ID D5VM30_CAUST Unreviewed; 883 AA. AC D5VM30; DT 13-JUL-2010, integrated into UniProtKB/TrEMBL. DT 13-JUL-2010, sequence version 1. DT 27-MAR-2024, entry version 68. 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=Cseg_3113 {ECO:0000313|EMBL:ADG11553.1}; OS Caulobacter segnis (strain ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / OS LMG 17158 / TK0059) (Mycoplana segnis). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales; OC Caulobacteraceae; Caulobacter. OX NCBI_TaxID=509190 {ECO:0000313|EMBL:ADG11553.1, ECO:0000313|Proteomes:UP000002629}; RN [1] {ECO:0000313|Proteomes:UP000002629} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 21756 / DSM 7131 / JCM 7823 / NBRC 15250 / LMG 17158 / RC TK0059 {ECO:0000313|Proteomes:UP000002629}; RX PubMed=21705585; DOI=10.1128/JB.05453-11; RG US DOE Joint Genome Institute; RA Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.; RT "Genome sequences of eight morphologically diverse alphaproteobacteria."; RL J. Bacteriol. 193:4567-4568(2011). 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; CP002008; ADG11553.1; -; Genomic_DNA. DR RefSeq; WP_013080202.1; NC_014100.1. DR AlphaFoldDB; D5VM30; -. DR STRING; 509190.Cseg_3113; -. DR KEGG; cse:Cseg_3113; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_0_1_5; -. DR Proteomes; UP000002629; 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; cd07971; OBF_DNA_ligase_LigD; 1. DR CDD; cd04862; PaeLigD_Pol_like; 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; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014143; NHEJ_ligase_prk. DR InterPro; IPR033651; PaeLigD_Pol-like. DR NCBIfam; TIGR02777; LigD_PE_dom; 1. DR NCBIfam; TIGR02778; ligD_pol; 1. DR NCBIfam; TIGR02779; NHEJ_ligase_lig; 1. DR NCBIfam; TIGR02776; NHEJ_ligase_prk; 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, ECO:0000313|EMBL:ADG11553.1}; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 353..487 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 208..251 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 883 AA; 96272 MW; 05E11B6DB679B622 CRC64; MAARKLAAYE AKRDFEKTAE PSGAAAVAAS ERARFVIQKH AATRLHYDLR LEHEGVFLSW AVTRGPSRDP HDRRLAVHVE DHPLAYGDFE GTIPKGQYGG GTVMLWDRGW WAPEPGFDLQ KGLKKGEIKL VFAGERMKGG WVLVRINNDK FGDGKRENWL LIKHRDEFAM EGDLDFLEDT AFSIASGRTM EEIAAGKGKA PTPFMTKKAT ASDAIWNSKG SPEATAEKAA KETGAPRRRS AKPSAKAQAP RKVVKKAIAM PDFVPPQLCK LVDRPPGGGD WAHEIKFDGY RMQMRVEGGE AALRTRAGLD WSGKFPQLIK DGAALPDALI DGEVVALDAD GSPSFAGLQA ALAEESTDDL IFFAFDLLYA HGEDLTDLPL SERKARLKAL LPEDGDRIRY VEHFESGGEA VLQSACRMSL EGVVSKKLDA PYRSGKPGTW TKAKCRAGHE VVIGGWTTTG DAFRSLIVGV YRDGDLIHVG RVGTGYGRDK VARLLPKLKA AERKTSPFSG KGAPRGGANI HWVDPVLVAE IEFAGFTGDG SVRQASFKGL REDKPAQAVE AEAPAPAEDV ELAEPKAAFA MKRSDGKVSV RGVAISNPDK TLWPDAGDGT PGTKRDLAEY FEAVGDWMLE HIKGRPCSVI RMPDGVDGET FFQRHSGKGV SALIDEIVVS GDRKPYLVFN TVESLVAAAQ WGATELHPWN CRPNEQDVPG RLVFDLDPAP DVSFDAVVEG AREIRDRLEA LGLAPFCKTT GGKGLHVVTP LKPTKVDWDA AKAFAREVCA QMAADSPDLY LLNMSKKERG GKIFLDYLRN DRMSTAVAPL SPRGRPGAPV SWPVSWTQVR KGLDPKRFNI RTAPSLLKTL DAWDAYAESE RDLEAAIRKL GKD //