ID DNLI_KINRD Reviewed; 503 AA. AC A6WG40; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Probable DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407}; DE EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407}; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407}; GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407}; GN OrderedLocusNames=Krad_4316; OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216). OC Bacteria; Actinomycetota; Actinomycetes; Kineosporiales; Kineosporiaceae; OC Kineococcus. OX NCBI_TaxID=266940; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216; RX PubMed=19057647; DOI=10.1371/journal.pone.0003878; RA Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R., RA Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.; RT "Survival in nuclear waste, extreme resistance, and potential applications RT gleaned from the genome sequence of Kineococcus radiotolerans SRS30216."; RL PLoS ONE 3:e3878-e3878(2008). CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA CC replication, DNA recombination and DNA repair. {ECO:0000255|HAMAP- CC Rule:MF_00407}. 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:0000255|HAMAP-Rule:MF_00407}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00407}; CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000255|HAMAP-Rule:MF_00407}. 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; CP000750; ABS05779.1; -; Genomic_DNA. DR RefSeq; WP_012085921.1; NC_009664.2. DR AlphaFoldDB; A6WG40; -. DR SMR; A6WG40; -. DR STRING; 266940.Krad_4316; -. DR KEGG; kra:Krad_4316; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_005138_6_1_11; -. DR OrthoDB; 3733803at2; -. DR Proteomes; UP000001116; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1. DR CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1. DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00407; DNA_ligase; 1. DR InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR012308; DNA_ligase_ATP-dep_N. DR InterPro; IPR036599; DNA_ligase_N_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1. DR PANTHER; PTHR45674:SF13; DNA LIGASE-RELATED; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS00697; DNA_LIGASE_A1; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination; KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..503 FT /note="Probable DNA ligase" FT /id="PRO_0000365220" FT ACT_SITE 214 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 219 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 234 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 263 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 296 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 368 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 374 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 503 AA; 52420 MW; E70DBA8C7C4CE942 CRC64; MLLADVVATS TAVAATRSRT AKVAAIAGLL RGLDPADAEL TAVVAAYLGG SLRQRRTGLG GRSLSGLPAP AGEASLEVAE VDRRFEEVAA LSGPGSAGRR AAAVADLFAR ATGEEQRWLR GVVAGELRQG ALDALVQDAA AAVAGVPGPD VRRAAMLAGS TVQAVVAALR GGAAELAGFG LHVGRPLLPM LAASTTSVAE AVAGFAGPVA VDTKLDGIRI QVHRGPEGVR IATRTLEDIT ARLPEVVEVV RELPARAFVL DGEALVLDGS GRPKAFQDTA SRTAQASGDA VVPYFFDVLH LDGADLLDVA LRERLAALDG FVPPRWRTPR LVTADPAAAA EFAAQALAGG HEGVVVKDLD SPYAAGRRGG AWVKVKPVHT LDLVVLAVER GSGRRAGWLS NVHLGARDPA TGGFVMLGKT FKGMTDETLA WQTARFRELQ TGEDGYVVTV RPEQVVEVAF DGLQRSTRYP GGVALRFARV VRYREDKTAA EADTLETVLA LAR //