ID DNLJ_DESAH Reviewed; 685 AA. AC C0QJ86; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_01588}; DE EC=6.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01588}; DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000255|HAMAP-Rule:MF_01588}; GN Name=ligA {ECO:0000255|HAMAP-Rule:MF_01588}; GN OrderedLocusNames=HRM2_28100; OS Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 / OS HRM2) (Desulfobacterium autotrophicum). OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales; OC Desulfobacteraceae; Desulforapulum. OX NCBI_TaxID=177437; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43914 / DSM 3382 / VKM B-1955 / HRM2; RX PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x; RA Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S., RA Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A., RA Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O., RA Meyerdierks A., Gottschalk G., Amann R.; RT "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate RT reducer oxidizing organic carbon completely to carbon dioxide."; RL Environ. Microbiol. 11:1038-1055(2009). CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- CC stranded DNA using NAD as a coenzyme and as the energy source for the CC reaction. It is essential for DNA replication and repair of damaged CC DNA. {ECO:0000255|HAMAP-Rule:MF_01588}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho- CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta- CC nicotinamide D-nucleotide.; EC=6.5.1.2; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01588}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01588}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01588}; CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01588}. 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; CP001087; ACN15899.1; -; Genomic_DNA. DR RefSeq; WP_015904662.1; NC_012108.1. DR AlphaFoldDB; C0QJ86; -. DR SMR; C0QJ86; -. DR STRING; 177437.HRM2_28100; -. DR KEGG; dat:HRM2_28100; -. DR eggNOG; COG0272; Bacteria. DR HOGENOM; CLU_007764_2_1_7; -. DR OrthoDB; 9759736at2; -. DR Proteomes; UP000000442; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR CDD; cd17748; BRCT_DNA_ligase_like; 1. DR CDD; cd00114; LIGANc; 1. DR Gene3D; 6.20.10.30; -; 1. DR Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2. DR Gene3D; 3.40.50.10190; BRCT domain; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 1.10.287.610; Helix hairpin bin; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_01588; DNA_ligase_A; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR041663; DisA/LigA_HHH. DR InterPro; IPR001679; DNA_ligase. DR InterPro; IPR033136; DNA_ligase_CS. DR InterPro; IPR013839; DNAligase_adenylation. DR InterPro; IPR013840; DNAligase_N. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004150; NAD_DNA_ligase_OB. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR004149; Znf_DNAligase_C4. DR NCBIfam; TIGR00575; dnlj; 1. DR PANTHER; PTHR23389; CHROMOSOME TRANSMISSION FIDELITY FACTOR 18; 1. DR PANTHER; PTHR23389:SF9; DNA LIGASE; 1. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF01653; DNA_ligase_aden; 1. DR Pfam; PF03120; DNA_ligase_OB; 1. DR Pfam; PF03119; DNA_ligase_ZBD; 1. DR Pfam; PF12826; HHH_2; 1. DR Pfam; PF14520; HHH_5; 1. DR PIRSF; PIRSF001604; LigA; 1. DR SMART; SM00292; BRCT; 1. DR SMART; SM00278; HhH1; 2. DR SMART; SM00532; LIGANc; 1. DR SUPFAM; SSF52113; BRCT domain; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR SUPFAM; SSF47781; RuvA domain 2-like; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS01056; DNA_LIGASE_N2; 1. PE 3: Inferred from homology; KW DNA damage; DNA repair; DNA replication; Ligase; Magnesium; Manganese; KW Metal-binding; NAD; Reference proteome; Zinc. FT CHAIN 1..685 FT /note="DNA ligase" FT /id="PRO_0000380361" FT DOMAIN 606..685 FT /note="BRCT" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT ACT_SITE 121 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 39..43 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 88..89 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 119 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 142 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 182 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 302 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 326 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 420 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 423 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 438 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 443 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" SQ SEQUENCE 685 AA; 75284 MW; 3B0C000032505C3C CRC64; MIDPSSSFDR IKKEARLLRE QLHVHNINYH VKDDPVISDG EYDRMMQRLI AIETQFPELS TPDSPTRRIG AKALTAFETA EHAIPMQSLD NAFSDQDVID FHNRTAKILN TSDIRYTVEP KLDGVAVELR YEQGSLTLAL TRGDGTMGEV ITDNARTIPS VPLKLAPAGN GTIPDVLEVR GEVIINSKDF EGLNKKRLAT GEPLFANPRN AAAGSLRQLD SRVTAKRPLE IFVYGVGRAQ ELMANFDIGS HSALLESLKR LGFRINPLIR SGLSLTEVLD RFKAFETMRQ DLDYEIDGMV IKVDDIVFQE RLGTKARSPR WAIAYKFPAM EETTVINDII VQVGRTGTLT PVAILEPVNI GGVMVARASL HNQDEIQNKD IRINDTVLVK RAGDVIPKVV KPVTALRTGS ERVFVMPTHC PVCHSPVRRL DNEAAVKCIN ASCKAQLKQR LKHFVSKGGF DMEGLGTKLI DQLVDRTLVG SFADLFTLDR ETLAAMDRMG EKSATNIVQA IERSKRIPLK RFLFALGMAH TGESAAQLLS STFFTLEALL KASAEALGAI EGVGPKTADS VVAFFANPDN QETIARMMEN GVVIENHTVV ESAALDNATF FSEKRVVLTG TLGTLTRSEA KQRLEEQGAR VVSSVSKNTD ILVAGEASGS KLVKARSLGV TIMDEQTFLE HLDRG //