ID C5ADZ9_BURGB Unreviewed; 905 AA. AC C5ADZ9; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 75. 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 OrderedLocusNames=bglu_1g10900 {ECO:0000313|EMBL:ACR28259.1}; OS Burkholderia glumae (strain BGR1). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR28259.1, ECO:0000313|Proteomes:UP000002187}; RN [1] {ECO:0000313|EMBL:ACR28259.1, ECO:0000313|Proteomes:UP000002187} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR28259.1, RC ECO:0000313|Proteomes:UP000002187}; RX PubMed=19329631; DOI=10.1128/JB.00349-09; RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.; RT "Complete genome sequence of Burkholderia glumae BGR1."; RL J. Bacteriol. 191:3758-3759(2009). 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001503; ACR28259.1; -; Genomic_DNA. DR RefSeq; WP_012735147.1; NC_012724.2. DR AlphaFoldDB; C5ADZ9; -. DR STRING; 626418.bglu_1g10900; -. DR KEGG; bgl:bglu_1g10900; -. DR PATRIC; fig|626418.3.peg.3867; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_0_1_4; -. DR Proteomes; UP000002187; Chromosome 1. 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}; 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:UP000002187}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 337..429 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 1..34 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 191..228 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 568..613 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..32 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 585..599 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 905 AA; 97421 MW; DE8090E26A002EFF CRC64; MTDTLSEYQR KRRFDATPEP AGAKRRGAPA RRRDGAAAPL RFVVQVHHAR RLHYDFRLEL DGVLKSWAVP KGPSPDPADK RLAIQVEDHP LDYASFEGEI PPGHYGAGSV RIDDAGVWRP EGGVAGARRG YRDGKLTFEL DGAKLRGRWS LTRTAMPGSR GKSSWLLVRA HEDAAGSEPA DQAADQLVDQ AAARRRTRQG RPAAKPAAKR PAKPAAAQPA ASASGTATAL PGARRAALPD ALAPQLATLV AAPPEDEGWR YEMKFDGYRV LIRIAGRGGR RSVRVLTREG LDWSAKFGAQ CAAFAALPVD DAWLDAEAVV LDARGVPDFA ALQRALSDGD DAAIVCFVFD LLHLDGRALQ AVPLDARRAR LAALLAGADS GCLRFSPTLD GAPAALLEAA ARAGLEGLIG KRADGAYRAG RSRQWIKLKC RQRQEFVIGG YSAPRGSRSH FGALLLGVHA APPRSTRRGG QAARERALQY VGRVGTGFDA QQLAALAKRL AALERERAPF AVPPPSRGDA VRWVEPRLVA ECEFAGWTRD GLLRQAAFIA LREDKPTARV VRETALPTAG RTTGGSMDSN EAASAGHAAR RRRGGADEPV EAGQARPAGA ASVAGVRITH PERVVDAQGG FRKIDVVRYY ESVARWLLPQ LSGRPVSLVR YMKGIGGESF FQKHAGARGM GFVTRHPGLD PGHDALMTLD DTAALVGAAQ FDAIEFHTWN ATVDRIERPE RLVFDLDPDP ALPWERMIEA AGLVRALLEA LGLPAFCKTS GGKGLHVVVP IVRHTEWDDA KAFSQAVARH LAGQLPERFT AKMGPENRRG LIFVDYLRNG RGASTVAAYS ARARPGMGVS VPLAWEEVAA TTGGAQWTIA NLSARLDAQR ADPWDGYDAA RTRITAAMRK RLGER //