ID DNLI_METHJ Reviewed; 547 AA. AC Q2FTH4; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 21-MAR-2006, sequence version 1. DT 02-SEP-2026, entry version 107. 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=Mhun_2882; OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / OS JF-1). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanomicrobiales; Methanospirillaceae; Methanospirillum. OX NCBI_TaxID=323259; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1; RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8; RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H., RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M., RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.; RT "Complete genome sequence of Methanospirillum hungatei type strain JF1."; RL Stand. Genomic Sci. 11:2-2(2016). 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; CP000254; ABD42574.1; -; Genomic_DNA. DR RefSeq; WP_011449827.1; NC_007796.1. DR AlphaFoldDB; Q2FTH4; -. DR SMR; Q2FTH4; -. DR FunCoup; Q2FTH4; 138. DR STRING; 323259.Mhun_2882; -. DR EnsemblBacteria; ABD42574; ABD42574; Mhun_2882. DR GeneID; 3924177; -. DR KEGG; mhu:Mhun_2882; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR InParanoid; Q2FTH4; -. DR OrthoDB; 31274at2157; -. DR Proteomes; UP000001941; 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: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:0006273; P:lagging strand elongation; IEA:TreeGrafter. DR CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1. DR CDD; cd07972; OBF_DNA_ligase_Arch_LigB; 1. DR FunFam; 1.10.3260.10:FF:000007; DNA ligase; 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; IPR050191; ATP-dep_DNA_ligase. 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; 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; Reference proteome. FT CHAIN 1..547 FT /note="DNA ligase" FT /id="PRO_0000365261" FT ACT_SITE 246 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 244 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 251 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 266 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 295 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 334 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 405 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 411 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 547 AA; 61698 MW; EEB45E15FAC1AA3F CRC64; MIFLEFAELC SRLEKISGRL ETISILAETI SSLSDDDLPH FCRLILGKPF PEWSGKKLGV GPNLLYEAVA YVTGRKREEV IDRLSRVGDA GAAVEELLSQ KSQTSFFTVE LTLADIMAAL IEISGMEGGR SQKEKVRVIQ RILSSASPLE GHYITAILLE DFRIGVGEGN LRDAIAQAFS VDPNLVEYAN QVRNDMGEVA VLARKGEEAL RSVRLVPFHP VRMMLARQGT ISGVLKEGDP VAVEFKYDGA RFQFHKQNKT CRMYSRRLEE VTNAMPDVVA LLDEALPDDI IVDGEVIAVQ GGHPMPFQTV LRRFRRKHNV AEAADAITMI PNLFDILYYN QEMLIDLPFR ERRNILTQVA SRYVTPQLVS DDETEIEAYY HTALDAGHEG VMLKLQGSRY TPGVRGKDWV KIKPEADTLD LVVTGAEWGE GKRAHVFGSF LLSVRDDDRL VPISRVATGF SDEQLIWLFD TLQDDIIRKD GKMVYFEPRL VFEIGYSEIQ KSPNYEGGYA LRFPRFIEVR EDKDLKEANT AEDVEERYIQ THSSLNT //