ID DNLI1_METBF Reviewed; 549 AA. AC Q46C04; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 27-MAR-2024, entry version 124. DE RecName: Full=DNA ligase 1 {ECO:0000255|HAMAP-Rule:MF_00407}; DE EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407}; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] 1 {ECO:0000255|HAMAP-Rule:MF_00407}; GN Name=lig1 {ECO:0000255|HAMAP-Rule:MF_00407}; GN OrderedLocusNames=Mbar_A1643; OS Methanosarcina barkeri (strain Fusaro / DSM 804). OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia; OC Methanosarcinales; Methanosarcinaceae; Methanosarcina. OX NCBI_TaxID=269797; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Fusaro / DSM 804; RX PubMed=16980466; DOI=10.1128/jb.00810-06; RA Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S., RA Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.; RT "The Methanosarcina barkeri genome: comparative analysis with RT Methanosarcina acetivorans and Methanosarcina mazei reveals extensive RT rearrangement within methanosarcinal genomes."; RL J. Bacteriol. 188:7922-7931(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 --------------------------------------------------------------------------- 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; CP000099; AAZ70588.1; -; Genomic_DNA. DR AlphaFoldDB; Q46C04; -. DR SMR; Q46C04; -. DR STRING; 269797.Mbar_A1643; -. DR PaxDb; 269797-Mbar_A1643; -. DR KEGG; mba:Mbar_A1643; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR OrthoDB; 31274at2157; -. 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; 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..549 FT /note="DNA ligase 1" FT /id="PRO_0000365258" FT ACT_SITE 214 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 212 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 219 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 234 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 264 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 310 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 387 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 393 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 549 AA; 61905 MW; AFEDB817138AF856 CRC64; MERKEIKDSA YLFLGSIGPA FENITLGIGD KLALKAIAGA YRVSEEEVKK RYSRTGDLGD VAFELNQGEE KSLAIDEVFG SLKEIKEASG KGSQEEKTGL LSSILQRASP KEGKYIVRIV LGKLRLGFGD QFLLEAFSIA FTGDKKYVVK IKESYSVCTD IGELAESLAE QGPKALGHFS IKLGRPVRSM LAQRVKTFEE LEERIPGKKA AEEKYDGERV QIHKNGEEIK AFSRRLEDIT AQYPDVIEAV RKGILAKKIV LDGEIIAYVE GGKANDSTGE FYSFQRLMKR RRKYEVQKYT EICPVAVFFF DILYLEGNSL LKKPYPERRA ILEEHVKESE ILHLARRIVT DNLEEIEDFF NEALEKRLEG IIIKSMGRNS AYEAGKRSWF WLKWKEEYAS GMRETFDLAI IGKYYGRGKR KGSFGALLCA ILNGEEQRFE TFTKVGTGFT EADAKEIDSL LSEHIISEVP KNVLIKSRML PDIFVEPSLV IEVLGSEITE SPSHTAGQGE GDTGLALRFP RFLRIRHDKG PYDITTLTEV RNLKEGKSI //