ID Q742F5_MYCPA Unreviewed; 764 AA. AC Q742F5; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 109. DE RecName: Full=DNA ligase (ATP) {ECO:0000256|ARBA:ARBA00012727}; DE EC=6.5.1.1 {ECO:0000256|ARBA:ARBA00012727}; DE AltName: Full=NHEJ DNA polymerase {ECO:0000256|ARBA:ARBA00029943}; GN OrderedLocusNames=MAP_0880 {ECO:0000313|EMBL:AAS03197.1}; OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10) OS (Mycobacterium paratuberculosis). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium avium complex (MAC). OX NCBI_TaxID=262316 {ECO:0000313|EMBL:AAS03197.1, ECO:0000313|Proteomes:UP000000580}; RN [1] {ECO:0000313|EMBL:AAS03197.1, ECO:0000313|Proteomes:UP000000580} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-968 / K-10 {ECO:0000313|Proteomes:UP000000580}; RX PubMed=16116077; DOI=10.1073/pnas.0505662102; RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N., RA Kanjilal S., Kapur V.; RT "The complete genome sequence of Mycobacterium avium subspecies RT paratuberculosis."; RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005). 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 -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|ARBA:ARBA00001936}; 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; AE016958; AAS03197.1; -; Genomic_DNA. DR RefSeq; WP_010949008.1; NZ_CP106873.1. DR AlphaFoldDB; Q742F5; -. DR STRING; 262316.MAP_0880; -. DR KEGG; mpa:MAP_0880; -. DR PATRIC; fig|262316.17.peg.919; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_2_1_11; -. DR Proteomes; UP000000580; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR CDD; cd07906; Adenylation_DNA_ligase_LigD_LigC; 1. DR CDD; cd04863; MtLigD_Pol_like; 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; 3.90.920.10; DNA primase, PRIM domain; 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; IPR014144; LigD_PE_domain. DR InterPro; IPR014145; LigD_pol_dom. DR InterPro; IPR033649; MtLigD_Pol-like. DR InterPro; IPR012340; NA-bd_OB-fold. DR NCBIfam; TIGR02777; LigD_PE_dom; 1. DR NCBIfam; TIGR02778; ligD_pol; 1. DR NCBIfam; TIGR02779; NHEJ_ligase_lig; 1. DR PANTHER; PTHR42705; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING PROTEIN LIGD; 1. DR PANTHER; PTHR42705:SF2; MULTIFUNCTIONAL NON-HOMOLOGOUS END JOINING DNA REPAIR PROTEIN LIGD; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF13298; LigD_N; 1. DR Pfam; PF21686; LigD_Prim-Pol; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW DNA damage {ECO:0000256|ARBA:ARBA00022763}; KW DNA recombination {ECO:0000256|ARBA:ARBA00023172}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204}; KW DNA-binding {ECO:0000256|ARBA:ARBA00023125}; KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932}; KW Exonuclease {ECO:0000256|ARBA:ARBA00022839}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Ligase {ECO:0000256|ARBA:ARBA00022598}; KW Manganese {ECO:0000256|ARBA:ARBA00023211}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268}; KW Nuclease {ECO:0000256|ARBA:ARBA00022722}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}; KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695}; KW Reference proteome {ECO:0000313|Proteomes:UP000000580}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 552..671 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 744..764 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 764 AA; 85151 MW; EEF05FD0AE1E7B29 CRC64; MNAPRAWPAE PTATPRVKLT NADKVLYPAT GTTKADVFDY YTRIADVMIP HIAGRPVTRK RWPNGVDQES FFEKQLASSA PDWLPRASVT HRSGTTTYPI IDSATGLAWI AQQAALEVHV PQWRFVAEWT RSRAEELKPG PATRLVFDLD PGEGVTMAQL AEVARAVRDL IDGIGLQTFP LTSGSKGLHL YTPLTEPVSS KGATVLAKRV AQQLEKTMPK LVTSTMTKSL RAGKIFVDWS QNNGSKTTIA PYSLRGRDHP TVAAPRTWDE LDDPALRHLR YDEVLTRVAR DGDLLAELDD NQTPVPDRLT KYRSMRDASK TPEPVPDAKP AAGQGNTFVI QEHHARRLHY DFRLERDGVL VSWAVPKNLP DTPAVNHLAV HTEDHPLEYG GFEGVIPKGE YGAGRVVIWD SGTYDAEKFQ DDEVIVNLHG RKISGRYALI QTQGDQWLAH RMKDQNVFEF DTIAPMLATH GSVSALKASQ WAFEGKWDGY RLLVEADHGT LRVRSRRGRE VTGEYRELRS LAKALEEHHA VLDGEAVVLD KRGVPNFHEM QNRGKSARVE FWAFDLLYLD GRSLLRARYR DRRKLLEMLA SGGALTVPEL LPGDGDQALR QSAERGWEGV IAKRRDSTYQ PGRRSSSWIK DKHWNTQEVV IGGWKAGEGG RSSGIGSLLM GIPGPGGLHF AGRVGTGFTE RDLANLKKTL APLRTDQSPF DAPLPRSEAK GVTFVEPVLV GEVRYSEWTP DDRLRQSSWR GLRPDKEASE VVRE //