ID DNLI_METM6 Reviewed; 573 AA. AC A9AAX4; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 15-JAN-2008, sequence version 1. DT 27-MAR-2024, entry version 92. 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=MmarC6_1685; OS Methanococcus maripaludis (strain C6 / ATCC BAA-1332). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=444158; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C6 / ATCC BAA-1332; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Sieprawska-Lupa M., Whitman W.B., RA Richardson P.; RT "Complete sequence of Methanococcus maripaludis C6."; RL Submitted (OCT-2007) 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; CP000867; ABX02497.1; -; Genomic_DNA. DR AlphaFoldDB; A9AAX4; -. DR SMR; A9AAX4; -. DR STRING; 444158.MmarC6_1685; -. DR KEGG; mmx:MmarC6_1685; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR OrthoDB; 31274at2157; -. DR PhylomeDB; A9AAX4; -. 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 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:SF7; DNA LIGASE; 1. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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..573 FT /note="DNA ligase" FT /id="PRO_0000365252" 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 301 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 432 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 438 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 573 AA; 65774 MW; E25F2EC289F2571D CRC64; MLFIDFCKIL DKIEKTTKRL EKTDYFVELI DFIKNNGKAE NLKQVSQITI GRVFAEFENK EIGIGPNLLI EAVKTTGISE KDLKAEIKKT GDIGIAVENL SSNIKQVSLF SQPLTLEEIY STLKKLSEIE GNSSQKKKTR IISNLLILSN PVESRYISRL ILEDMRIGMN IPTILASFSN YFNVNKEAVE KIYAVTNDIG LIGKKLISGS DIENDSELKL KVFRPIKPML AQLTPSIEDA IIETKMPQFE TKYDGARVQV HKSNGKVNIY SRRLENITNS VPELVEEINK IDIDNIILEG ECVAMDLSSG KPRPFQDILR RFRRKYDIDK VAEKIALRIY FFDVLYYEKG LIDTPLKNRR EILEKLFGTN NWDSELEKIQ KEIFSNKMLF SSFKLNSDDP DLAKEFFNWS LSIGHEGIMI KNPDAPYTPG SRVKTMYKVK PTLENLDVVV TRAKIGMGKR KDWYGSYEIS VKDDEDNLHV IGNVGSGLTE DDLERLTTIV NEIKIEDLGE EVILEPKIVL EVTYEEIQTS EKYEMGYALR FPRVVQIRED KSINDINTLD DVKKIYEIER NRK //