ID H9ZZY7_FERFK Unreviewed; 599 AA. AC H9ZZY7; DT 13-JUN-2012, integrated into UniProtKB/TrEMBL. DT 13-JUN-2012, sequence version 1. DT 27-MAR-2024, entry version 56. 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=FFONT_0304 {ECO:0000313|EMBL:AFH42294.1}; OS Fervidicoccus fontis (strain DSM 19380 / JCM 18336 / VKM B-2539 / Kam940). OC Archaea; Thermoproteota; Thermoprotei; Fervidicoccales; Fervidicoccaceae; OC Fervidicoccus. OX NCBI_TaxID=1163730 {ECO:0000313|EMBL:AFH42294.1, ECO:0000313|Proteomes:UP000007391}; RN [1] {ECO:0000313|Proteomes:UP000007391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19380 / VKM B-2539 / Kam940 RC {ECO:0000313|Proteomes:UP000007391}; RA Lebedinsky A.V., Mardanov A.V., Gumerov V.M., Beletsky A.V., Kublanov I.V., RA Perevalova A.A., Bonch-Osmolovskaya E.A., Ravin N.V., Skryabin K.G.; RT "Fervidicoccus fontis complete genome analysis confirms its distinct RT phylogenetic position and predicts its environmental function."; RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFH42294.1, ECO:0000313|Proteomes:UP000007391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19380 / VKM B-2539 / Kam940 RC {ECO:0000313|Proteomes:UP000007391}; RX PubMed=24366681; DOI=10.1007/s00792-013-0616-7; RA Lebedinsky A.V., Mardanov A.V., Kublanov I.V., Gumerov V.M., Beletsky A.V., RA Perevalova A.A., Bidzhieva S.Kh., Bonch-Osmolovskaya E.A., Skryabin K.G., RA Ravin N.V.; RT "Analysis of the complete genome of Fervidococcus fontis confirms the RT distinct phylogenetic position of the order Fervidicoccales and suggests RT its environmental function."; RL Extremophiles 18:295-309(2014). 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; CP003423; AFH42294.1; -; Genomic_DNA. DR AlphaFoldDB; H9ZZY7; -. DR STRING; 1163730.FFONT_0304; -. DR KEGG; ffo:FFONT_0304; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR InParanoid; H9ZZY7; -. DR OrthoDB; 31274at2157; -. DR Proteomes; UP000007391; 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:UP000007391}. FT DOMAIN 340..475 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT ACT_SITE 262 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 260 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 267 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 282 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 312 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 352 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 429 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" SQ SEQUENCE 599 AA; 67836 MW; 573DF58B5B061B2C CRC64; MDFEIIARTF DALEKISSRI ALTNALVDLF KQTSKDEVKI VVYLIQGRLW PDWKGMPEIG VAEKLLIKAA SIALNVKEEQ INKIYKEVGD LGKAIEQIKA SKDATAGTLT SFLGVQKKEK LSVKKIYESF VKIATAEGEG SRDIKLRVLA GLLKDAQPIE ARFIVRFVEG RLRINIGDAT VMDALSIAFT GTDANRPIIE RAYNLRADLG DIAEILVKDG INALQNITPK VGIPIRPMLA ERHNDPKVML EKVGGKAYVE YKYDGERAQI HKSNDEITIF SRRLENITHQ YPDVVEYSRK YIKANEAIVE GEIVAIDPDT RELRPFQILM TRKRKHDITK MMKEVPVSVF LFDAIYVDGK DLTNFPLPER RKYLESVIAQ SDDMQIAQYK YIDNAEDLEK MFYEAISNGA EGVMIKSISE KSIYQAGNRG WLWIKYKRDY RSEMSDSVDL VVVGAFYGKG KRAGKLSTIL VAGYDPDADV FRTVCKVGTG FTDEELDKMT EEFKGYIIDH KDPRVISEIT PDVWLIPKKV VEVIGAELTL SPLHTCAKGE ISKEAGLSIR FPRFINWRPD KGPEDATTCK ELVEMYRMQL KQVEEEQNP //