ID DNLI_PYRIL Reviewed; 584 AA. AC A1RTK4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 06-FEB-2007, sequence version 1. DT 27-MAR-2024, entry version 93. DE RecName: Full=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=Pisl_1115; OS Pyrobaculum islandicum (strain DSM 4184 / JCM 9189 / GEO3). OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae; OC Pyrobaculum. OX NCBI_TaxID=384616; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 4184 / JCM 9189 / GEO3; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Meincke L., Brettin T., RA Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M., RA Hauser L., Kyrpides N., Mikhailova N., Lowe T., Richardson P.; RT "Complete sequence of Pyrobaculum islandicum DSM 4184."; RL Submitted (DEC-2006) 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; CP000504; ABL88286.1; -; Genomic_DNA. DR RefSeq; WP_011762861.1; NC_008701.1. DR AlphaFoldDB; A1RTK4; -. DR SMR; A1RTK4; -. DR STRING; 384616.Pisl_1115; -. DR GeneID; 4616742; -. DR KEGG; pis:Pisl_1115; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR OrthoDB; 31274at2157; -. DR Proteomes; UP000002595; 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; cd07969; OBF_DNA_ligase_I; 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:SF9; DNA LIGASE 3; 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; 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..584 FT /note="DNA ligase" FT /id="PRO_1000049877" FT ACT_SITE 251 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 249 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 256 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 271 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 301 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 341 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 416 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 422 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 584 AA; 65093 MW; D050BF645449D34A CRC64; MQFGELVKTL AAVESTTQRT TMVKLLTSLF KKARPEEIDK IIYFVLGDLR PPWEGVELGV AEKLCLRAVS KATGVSISEL EALYKKTGDV GEAARKALST AKRPGLLAFG QQKPLEVSEV YDTLLKVAQA SGEGAQDMKI SLLASLFAKA SPEEAKYIAR FVVGKLRLGV ADMTLIEALS DAFGVDKEAL ERAYHIYPDL GKLARHVAEG RPLEEIKITP GVPVLPMLAQ RLSSSSEILA KLGGSAICEY KYDGERAQIH LKEGVVKIFS RRLEDITHAY PDVVKAVREA VSAREAILEG EIVAIDPDTG DMLPFQELMH RKRKHEVAVA VEMYPVVLNL FDLLYIDGED LTNEPLIYRR VRLSEVVQET EKVSIAKWRV FDDAEEIDVF FHEAVSLGME GLVCKSPTSV YEMGARGWNW IKYKRDYKSE MIDTVDLVVV GAFYGRGKRA GLYGAFLLAA YDPATDMFYT VCKVGSGFTD ADLKKMYEML QPYKIPHRHP RVVSKMEPDV WFTPQVVIEV IGAEITLSPL HTCCLGAVKP GVGLAIRFPR FTGRYRTDKS PEQATTVSEM IELYKRQKKV AQPE //