ID I3VUX2_THESW Unreviewed; 307 AA. AC I3VUX2; DT 05-SEP-2012, integrated into UniProtKB/TrEMBL. DT 05-SEP-2012, sequence version 1. DT 27-MAR-2024, entry version 45. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN OrderedLocusNames=Tsac_1306 {ECO:0000313|EMBL:AFK86317.1}; OS Thermoanaerobacterium saccharolyticum (strain DSM 8691 / JW/SL-YS485). OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales; OC Thermoanaerobacteraceae; Thermoanaerobacterium. OX NCBI_TaxID=1094508 {ECO:0000313|EMBL:AFK86317.1, ECO:0000313|Proteomes:UP000006178}; RN [1] {ECO:0000313|Proteomes:UP000006178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178}; RA Brown S.D., Land M.L., Herring C.D.; RT "Thermoanaerobacterium saccharolyticum JW/SL-YS485."; RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:AFK86317.1, ECO:0000313|Proteomes:UP000006178} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 8691 / JW/SL-YS485 {ECO:0000313|Proteomes:UP000006178}; RX PubMed=24907337; DOI=10.1128/AEM.00998-14; RA Currie D.H., Guss A.M., Herring C.D., Giannone R.J., Johnson C.M., RA Lankford P.K., Brown S.D., Hettich R.L., Lynd L.R.; RT "Profile of Secreted Hydrolases, Associated Proteins, and SlpA in RT Thermoanaerobacterium saccharolyticum during the Degradation of RT Hemicellulose."; RL Appl. Environ. Microbiol. 80:5001-5011(2014). 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; CP003184; AFK86317.1; -; Genomic_DNA. DR AlphaFoldDB; I3VUX2; -. DR STRING; 1094508.Tsac_1306; -. DR KEGG; tsh:Tsac_1306; -. DR PATRIC; fig|1094508.3.peg.1320; -. DR eggNOG; COG1793; Bacteria. DR BioCyc; TSAC1094508:GLMA-1330-MONOMER; -. DR Proteomes; UP000006178; 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; IPR012340; NA-bd_OB-fold. 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:AFK86317.1}. FT DOMAIN 114..250 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" SQ SEQUENCE 307 AA; 35506 MW; DAD5EBC1EA45C90F CRC64; MSMMDEKIPP MLAISGNVFD DPNWVYEIKW DGSRTIAFLS SSTKLQDRRL VNISHQFPEL MNINKCLKSN EAILDGELIV LKDNKPSYRN IMMRKHQQNK LRIELLSKSN PAIFITWDVI YVDGKELLNY PLIERREILS KIVSESNLIR ISDYIFGHGK TLFAETGKKQ LEGVMAKKAD SKYYLGKRSS LWQKFKHHIV LNAVILGYMI DKTALVLGLY NEEDKLVHIG NVESGISQKE LSSFLYVAND LKVGSEFYGL AINNVQWIMP FIVCKVKFME WSENFKMRAP SFLEFALDVK PTECRFM //