ID A5D2W1_PELTS Unreviewed; 324 AA. AC A5D2W1; DT 12-JUN-2007, integrated into UniProtKB/TrEMBL. DT 12-JUN-2007, sequence version 1. DT 27-MAR-2024, entry version 75. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN Name=CDC9 {ECO:0000313|EMBL:BAF59424.1}; GN OrderedLocusNames=PTH_1243 {ECO:0000313|EMBL:BAF59424.1}; OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfotomaculaceae; OC Pelotomaculum. OX NCBI_TaxID=370438 {ECO:0000313|EMBL:BAF59424.1, ECO:0000313|Proteomes:UP000006556}; RN [1] {ECO:0000313|Proteomes:UP000006556} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13744 / JCM 10971 / SI {ECO:0000313|Proteomes:UP000006556}; RX PubMed=18218977; DOI=10.1101/gr.7136508; RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.; RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated RT evolution in anaerobic microbiota."; RL Genome Res. 18:442-448(2008). 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|ARBA:ARBA00034003}; 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; AP009389; BAF59424.1; -; Genomic_DNA. DR AlphaFoldDB; A5D2W1; -. DR STRING; 370438.PTH_1243; -. DR KEGG; pth:PTH_1243; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_008325_4_0_9; -. DR Proteomes; UP000006556; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1. DR CDD; cd07971; OBF_DNA_ligase_LigD; 1. DR Gene3D; 3.30.1490.70; -; 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 InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR014146; LigD_ligase_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR NCBIfam; TIGR02779; NHEJ_ligase_lig; 1. DR PANTHER; PTHR45674:SF15; DNA LIGASE (ATP); 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 SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 4: Predicted; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:BAF59424.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000006556}. FT DOMAIN 106..238 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" SQ SEQUENCE 324 AA; 35801 MW; DE476C3589D406F5 CRC64; MSDGSLPLLR PMLAVSSRPF DSAEYIYEVK WDGYRGLCYL DGNTVIRSRN LADLTGKFPE LAGMHRKVSR KPAILDGEIV LFEKGKPSFA GLQSRGKISE LKSISRASAE RPVIFIAFDV LYCGGKSVMG LSLIERKRLL EEMVGTGEEL VLSRYICGEG RKFFEACVKE GLEGAVAKKL NSVYLPGRRS AYWLKFRHTK EADLVICGYQ YGPGGKNLGC LVLGGYHNGR LVYQGKVGTG FSSEEANALL EGLRRLEVAG ETLQVPRAEK SRTRWVRPLL VCAVEYLEAT AGGCLRHPVY RGLRRDKTPA ECPAVAIKVW LDGT //