ID DNLI_METM5 Reviewed; 573 AA. AC A4FY19; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 17-APR-2007, sequence version 1. DT 27-MAR-2024, entry version 91. 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=MmarC5_0793; OS Methanococcus maripaludis (strain C5 / ATCC BAA-1333). OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanococcus. OX NCBI_TaxID=402880; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C5 / ATCC BAA-1333; 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., Chertkov O., Brettin T., Bruce D., Han C., RA Detter J.C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Mikhailova N., Sieprawska-Lupa M., Whitman W.B., Richardson P.; RT "Complete sequence of chromosome of Methanococcus maripaludis C5."; RL Submitted (MAR-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; CP000609; ABO35103.1; -; Genomic_DNA. DR RefSeq; WP_011868557.1; NC_009135.1. DR AlphaFoldDB; A4FY19; -. DR SMR; A4FY19; -. DR STRING; 402880.MmarC5_0793; -. DR GeneID; 4928716; -. DR KEGG; mmq:MmarC5_0793; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR OrthoDB; 31274at2157; -. DR Proteomes; UP000000253; 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 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_1000049870" 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; 65893 MW; BC74B0A7585AECA8 CRC64; MLFNDFCKIL DKIEKTTKRL EKTDYFVELI DFIKTNGKPE NLKQVSQITI GRVFAEFENK EIGIGPNLLL EAVKTTGISE KDLKAEIKKT GDIGTAVENL SSNIKQVSLF SQPLTLEEMY STLKKLSEIE GNSSQKKKIR IISNLLILAN PVESRYISRL ILEDMRIGMN IPTILASFSN YFNVNKENVE KIYAVTNDIG LLGEKLISGS DIENDSELHL KVFRPIKPML AQLTPSIEDA IIETKIPQFE TKYDGARVQV HKSNGEVKIY SRRLEDITNS VPELVEEIKK IDIDNIILEG ECVAMDLSSG KPRPFQDILR RFRRKYDINK MAEKIALRIY FFDVLYYNRG LIDTPLRNRR EILEKLFGTN DWDTELEKIE KEILSKKMLF SSFKLNSDDP NLAKEFFNWS LSIGHEGVMI KNPDAPYTPG SRVKTMYKVK PTLENLDVVV TRAKIGMGKR KDWYGSYEIS VKDDESNLHV IGNVGSGLTE DDLERLTKIV NEIKIEDLGE EVILEPKIVL EVTYEEIQTS EKYEMGYALR FPRVVQIRED KSINDINTLD DVKKIYDIER NRK //