ID DNLI_ARCFU Reviewed; 555 AA. AC O29632; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 27-MAR-2024, entry version 139. 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}; OrderedLocusNames=AF_0623; OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC OS 100126 / VC-16). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; OC Archaeoglobus. OX NCBI_TaxID=224325; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16; RX PubMed=9389475; DOI=10.1038/37052; RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F., RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N., RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R., RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D., RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P., RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M., RA Smith H.O., Woese C.R., Venter J.C.; RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing RT archaeon Archaeoglobus fulgidus."; RL Nature 390:364-370(1997). 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 -!- SEQUENCE CAUTION: CC Sequence=AAB90616.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AE000782; AAB90616.1; ALT_INIT; Genomic_DNA. DR PIR; G69327; G69327. DR PDB; 3GDE; X-ray; 2.30 A; A=1-555. DR PDBsum; 3GDE; -. DR AlphaFoldDB; O29632; -. DR SMR; O29632; -. DR STRING; 224325.AF_0623; -. DR PaxDb; 224325-AF_0623; -. DR EnsemblBacteria; AAB90616; AAB90616; AF_0623. DR KEGG; afu:AF_0623; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR OrthoDB; 31274at2157; -. DR PhylomeDB; O29632; -. DR BRENDA; 6.5.1.1; 414. DR EvolutionaryTrace; O29632; -. DR Proteomes; UP000002199; 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 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell cycle; Cell division; DNA damage; KW DNA recombination; DNA repair; DNA replication; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1..555 FT /note="DNA ligase" FT /id="PRO_0000059601" FT ACT_SITE 249 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 247 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 254 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 269 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 298 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 337 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" FT BINDING 417 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT HELIX 3..13 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 19..31 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 36..46 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 63..74 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 78..88 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 91..105 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 114..126 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 132..146 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 149..159 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 169..179 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 184..194 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 197..213 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 227..230 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 234..240 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 241..249 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 251..259 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 265..268 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 275..277 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 279..288 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 291..303 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 306..308 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 310..318 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 324..329 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 332..345 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 351..361 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 366..370 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 373..377 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 379..391 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 396..400 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 411..421 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 425..434 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 439..441 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 442..451 FT /evidence="ECO:0007829|PDB:3GDE" FT TURN 453..455 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 458..464 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 470..480 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 481..483 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 484..488 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 491..494 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 499..503 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 505..509 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 511..513 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 516..521 FT /evidence="ECO:0007829|PDB:3GDE" FT STRAND 523..527 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 533..535 FT /evidence="ECO:0007829|PDB:3GDE" FT HELIX 539..547 FT /evidence="ECO:0007829|PDB:3GDE" SQ SEQUENCE 555 AA; 63553 MW; D050FE80B2341EDB CRC64; MLFAEFAEFC ERLEKISSTL ELTARIAAFL QKIEDERDLY DVVLFITGKV YPPWDERELG VGIGLLYEAL ENVSGVKRSE IESMIREYGD LGLVAEQLIK KKKMTTLAFE ELTVRKVRET FDEIASLTGE GSMKRKIMLL TGLYGLATPL EARYLTRLIL NEMRLGVGEG IMRDAIARAF RADPETVERA YMITNDLGRV AVVAKKEGEE GLRKMKIEIH IPVRMMLAQV AESLESAVRE MRTAAVEWKF DGSRVQVHWD GSRVTIYSRR LENVTNALPD IVEEIKKSVK PGVILDGEVI AVKEGKPMPF QHVLRRFRRK HDVAKMVEKI PLEAHFFDIL YHDGECIDLP LRERRKLLES AVNESEKIKL AKQIVTDSVD EVRKMYDEAI SAGHEGVMIK LPSSPYIPGK RGKNWLKVKA IMETLDLVVV GGEWGEGKRS HWLSSFELAC LDPVTGKLLK VGRVATGFTE EDLEELTEMF RPLIVSQQGK KVEFIPKYVF EVAYQEIQKS PKYESGYALR FPRFVRLRDD KDVDEADTIE RVENLYKLQF EVKRQ //