ID D3E0Q0_METRM Unreviewed; 550 AA. AC D3E0Q0; DT 23-MAR-2010, integrated into UniProtKB/TrEMBL. DT 23-MAR-2010, sequence version 1. DT 27-MAR-2024, entry version 74. DE RecName: Full=DNA ligase {ECO:0000256|ARBA:ARBA00013308, ECO:0000256|HAMAP-Rule:MF_00407}; DE EC=6.5.1.1 {ECO:0000256|HAMAP-Rule:MF_00407}; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000256|HAMAP-Rule:MF_00407}; GN Name=dnll {ECO:0000313|EMBL:ADC46296.1}; GN Synonyms=lig {ECO:0000256|HAMAP-Rule:MF_00407}; GN OrderedLocusNames=mru_0445 {ECO:0000313|EMBL:ADC46296.1}; OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 / OS OCM 146 / M1) (Methanobacterium ruminantium). OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria; OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter. OX NCBI_TaxID=634498 {ECO:0000313|EMBL:ADC46296.1, ECO:0000313|Proteomes:UP000008680}; RN [1] {ECO:0000313|EMBL:ADC46296.1, ECO:0000313|Proteomes:UP000008680} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1 RC {ECO:0000313|Proteomes:UP000008680}; RX PubMed=20126622; DOI=10.1371/journal.pone.0008926; RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J., RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C., RA Janssen P.H., Dey D., Attwood G.T.; RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium RT reveals new possibilities for controlling ruminant methane emissions."; RL PLoS ONE 5:E8926-E8926(2010). CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA CC replication, DNA recombination and DNA repair. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00407}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00407}; CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000256|HAMAP-Rule:MF_00407, ECO:0000256|RuleBase:RU004196}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; CP001719; ADC46296.1; -; Genomic_DNA. DR RefSeq; WP_012955247.1; NC_013790.1. DR AlphaFoldDB; D3E0Q0; -. DR STRING; 634498.mru_0445; -. DR GeneID; 8770085; -. DR KEGG; mru:mru_0445; -. DR PATRIC; fig|634498.28.peg.447; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR OrthoDB; 31274at2157; -. DR Proteomes; UP000008680; 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; cd07972; OBF_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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00407}; KW Cell cycle {ECO:0000256|ARBA:ARBA00023306, ECO:0000256|HAMAP- KW Rule:MF_00407}; KW Cell division {ECO:0000256|ARBA:ARBA00022618, ECO:0000256|HAMAP- KW Rule:MF_00407}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_00407}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172, ECO:0000256|HAMAP- KW Rule:MF_00407}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_00407}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_00407}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00407}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00407}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00407}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00407}; Reference proteome {ECO:0000313|Proteomes:UP000008680}. FT DOMAIN 325..455 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT ACT_SITE 248 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 246 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 253 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 268 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 298 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 414 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 420 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" SQ SEQUENCE 550 AA; 61113 MW; 5C33843B98B80B05 CRC64; MKYEELVNVY EALGATTKRL EKTEILADFL KTVELEDLQK ITLMALGRVF PPWSEEEQGI GDKLVMKAVG DAVGVSVAVV EDAIRDEGDI GAAAEKLYGK KTQMTFFSQP LTVNFVYNQL RKLAKITGNR STAKKISNIL ELLSSASALE AKYICRTILE ELRIGVGEGI IRDAISQAFG VDKALAERAH MLTNDLGLVA KVAKEEGEDG LKKLSLIPGR PVKPMLAQLS EGIEISINEM GCALCETKYD GIRMQVHKKD DEITIFTRRL ENVTMALPEA VDLIREAFPD EDFIAEGEII AIRDGKPTTF QNILQRVRRK HNIEEAMEKV PIKIYLYDLL YFKEPTIDEP IIKRREILES VVDCSNPNLA LSSLVKVGPD NIDDAVDLFN KSIEGGHEGI MIKDCDEPYI PGIRGKKMLK LKAEPETLDA VVIGGVKGIG KRGDFIGSYV IALRDENDQL QPIAHVGTGL SDDDLANLTE KMEALKITEK GTRITVHPKI VFEIAYSEIV KSPEYSAGYS LRFPVVKRIR DDKGVDDIDT IERLESMFKG //