ID G0EDM6_PYRF1 Unreviewed; 609 AA. AC G0EDM6; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 62. 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=lig {ECO:0000256|HAMAP-Rule:MF_00407}; GN OrderedLocusNames=Pyrfu_1977 {ECO:0000313|EMBL:AEM39830.1}; OS Pyrolobus fumarii (strain DSM 11204 / 1A). OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae; OC Pyrolobus. OX NCBI_TaxID=694429 {ECO:0000313|EMBL:AEM39830.1, ECO:0000313|Proteomes:UP000001037}; RN [1] {ECO:0000313|EMBL:AEM39830.1, ECO:0000313|Proteomes:UP000001037} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 11204 / 1A {ECO:0000313|Proteomes:UP000001037}; RX PubMed=21886865; RA Anderson I., Goker M., Nolan M., Lucas S., Hammon N., Deshpande S., RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Huntemann M., RA Liolios K., Ivanova N., Pagani I., Mavromatis K., Ovchinikova G., Pati A., RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Huber H., RA Yasawong M., Rohde M., Spring S., Abt B., Sikorski J., Wirth R., RA Detter J.C., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., RA Kyrpides N.C., Klenk H.P., Lapidus A.; RT "Complete genome sequence of the hyperthermophilic chemolithoautotroph RT Pyrolobus fumarii type strain (1A)."; RL Stand. Genomic Sci. 4:381-392(2011). 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|ARBA:ARBA00007572, ECO:0000256|HAMAP-Rule:MF_00407, CC ECO:0000256|RuleBase:RU004196}. 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; CP002838; AEM39830.1; -; Genomic_DNA. DR RefSeq; WP_014027507.1; NC_015931.1. DR AlphaFoldDB; G0EDM6; -. DR STRING; 694429.Pyrfu_1977; -. DR GeneID; 11138318; -. DR KEGG; pfm:Pyrfu_1977; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR InParanoid; G0EDM6; -. DR OrthoDB; 31274at2157; -. DR Proteomes; UP000001037; 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; cd07969; OBF_DNA_ligase_I; 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; 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:UP000001037}. FT DOMAIN 346..481 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT ACT_SITE 268 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 266 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 273 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 288 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 318 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 358 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 435 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 441 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" SQ SEQUENCE 609 AA; 68833 MW; F71A9C6F3BA53E90 CRC64; MPMPFSILAE TFEKLERTTS RTQMVLYLVD LFKKTPPETI DKVVYFLQGK LWPDWKGLPE LGVGEKTLIK AVSIALHVPE RTVEELAKRL GDLGLAVERL KREKEKGAKA VGLLAFMKQP SSGESTLTVE KVYDTLARVA LTTGEGSREL KLKLVAGLIA EASPREAKYI VRFIEGRLRL GVGDATIIEA LSIVYAGSAA MKHVVERAYN LRADLGLVAK ILATQGVEAV KNIKPEVGIP IRPMLAERLN NPVEILKKLG GRALVEYKYD GERAQIHKKG DKIWIFSRRL ENITKMYPDV VEMALKGIKA NEAIVEGEIV AIDPDTGELR PFQELMRRKR KHDIHIAMKE VPVAVYLFDI LYRDGEDLTV KPLPERRKHL EEVLVQSDTW RLAEHIYTDK PEELEQFFLR AIEDGAEGVM AKAVHSRSIY QAGARGWLWI KYKRDYKSEM IDTVDLVVVG AFYGKGRRGG KFGALLMAAY DPDTDTFKTV CKVGSGFTDE DLERLNEMLK PYIIPHKHPR VDSKMKPDVW VQPALVAEII GAELTLSPIH TCCHGWVKPG AGISIRFPRF IRWRPDKSPE DATTTKELYE MYKRQLHKIE EKTATREAA //