ID D3S0Y1_FERPA Unreviewed; 555 AA. AC D3S0Y1; DT 20-APR-2010, integrated into UniProtKB/TrEMBL. DT 20-APR-2010, sequence version 1. DT 27-MAR-2024, entry version 73. 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=Ferp_0025 {ECO:0000313|EMBL:ADC64217.1}; OS Ferroglobus placidus (strain DSM 10642 / AEDII12DO). OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae; OC Ferroglobus. OX NCBI_TaxID=589924 {ECO:0000313|EMBL:ADC64217.1, ECO:0000313|Proteomes:UP000002613}; RN [1] {ECO:0000313|Proteomes:UP000002613} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., RA Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R., RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D., RA Lovley D., Kyrpides N., Anderson I.J., Woyke T.; RT "Complete sequence of Ferroglobus placidus DSM 10642."; RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:ADC64217.1, ECO:0000313|Proteomes:UP000002613} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10642 / AEDII12DO {ECO:0000313|Proteomes:UP000002613}; RX PubMed=22180810; DOI=10.4056/sigs.2225018; RA Anderson I., Risso C., Holmes D., Lucas S., Copeland A., Lapidus A., RA Cheng J.F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., RA Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Woyke T., RA Lovley D., Kyrpides N., Ivanova N.; RT "Complete genome sequence of Ferroglobus placidus AEDII12DO."; RL Stand. Genomic Sci. 5:50-60(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|HAMAP-Rule:MF_00407, 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; CP001899; ADC64217.1; -; Genomic_DNA. DR RefSeq; WP_012964566.1; NC_013849.1. DR AlphaFoldDB; D3S0Y1; -. DR STRING; 589924.Ferp_0025; -. DR PaxDb; 589924-Ferp_0025; -. DR GeneID; 8777517; -. DR KEGG; fpl:Ferp_0025; -. DR eggNOG; arCOG01347; Archaea. DR HOGENOM; CLU_005138_6_0_2; -. DR OrthoDB; 31274at2157; -. DR Proteomes; UP000002613; 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 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:UP000002613}. FT DOMAIN 326..453 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT ACT_SITE 250 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 248 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 255 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 270 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 299 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 338 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 412 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" FT BINDING 418 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00407" SQ SEQUENCE 555 AA; 63726 MW; 4479C2BC547A3420 CRC64; MLTFKEFAEF CSVIEKISST LELTARIAAF IRKIEDEDDL YNVIHFLMGR IFPPWDEREI GVGVGLIYEA LRQVTGVSKS RIEQLVKETG DLGLAAERLL KEKKQTTLFQ EELTIKRVKE IFEEMAKLSG EGSQKRRVML LTDLYVSATP IETRYLTRLI LGEMRLGVGE GIIRDAIARA FGIDSSIVER AYMLTNDYGR VAVVAKKEGK DGLMRMKIQL HYPVKMMLAQ VAESVDEALR EMREAAVEWK YDGSRVQVHY GNGKVTIFSR RLENVTSALP EIVDEVKKCV RENVILDGEV IAVKDGKPMP FQQVLRRFRR KHEISKAMER IPLIVYFFDI LYDGEMLIDL PLKERRKKLE EVIGESEIIK VAQQVITSDP KVVEEEFNRA IEAGHEGLML KRLDSPYTPG KRGKLWLKLK AVMETLDLVV VGGEWGEGKR SHLLSSFELA CRDENGRLLR VGKVATGFTD EDLEELTELF KPLIEYEEGK RVVFQPKYLF EVAYQEIQKS PKYESGFALR FPRFVRLRDD KSVEEADTLE RIAKLYEMQF KSKGG //