ID E8TEF1_MESCW Unreviewed; 336 AA. AC E8TEF1; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 64. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN OrderedLocusNames=Mesci_5469 {ECO:0000313|EMBL:ADV14566.1}; OS Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 / OS WSM1271). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Phyllobacteriaceae; Mesorhizobium. OX NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV14566.1, ECO:0000313|Proteomes:UP000007471}; RN [1] {ECO:0000313|Proteomes:UP000007471} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAMBI 2942 / LMG 23838 / WSM1271 RC {ECO:0000313|Proteomes:UP000007471}; RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., RA Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G., RA Tiwari R.P., Woyke T.; RT "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae RT WSM1271."; RL Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases. 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 -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000256|ARBA:ARBA00007572}. 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; CP002447; ADV14566.1; -; Genomic_DNA. DR RefSeq; WP_013533217.1; NC_014923.1. DR RefSeq; YP_004144616.1; NC_014923.1. DR AlphaFoldDB; E8TEF1; -. DR STRING; 765698.Mesci_5469; -. DR KEGG; mci:Mesci_5469; -. DR PATRIC; fig|765698.3.peg.6005; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_008325_4_1_5; -. DR OrthoDB; 9770771at2; -. DR Proteomes; UP000007471; 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; cd07905; Adenylation_DNA_ligase_LigC; 1. DR CDD; cd07970; OBF_DNA_ligase_LigC; 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; IPR044119; Adenylation_LigC-like. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR044117; OBF_LigC-like. 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 SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:ADV14566.1}. FT DOMAIN 27..207 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|Pfam:PF01068" FT DOMAIN 226..325 FT /note="DNA ligase ATP-dependent C-terminal" FT /evidence="ECO:0000259|Pfam:PF04679" FT REGION 268..289 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 336 AA; 37654 MW; BF7104515EC8D7F2 CRC64; MHEPTNAFPL PLDTSPMEAR LADAIPRDGN RWQYEPKWDG FRCLAFKSDD TVDLRAKSGK PLGRYFPEIT EILRDLKRGH FVIDGEIVIE VDGELSFEAL QMRLHPAQSR IRKLSSQTPA SLILFDMLAR PGGEVITGKP LVERRRAIED FVTSSNSPDL RLSKCTYDAA TAARWLNGAG HASTDGIVAK VLDEHYLCGE RAMVKVKPRR TADCVVGGFR YLAGSREVGS LLLGLYNDDG KLDHVGFTST IARTDRGALT RRLEGLRSEP GFTGKAPGGP SRWSTERSGQ WEPLEPELVV EVRFDHVTGN RFRHGTKLLR WRPDKAPRQC TFEQIE //