ID DNLI_DICTD Reviewed; 582 AA. AC B8DZX8; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 79. 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=Dtur_0780; OS Dictyoglomus turgidum (strain DSM 6724 / Z-1310). OC Bacteria; Dictyoglomota; Dictyoglomia; Dictyoglomales; Dictyoglomaceae; OC Dictyoglomus. OX NCBI_TaxID=515635; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 6724 / Z-1310; RX PubMed=28066333; DOI=10.3389/fmicb.2016.01979; RA Brumm P.J., Gowda K., Robb F.T., Mead D.A.; RT "The complete genome sequence of hyperthermophile Dictyoglomus turgidum DSM RT 6724 reveals a specialized carbohydrate fermentor."; RL Front. Microbiol. 7:1979-1979(2016). 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; CP001251; ACK42061.1; -; Genomic_DNA. DR RefSeq; WP_012583146.1; NC_011661.1. DR RefSeq; YP_002352675.1; NC_011661.1. DR AlphaFoldDB; B8DZX8; -. DR SMR; B8DZX8; -. DR STRING; 515635.Dtur_0780; -. DR EnsemblBacteria; ACK42061; ACK42061; Dtur_0780. DR KEGG; dtu:Dtur_0780; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_005138_6_0_0; -. DR InParanoid; B8DZX8; -. DR OrthoDB; 9802472at2; -. DR Proteomes; UP000007719; 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; IBA:GO_Central. 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:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0006266; P:DNA ligation; IBA:GO_Central. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central. DR CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1. DR CDD; cd07893; OBF_DNA_ligase; 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; IPR000977; DNA_ligase_ATP-dep. 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 NCBIfam; TIGR00574; dnl1; 1. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1. DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 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; PS00333; DNA_LIGASE_A2; 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..582 FT /note="Probable DNA ligase" FT /id="PRO_1000189919" FT ACT_SITE 245 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 243 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 250 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 265 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 295 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 335 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 410 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 416 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 582 AA; 66609 MW; 8F52513B1C69AED3 CRC64; MLFGELAQYF EKIEKTTKRN EMMEILADLF KRVDKEEIEK IIYLLNGRVA PDYEKIEFGM SEKLVLRAMA LALKVPIFDL EKVYKEVGDL GELIIKYSQN EGKDLTVVET FNTLFEIANL SGEGSVDAKV NRLAFLINSL TPQGGKYLVR IVLGKLRLGV GEPTVMDALS FAKVKDKSLR PFIERAFNIT SDLGYVAKVF WEGGIEALKK IKVEVGKPIR MALAERVSKV EEIVKRLGKC AIEPKFDGFR CQIHKKENNV RIFSRNLEDN THMFPDLVEA VLKQFSDKNV IIEGEAISYN PETGEFYPFQ VTVQRKRKYN ISEMVELYPL QLFAFDILYL NGEDITSLPY IRRRQKLEEA ISEGEKIFVT KNIITNDPKE IQAFFEECIT EGLEGIVAKR LDAPYQAGIR NFNWIKLKRS YQGHLADTVD CVILGYFKGR GHRAKFGIGA LLVGVYDDER DLFKTVAKIG TGPTEEEWVR FREVLDEIKL ESKPNNVESL IEPDVWVEPK YVVVIQADEI TRSPVHTCGR ELDGLGYALR FPRVIGFVRE DKGPYDATTV KEILEMFRGQ KKEKVEEDSD NL //