ID V5XFH7_MYCNE Unreviewed; 309 AA.
AC V5XFH7;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=D174_22690 {ECO:0000313|EMBL:AHC27180.1};
OS Mycolicibacterium neoaurum VKM Ac-1815D.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=700508 {ECO:0000313|EMBL:AHC27180.1, ECO:0000313|Proteomes:UP000018763};
RN [1] {ECO:0000313|EMBL:AHC27180.1, ECO:0000313|Proteomes:UP000018763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM Ac-1815D {ECO:0000313|EMBL:AHC27180.1,
RC ECO:0000313|Proteomes:UP000018763};
RX PubMed=24435872;
RA Shtratnikova V.Y., Bragin E.Y., Dovbnya D.V., Pekov Y.A., Schelkunov M.I.,
RA Strizhov N., Ivashina T.V., Ashapkin V.V., Donova M.V.;
RT "Complete Genome Sequence of Sterol-Transforming Mycobacterium neoaurum
RT Strain VKM Ac-1815D.";
RL Genome Announc. 2:e01177-13(2014).
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}.
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DR EMBL; CP006936; AHC27180.1; -; Genomic_DNA.
DR RefSeq; WP_019510361.1; NC_023036.2.
DR AlphaFoldDB; V5XFH7; -.
DR KEGG; mne:D174_22690; -.
DR eggNOG; COG1273; Bacteria.
DR HOGENOM; CLU_048975_1_1_11; -.
DR Proteomes; UP000018763; 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:UP000018763}.
FT DOMAIN 52..184
FT /note="Ku"
FT /evidence="ECO:0000259|SMART:SM00559"
FT REGION 260..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 281..309
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 309 AA; 34538 MW; 31DADB6E1C848A9B CRC64;
MRSIWKGSVS FGLVNVPVKV YSATEDHDIK FHQVHEKDNG RIRYKRTCEV CGEVVEYRDI
ARAYDSEDGQ TVIITDEDIA TLPEERSREI EVVEFVPADQ LDPMMYDKSY FLEPDSKSTK
SYVLLAKTLA ETDRVAIVHF ALRNKTRLAA LRVKDFSKRD VMVIHTLLWP DEIRDPDFPS
LDKDVDIKPA ELKMAGQVVE SMTDDFKPDQ FRDDYQEQLH ELVQAKLEGG EAFTVEEQPT
DLDETEDVSD LLAKLEASVK ARGSASADTA PAEKAPAKKA AAKKAPAKKA AAKKAPAKKA
PAKKAAAKK
//
