ID DNLJ_CLASE Reviewed; 847 AA. AC B0RGA7; DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 02-SEP-2026, entry version 111. 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=CMS1049; OS Clavibacter sepedonicus (Clavibacter michiganensis subsp. sepedonicus). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales; OC Microbacteriaceae; Clavibacter. OX NCBI_TaxID=31964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33113 / DSM 20744 / JCM 9667 / LMG 2889 / ICMP 2535 / C-1; RX PubMed=18192393; DOI=10.1128/jb.01598-07; RA Bentley S.D., Corton C., Brown S.E., Barron A., Clark L., Doggett J., RA Harris B., Ormond D., Quail M.A., May G., Francis D., Knudson D., RA Parkhill J., Ishimaru C.A.; RT "Genome of the actinomycete plant pathogen Clavibacter michiganensis subsp. RT sepedonicus suggests recent niche adaptation."; RL J. Bacteriol. 190:2150-2160(2008). 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; AM849034; CAQ01163.1; -; Genomic_DNA. DR RefSeq; WP_012298452.1; NC_010407.1. DR AlphaFoldDB; B0RGA7; -. DR SMR; B0RGA7; -. DR STRING; 31964.CMS1049; -. DR GeneID; 29472666; -. DR KEGG; cms:CMS1049; -. DR eggNOG; COG0272; Bacteria. DR HOGENOM; CLU_007764_2_1_11; -. DR OrthoDB; 9759736at2; -. DR Proteomes; UP000001318; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR CDD; cd17748; BRCT_DNA_ligase_like; 1. DR CDD; cd00114; LIGANc; 1. DR FunFam; 1.10.150.20:FF:000006; DNA ligase; 1. DR FunFam; 2.40.50.140:FF:000012; DNA ligase; 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; IPR018239; DNA_ligase_AS. DR InterPro; IPR013839; DNAligase_adenylation. DR InterPro; IPR013840; DNAligase_N. 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 NCBIfam; NF005932; PRK07956.1; 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; PF03119; DNA_ligase_ZBD; 1. DR Pfam; PF12826; HHH_2; 1. DR Pfam; PF22745; Nlig-Ia; 1. DR Pfam; PF03120; OB_DNA_ligase; 1. 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; PS01055; DNA_LIGASE_N1; 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..847 FT /note="DNA ligase" FT /id="PRO_0000340338" FT DOMAIN 686..775 FT /note="BRCT" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT REGION 1..23 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 770..847 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..22 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 786..807 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 819..833 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 137 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 54..58 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 104..105 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 135 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 158 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 195 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 350 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 444 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 447 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 463 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 469 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" SQ SEQUENCE 847 AA; 89734 MW; 3411938F726FDEDC CRC64; MSDTTTGSDA ADAAVPATTP ADLEAASARV DELRAEIERH RDAYYGETGG TVSDAEYDAL ERELRAIEDA HPTLRSQDSP TQTVGGRAET TLFAPVTHAE RMLSLDNVFS EEELAEWAAK VERDAGRGRV RYLSELKIDG LAINLRYEHG VLVTAATRGD GVVGEDVTQN VLTMGTVPER LAGSGHPPLV EVRGEIFFPV AEFDELNARQ LEVGERVFAN PRNAAAGSLR QKEEGKSPAR LELMHARIRR LRMLVHGIGA WPVRELERDA HVSAQSEVYG LLEAWGLPIS THFRVFDDIA EVAGFVRRQG ADRAAVEHQI DGIVVKVDDL GLHEELGATS RAPRWATAYK YPPEEVNTTL LDIVVSVGRT GRATPFAVME KVEVAGSEVR QATLHNQQVV KAKGVLIGDT VVLRKAGDVI PEVLGPVVEL RTGKEHEFVM PTLCPECQTP LKPAKEGDID LRCPNARSCP AQVRGRVEHV ASRGALDIEG LGEVAAAALT QPLEPEDPPL ETEAGLFELT MADLVPITVV VRDAETGMVK VDEKTGEAKR VTPFRRKRVL KRDGAFDPAE PWGDEASVPS KSAEVLLENL EKAKTQDLWR ILVALSIRHV GPVAARALAG WFGSLDVIRA ASREELAAVD GVGGIIADAL LDWFEVDWHR EIVARWEKAG VVTAVPGHPG PGAAAAAGGV LAGLAVVATG SLEGYTREGA LEAIMAAGGK AGSSVSKKTH YVAAGPGAGS KLGKAEALGV RIIDAAEFRL LVEQGPDAIA LPEADPVPDA AETAPDGGSA EDATAATAGA AEAATAEAKP KRARKRKAPA AAAAAPPTDV EAGTAVHAEP DGPAETP //