OX NCBI_TaxID=205875;
OH NCBI_TaxID=246196; Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12705866; DOI=10.1016/s0092-8674(03)00233-2;
RA Pedulla M.L., Ford M.E., Houtz J.M., Karthikeyan T., Wadsworth C.,
RA Lewis J.A., Jacobs-Sera D., Falbo J., Gross J., Pannunzio N.R., Brucker W.,
RA Kumar V., Kandasamy J., Keenan L., Bardarov S., Kriakov J., Lawrence J.G.,
RA Jacobs W.R. Jr., Hendrix R.W., Hatfull G.F.;
RT "Origins of highly mosaic mycobacteriophage genomes.";
RL Cell 113:171-182(2003).
RN [2]
RP FUNCTION, SUBUNIT, PROBABLE INTERACTION WITH HOST LIGD, AND DNA-BINDING.
RX PubMed=16949369; DOI=10.1016/j.molcel.2006.07.009;
RA Pitcher R.S., Tonkin L.M., Daley J.M., Palmbos P.L., Green A.J.,
RA Velting T.L., Brzostek A., Korycka-Machala M., Cresawn S., Dziadek J.,
RA Hatfull G.F., Wilson T.E., Doherty A.J.;
RT "Mycobacteriophage exploit NHEJ to facilitate genome circularization.";
RL Mol. Cell 23:743-748(2006).
CC -!- FUNCTION: Required for replication of viruses with short cos ends (4
CC bases). Stimulates dsDNA end-joining by host LigD. Binds dsDNA with
CC either blunt, 5'- or 3-overhangs, protecting it from host exonuclease
CC degradation. {ECO:0000269|PubMed:16949369}.
CC -!- SUBUNIT: Homodimer (Probable). Interacts with host LigD.
CC {ECO:0000269|PubMed:16949369, ECO:0000305}.
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DR EMBL; AY129335; AAN02019.1; -; Genomic_DNA.
DR RefSeq; NP_817938.1; NC_004685.1.
DR SMR; Q856K7; -.
DR GeneID; 1259566; -.
DR KEGG; vg:1259566; -.
DR OrthoDB; 5222at10239; -.
DR Proteomes; UP000000964; Segment.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
DR GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:InterPro.
DR GO; GO:0099016; P:evasion by virus of DNA end degradation; IEA:UniProtKB-KW.
DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
DR GO; GO:0099009; P:viral genome circularization; IEA:UniProtKB-KW.
DR Gene3D; 2.40.290.10; -; 1.
DR InterPro; IPR006164; Ku70/Ku80_beta-barrel_dom.
DR InterPro; IPR009187; Prok_Ku.
DR InterPro; IPR016194; SPOC-like_C_dom_sf.
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 1: Evidence at protein level;
KW DNA end degradation evasion by virus; DNA-binding; Host-virus interaction;
KW Inhibition of host innate immune response by virus; Reference proteome;
KW Viral genome circularization; Viral immunoevasion;
KW Virus entry into host cell.
FT CHAIN 1..284
FT /note="Protein Ku"
FT /id="PRO_0000425947"
FT DOMAIN 10..189
FT /note="Ku"
SQ SEQUENCE 284 AA; 30836 MW; 7EF2455A3F63DC77 CRC64;
MRSVGNVDLT IGLVTVPVKM VGVSESHDRK ASMYHPHEDG NFGKIKMPKL CEDCGEVVPT
ADIAKGFEEG GDIVILTADE LASIAAATGA ALEVPQFVKA EQINPMLFAN ENIYRLVPDP
KRGRQAATTY LMVRHILVSQ ELVGVVQYTR WGRNRLGVLD VEPSDDGGVL VIRNMMWADE
LRSTEGIVPT NVTEDDIDPR LLPVMASVVE SMTGDWDPTA YTDRYTEQLS EAITAKAQGD
EIATVASESG KAIDDVSDLL AKLEASIQKK APAKKATARR KKTA
//
