ID DNLI_ANAD2 Reviewed; 513 AA. AC B8JBM1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 1. DT 07-APR-2021, entry version 73. 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}; OrderedLocusNames=A2cp1_4312; OS Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258). OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales; OC Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter. OX NCBI_TaxID=455488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=2CP-1 / ATCC BAA-258; 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., Ovchinnikova G., RA Beliaev A.S., Richardson P.; RT "Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."; RL Submitted (JAN-2009) 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; CC Evidence={ECO:0000255|HAMAP-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; CP001359; ACL67629.1; -; Genomic_DNA. DR RefSeq; WP_015935329.1; NC_011891.1. DR SMR; B8JBM1; -. DR EnsemblBacteria; ACL67629; ACL67629; A2cp1_4312. DR KEGG; acp:A2cp1_4312; -. DR HOGENOM; CLU_005138_6_1_7; -. DR OMA; WLFEESY; -. DR BioCyc; ADEH455488:G1GUO-4359-MONOMER; -. DR Proteomes; UP000007089; 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 Gene3D; 1.10.3260.10; -; 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 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; SSF117018; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00574; dnl1; 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_1000134725" FT ACT_SITE 215 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 213 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 220 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 235 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 264 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 304 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 376 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 382 FT /note="ATP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 513 AA; 54060 MW; A4CCC38389CAB126 CRC64; MLLAELAEVS RAVAATPARL EKIARLAEAL RRLAPDERAV GASWLAGDLP GGRIGIGGAT VRAALDAAPA EGGGPGLTVA EVDAALGRIA TASGAGSAGA RRRELDALLA RAGAPERWFL AALLLGELRQ GALEGVLADA VARAAGLPAA EVRRAAMLAG ALPPVAVAAL SEGAAGLARF RLRVGEPVSP MLAQTAADVE EALRALGGEA ALEWKLDGAR IQAHRDGGEV RVFSRSLRDV TAAVPEVVAL LRAAPEPRLV LDGEAIALRA DGTPEPFQVT MRRFGRRLDV ERLAPDLPLT AFFFDALVAG GAELLASPER VRWAALERAV PAEQRVPRLV TRDPAEAGAF LEDALARGQE GVVAKALDAP YEAGRRGAAW LKVKRAHTLD LVVLAAEWGS GRRRGWLSNL HLGARDPSTG GFVMLGKTFK GMTDAMLAWQ TERLKALATG PLDAWQVPVR PELVVEVAFD GIQSSPRYPG GLALRFARVK RYREDKRPED ADTIETVRGL YGG //