ID DNLI1_HALWD Reviewed; 618 AA. AC Q18HT7; DT 03-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 1. DT 02-SEP-2026, entry version 117. 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=HQ_2327A; OS Haloquadratum walsbyi (strain DSM 16790 / HBSQ001). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Halobacteria; Halobacteriales; Haloferacaceae; Haloquadratum. OX NCBI_TaxID=362976; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 16790 / HBSQ001; RX PubMed=16820047; DOI=10.1186/1471-2164-7-169; RA Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F., RA Pfeiffer F., Oesterhelt D.; RT "The genome of the square archaeon Haloquadratum walsbyi: life at the RT limits of water activity."; RL BMC Genomics 7:169-169(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; AM180088; CAJ52448.1; -; Genomic_DNA. DR RefSeq; WP_011571574.1; NC_008212.1. DR AlphaFoldDB; Q18HT7; -. DR SMR; Q18HT7; -. DR STRING; 362976.HQ_2327A; -. DR GeneID; 4194189; -. DR KEGG; hwa:HQ_2327A; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR Proteomes; UP000001975; 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 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; 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; Reference proteome. FT CHAIN 1..618 FT /note="DNA ligase 1" FT /id="PRO_0000365246" FT REGION 396..422 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 274 FT /note="N6-AMP-lysine intermediate" 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 279 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 294 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 324 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 367 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 472 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 478 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 618 AA; 68163 MW; 8251D00071A1C56F CRC64; MKYSELAEVY TDVAATSATT QKETLLADCF LDVYDNTETS LLPVTVRLVR GRVFARWEAA EIGVSTAGAA DAISKATGVE SEQIETWWRE EGDLGDAAAY AVDDRVQQTL TATPLTVTRV YETLREVASY EGSGSQQKQR DEIAGLISDA SPLAARYIVR TVTGSMRLGV GEGIVRNALA SAFLDMSDDA ADAVQRAIDL TNDVAVVAQR VAEQGQPGLD DVDLELFRPI KPMLAKQAES IQTAVDELAA DPKHIERNHN IELSHSGAVL IEFKYDGIRA KIHRDGDDIR VYTRRLSDVT EQFPDVVSAA RDHIDAKHYI IEAELVGYDP QSNDDTPVTF QTLAQRIQRT DNVATIAKSI PVTTYVFDLL ALNGESLLTD TLEMRLERLN TILSTKATSD SKSASTHNAH SSTSVTTVSS DQYQSSSSLR RAQCTWATTQ TTAAEFYEDA LAAGHEGVMI KNPARPYQPG SRVGYQRKIK PTMEPLDLVV TRAKWSEGRK SDFLGRPYLA CRTADGNLAE VGRMHTGFTD DQLETFTNRV EPLIENVEGR EATLTPAVVL AVEYEEIQIS STYDSGYALR FPRLKQIRHD CDPSQADSLE RVERLYEQQS LDESQTSV //