ID DNLI_CENSY Reviewed; 589 AA. AC A0RWD6; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 2. DT 27-MAR-2024, entry version 79. 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=CENSYa_1021; OS Cenarchaeum symbiosum (strain A). OC Archaea; Nitrososphaerota; Cenarchaeales; Cenarchaeaceae; Cenarchaeum. OX NCBI_TaxID=414004; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=A; RX PubMed=17114289; DOI=10.1073/pnas.0608549103; RA Hallam S.J., Konstantinidis K.T., Putnam N., Schleper C., Watanabe Y., RA Sugahara J., Preston C., de la Torre J., Richardson P.M., DeLong E.F.; RT "Genomic analysis of the uncultivated marine crenarchaeote Cenarchaeum RT symbiosum."; RL Proc. Natl. Acad. Sci. U.S.A. 103:18296-18301(2006). 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 -!- SEQUENCE CAUTION: CC Sequence=ABK77653.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; DP000238; ABK77653.1; ALT_INIT; Genomic_DNA. DR AlphaFoldDB; A0RWD6; -. DR SMR; A0RWD6; -. DR STRING; 414004.CENSYa_1021; -. DR EnsemblBacteria; ABK77653; ABK77653; CENSYa_1021. DR KEGG; csy:CENSYa_1021; -. DR PATRIC; fig|414004.10.peg.943; -. DR HOGENOM; CLU_005138_6_0_2; -. DR Proteomes; UP000000758; 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; Reference proteome. FT CHAIN 1..589 FT /note="DNA ligase" FT /id="PRO_0000365244" FT ACT_SITE 252 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 250 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 257 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 272 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 302 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 342 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 417 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 423 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 589 AA; 65183 MW; 862D43048CA15D39 CRC64; MQFSVLAGSL EKMESTAKRL ELTGILEELL RETPHEVIAQ IVYLIQGKLR PEFEGIELGV AEKLAVRAVS KSSGMPAARI EAAYRRDGDL GRAASSILEQ KTQTTFLAEE ITVERVYDTL MRIARLEGAR SQDMKMRHIS SLLNDASPRD ACYILKLILG TLRLGIAENT VMDALAAAFT GSKSNRPELE RAYNVSSDLG RVAEAVSSGG LEAVRGFAVA VFSPIRPMLA DRVRSESEAL EKMGAGLAAE YKLDGERVQV HLSGGRVELF SRSLENITAY YPDIVERIPG RLRAREAVLE AEAVAVNEET GEFLPFQELM HRRRKYDIDK AVMRYPITVN FFDILYLDGR DCLGISYSER RALLEGVVDE DSFARCVPVS TIPDESALED SLENSINAGC EGLMLKLPDA PYRAGSRGGY WLKLKREYRN ELGDSLDLVI IGAFFGKGRR TGRYGTLLLA TYDDSRDTFP SICKVGTGFT DEDLDQLYQL LSPRVTLKRN PRIDSGMEAD VWFDPEVVME VVASEITLSP VHKTALDSVR KGAGLALRFP KFTGKLRTEK TAEDASTDQE VIALYKSQKK VVPDGQPGV //