ID DNLJ_ANAPZ Reviewed; 677 AA. AC Q2GLI8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, 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=APH_0138; OS Anaplasma phagocytophilum (strain HZ). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Rickettsiales; Anaplasmataceae; Anaplasma; phagocytophilum group. OX NCBI_TaxID=212042; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HZ; RX PubMed=16482227; DOI=10.1371/journal.pgen.0020021; RA Dunning Hotopp J.C., Lin M., Madupu R., Crabtree J., Angiuoli S.V., RA Eisen J.A., Seshadri R., Ren Q., Wu M., Utterback T.R., Smith S., Lewis M., RA Khouri H., Zhang C., Niu H., Lin Q., Ohashi N., Zhi N., Nelson W.C., RA Brinkac L.M., Dodson R.J., Rosovitz M.J., Sundaram J.P., Daugherty S.C., RA Davidsen T., Durkin A.S., Gwinn M.L., Haft D.H., Selengut J.D., RA Sullivan S.A., Zafar N., Zhou L., Benahmed F., Forberger H., Halpin R., RA Mulligan S., Robinson J., White O., Rikihisa Y., Tettelin H.; RT "Comparative genomics of emerging human ehrlichiosis agents."; RL PLoS Genet. 2:208-222(2006). 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; CP000235; ABD43878.1; -; Genomic_DNA. DR RefSeq; WP_011450289.1; NC_007797.1. DR AlphaFoldDB; Q2GLI8; -. DR SMR; Q2GLI8; -. DR STRING; 212042.APH_0138; -. DR PaxDb; 212042-APH_0138; -. DR EnsemblBacteria; ABD43878; ABD43878; APH_0138. DR GeneID; 92747626; -. DR KEGG; aph:APH_0138; -. DR eggNOG; COG0272; Bacteria. DR HOGENOM; CLU_007764_2_1_5; -. DR Proteomes; UP000001943; 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; 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 PIRSF; PIRSF001604; LigA; 1. DR SMART; SM00292; BRCT; 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..677 FT /note="DNA ligase" FT /id="PRO_0000313114" FT DOMAIN 594..677 FT /note="BRCT" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT ACT_SITE 120 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 34..38 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 84..85 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 118 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 141 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 283 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 307 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 403 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 406 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 421 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" FT BINDING 427 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01588" SQ SEQUENCE 677 AA; 74768 MW; 413BAC9CF1B8F090 CRC64; MSDNDSRRRL ADLNAQLKLH DVLYHEHDAP EISDAQYDAL VQEKRELLEK FPELSAYNDY EGVIGALTVD ARLPKIAHRE PMLSLENSFT IQDVEKFISR VKRSLNMDPE VSITIACEPK IDGLSFAALY EKGSLIRVAT RGNGHLGEDI TNTAKVIRKL PHKIANAPEV LEVRGEIYMH HSDFEKLKDV CNFANPRNAA AGSIRQLNPK IAEERNLRYV AYCIVNSALA SQEAILKQLA EWGFCTHTEV LFADNMDDAL SFHTRMYNTR STLGYDIDGI VYKVNDTHLQ KLLGSTSKYP RWATAHKFPS TEAITKLRDI SVQVGRTGVI TPIAELEPIN IGGTLVSRAS LHNLNEIARK DIRIGDSVIV KRAGEVIPQV VGVDHTARCN SAVPEEYVFP SHCPSCGSTL SRAPGEVAMR CTAELSCQAQ VLERVKHFVS RDGLNIVGLG EKQIEFFCNA SYISNVADIF SLREKISHMN LSAEHGWGEK SIALLINAIN ASTTVKLSNF IFALGIRFIG KGAAKLIAEH YRSYSAWVRA MTSLANGEDP DNIHGIGLKS IESLRAFFSS EDNLRVLQTL EEKLNILNEI ANTETASPIS GKTIVFTGVL EDMSRNEAAK YAETLGAKVG NTVTTKTDIL VAGSNSGSKL DTARKLGIQV MNESEWKDLL KTVSNSE //