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Database: UniProt/TrEMBL
Entry: A0A0C4YPL7_9BURK
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Original site: A0A0C4YPL7_9BURK 
ID   A0A0C4YPL7_9BURK        Unreviewed;       833 AA.
AC   A0A0C4YPL7;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727};
DE            EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727};
DE   AltName: Full=NHEJ DNA polymerase {ECO:0000256|ARBA:ARBA00029943};
GN   ORFNames=RR42_s3417 {ECO:0000313|EMBL:AJG24993.1};
OS   Cupriavidus basilensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG24993.1, ECO:0000313|Proteomes:UP000031843};
RN   [1] {ECO:0000313|EMBL:AJG24993.1, ECO:0000313|Proteomes:UP000031843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4G11 {ECO:0000313|EMBL:AJG24993.1};
RX   PubMed=25977418;
RA   Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA   Chakraborty R., Arkin A.P., Deutschbauer A.;
RT   "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT   Oak Ridge Field Research Center Site.";
RL   Genome Announc. 3:0-0(2015).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-
CC         (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP +
CC         diphosphate.; EC=6.5.1.1; Evidence={ECO:0000256|ARBA:ARBA00034003};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
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DR   EMBL; CP010537; AJG24993.1; -; Genomic_DNA.
DR   RefSeq; WP_043357378.1; NZ_CP010537.1.
DR   AlphaFoldDB; A0A0C4YPL7; -.
DR   STRING; 68895.RR42_s3417; -.
DR   KEGG; cbw:RR42_s3417; -.
DR   OrthoDB; 9802472at2; -.
DR   Proteomes; UP000031843; Chromosome secondary.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1.
DR   CDD; cd07971; OBF_DNA_ligase_LigD; 1.
DR   CDD; cd04862; PaeLigD_Pol_like; 1.
DR   Gene3D; 3.30.1490.70; -; 1.
DR   Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1.
DR   Gene3D; 3.90.920.10; DNA primase, PRIM domain; 1.
DR   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR012309; DNA_ligase_ATP-dep_C.
DR   InterPro; IPR012310; DNA_ligase_ATP-dep_cent.
DR   InterPro; IPR014146; LigD_ligase_dom.
DR   InterPro; IPR014144; LigD_PE_domain.
DR   InterPro; IPR014145; LigD_pol_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR014143; NHEJ_ligase_prk.
DR   InterPro; IPR033651; PaeLigD_Pol-like.
DR   NCBIfam; TIGR02777; LigD_PE_dom; 1.
DR   NCBIfam; TIGR02778; ligD_pol; 1.
DR   NCBIfam; TIGR02779; NHEJ_ligase_lig; 1.
DR   NCBIfam; TIGR02776; NHEJ_ligase_prk; 1.
DR   PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1.
DR   PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1.
DR   Pfam; PF04679; DNA_ligase_A_C; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF13298; LigD_N; 1.
DR   Pfam; PF21686; LigD_Prim-Pol; 1.
DR   SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   PROSITE; PS50160; DNA_LIGASE_A3; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AJG24993.1};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022722};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031843};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          316..407
FT                   /note="ATP-dependent DNA ligase family profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50160"
SQ   SEQUENCE   833 AA;  93328 MW;  521F4E820376F843 CRC64;
     MAADRIRPPL SQYEQKRDFN VTPEPASQIF SHPTPVKGLF VIQKHWAGRL HYDFRLELDG
     VLLSWAVPKG PSFDPQQKRM AIHVEDHPLD YANFEGSIPP KQYGAGVVLV WDRGTWEPVG
     DPHVGMNNGK LIFQLHGEKL AGLWEFVRIS KPEDKQDSWM LFKKPDEWAQ PLAEYDVVKA
     LPDSVIDRPL GLVEQREPKT SFANPPAAVS KIDLSLAVKA DLPAKLEPQL ATLATSLPKG
     DDWIVEMKFD GYRMMARIDK GRVRLFTRGG HDWTNKLKSL AAGVEKVGIT SAWLDGELVV
     LKDGLPDFNA LQNAIDGARN ENIVYFLFDI PYWNGQDLRK VPLTARQALL EHLIGEPTER
     IRISQHFDAP PAQVFKAASE LGLEGLMFKR QDAPYVSTRT QTWLKAKCTL RQEFVICGFL
     DRSAAPQEVG SLLLGYHVDG KLRYAGNVGT GWDAKTGRDL WTRLTALAAP SAPFDAESVK
     PGRWSKRSAG SEHWVRPLLV AEVAFAEWTP EGHVRQASFK GLRTDKPTSQ IIREVKTTAA
     VPVPSSVKVT HSERVIDPTT GLTKLDLVRY YESVAEWMLP HLKDRPLSML RAPNGITEEQ
     FFQKHPESKM PWLKEHDPAL WPGHAALLTV GSLDALVSAA QMNVVEFHTW NSVVKRLNKP
     DRVIFDLDPG EDLKWPYMQE AALLVRTLLT ELGLKAWLKT SGGKGLHVVV PLLPRLDYDA
     VKGFSQAFVQ HIARTIPQRF SATSGPANRK GKVFVDYLRN GMGQTTVAAF SARARPGLGV
     SMPVTWEQLM SLKSGAQWTV ATARDYLSFQ TADPWRDYWS TRQSLTTALK RLS
//
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