ID J9W630_MYCIP Unreviewed; 351 AA. AC J9W630; DT 28-NOV-2012, integrated into UniProtKB/TrEMBL. DT 28-NOV-2012, sequence version 1. DT 27-MAR-2024, entry version 40. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; GN ORFNames=MIP_00682 {ECO:0000313|EMBL:AFS12464.1}; OS Mycobacterium indicus pranii (strain DSM 45239 / MTCC 9506). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=1232724 {ECO:0000313|EMBL:AFS12464.1, ECO:0000313|Proteomes:UP000007329}; RN [1] {ECO:0000313|EMBL:AFS12464.1, ECO:0000313|Proteomes:UP000007329} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MTCC 9506 {ECO:0000313|EMBL:AFS12464.1}; RX PubMed=17912347; DOI=10.1371/journal.pone.0000968; RA Ahmed N., Saini V., Raghuvanshi S., Khurana J.P., Tyagi A.K., Tyagi A.K., RA Hasnain S.E.; RT "Molecular analysis of a leprosy immunotherapeutic bacillus provides RT insights into Mycobacterium evolution."; RL PLoS ONE 2:E968-E968(2007). RN [2] {ECO:0000313|EMBL:AFS12464.1, ECO:0000313|Proteomes:UP000007329} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 45239 / MTCC 9506 {ECO:0000313|Proteomes:UP000007329}; RX PubMed=22965120; DOI=10.1093/nar/gks793; RA Saini V., Raghuvanshi S., Khurana J.P., Ahmed N., Hasnain S.E., Tyagi A.K., RA Tyagi A.K.; RT "Massive gene acquisitions in Mycobacterium indicus pranii provide a RT perspective on mycobacterial evolution."; RL Nucleic Acids Res. 40:10832-10850(2012). 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; CP002275; AFS12464.1; -; Genomic_DNA. DR AlphaFoldDB; J9W630; -. DR KEGG; mid:MIP_00682; -. DR PATRIC; fig|1232724.3.peg.487; -. DR HOGENOM; CLU_008325_4_1_11; -. DR Proteomes; UP000007329; 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. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 3: Inferred from homology; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:AFS12464.1}. FT DOMAIN 109..243 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" SQ SEQUENCE 351 AA; 39353 MW; 7EF20D9CF2022FB9 CRC64; MPPVSPMLAK SVRAIPPHAS YEPKWDGFRS ICFRDGDDVE LGSRNERPMT RYFPELVAAV RAELPERCVI DGEIVIATDH GLDFEALQQR IHPADSRVRM LAEATPASFI AFDLLALGGD DYTRRPFSER RAALVDAVGG SGRSIHVTPA TTDLGTAQRW FDEFEGAGLD GVIAKPLDVT YQPDKRVMFK IKHERTADCV VAGYRVHKSG ADAIGSLLLG LYQDDGQLAS VGVIGAFPMA ERRRLFAELQ PLVTDFADHP WNWAAHEAGE RTPRKNEYSR WNAGKDLSFV PLRPERVVEV RYDHMEGRRF RHTAQFNRWR PDRDPRSCTY EQLEQPVTFS LGEIVPGLGP G //