ID DNLI_ANASK Reviewed; 513 AA. AC B4UIS1; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 23-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 89. 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=AnaeK_4290; OS Anaeromyxobacter sp. (strain K). OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae; OC Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=447217; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikiva G., RA Beliaev A.; RT "Complete sequence of Anaeromyxobacter sp. K."; RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases. 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; CP001131; ACG75493.1; -; Genomic_DNA. DR RefSeq; WP_012528245.1; NC_011145.1. DR AlphaFoldDB; B4UIS1; -. DR SMR; B4UIS1; -. DR KEGG; ank:AnaeK_4290; -. DR HOGENOM; CLU_005138_6_1_7; -. DR OrthoDB; 9767858at2; -. DR Proteomes; UP000001871; 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:0071897; P:DNA biosynthetic process; IEA:InterPro. 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; 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: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; 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. FT CHAIN 1..513 FT /note="Probable DNA ligase" FT /id="PRO_0000365218" FT ACT_SITE 215 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 213 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 220 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 235 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 304 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 376 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 382 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 513 AA; 54097 MW; 53187E6F37F04B77 CRC64; MLLAELAEVS RAVAATPARL EKVALLSEAL RRLAPDERAV GASWLAGDLA GGRVGIGAAT LRAALEAAPP GAAGPGLTVG EVDAALRRIA AAAGPGSGAA RRRELDALLA RAGDPERRFL AALVLGELRQ GALEGVLSDA VARVAGLPGA EVRRAAMLAG ALPPVAEAAL AEGAAGLARF RLRVGEPVSP MLAQTAAGVD EALRALGGEA ALEWKLDGAR IQAHRDGDEV RVFSRSLREV TAAVPEVVAL LRAAPEPLLV LDGEAIALRA DGTPEPFQVT MRRFGRKLDV ERLAPDLPLT AFFFDALVAG GGELLGAPER ERWAALERAI PAERRVPRLV TGDAAEARAF LEEALARGQE GVVAKALDAP YEAGRRGAAW LKVKRAHTLD LVVLAAEWGS GRRRGWLSNL HLGARDPATG EFVMLGKTFK GMTDAMLAWQ TERLKALATG PLDAWQVPVR PELVVEVAFD GIQASPRYPG GLALRFARVK RYREDKRPED ADTIETVRGL YGG //