ID C5CTW0_VARPS Unreviewed; 847 AA. AC C5CTW0; DT 28-JUL-2009, integrated into UniProtKB/TrEMBL. DT 28-JUL-2009, sequence version 1. DT 27-MAR-2024, entry version 72. 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=Vapar_1660 {ECO:0000313|EMBL:ACS18310.1}; OS Variovorax paradoxus (strain S110). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Comamonadaceae; Variovorax. OX NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS18310.1}; RN [1] {ECO:0000313|EMBL:ACS18310.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=S110 {ECO:0000313|EMBL:ACS18310.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P., RA Leadbetter J.R., Spain J.C., Han J.I.; RT "Complete sequence of chromosome 1 of Variovorax paradoxus S110."; RL Submitted (JUN-2009) 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 -!- 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; CP001635; ACS18310.1; -; Genomic_DNA. DR AlphaFoldDB; C5CTW0; -. DR STRING; 543728.Vapar_1660; -. DR KEGG; vap:Vapar_1660; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_0_0_4; -. DR OrthoDB; 9802472at2; -. 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:ACS18310.1}; 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 320..466 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 194..214 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..18 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 847 AA; 93428 MW; D177C97E9F80166F CRC64; MARANPLKRY KEKRNFGATP EPAEGGASAP GVLQFVVQKH WATRLHYDFR IELDGAMKSW AVPKGPSYDT HDKRMAVHVE DHPIAYNQFE GEIPPRQYGA GKVIIWDKGS WTPIGDPRKG YRAGRLKFEL HGYKLRGKWT LVRMHGKADD KQDAWLLIKE HDEYARPAAE FSVVDQFPDS VAQMPMPAAA VSAPAEAPAA PARKRGGKAS ASGMPADAVK AAMPAKLSPL LATLVDGPPH DPQNWLYEIK FDGYRLLARI DAKGGVQLVT RNGHDWSSRM PHLVRAIERM KLAPGWLDGE IVVLNESGGT DFQALQNAFD SENTRNIVYF LFDLPYYGGF DLTGVPLVER RGLLQALLAK APPEIRFSEI FDAPPEDIVA SACKIGLEGV IGKRKNSTYA SRRSPDWIKL KCSQRQEFVI GGYTDPKGSR VGIGALLIGV HDDKGDLIYA GAVGAGFNGR TLADMLERLK PLGIDKRPFK NPTENDRRAH WVKPVLLAEV TFSEWTKDGH VRHPVFHSVR SDKPAKAIVR EKPVHPAGAG REAEAEPEPA ATMPANFKVS HADRVVDPST GITKVEVVRF YGLVAPLMMP HLKGRPVSFV RAPQGIGGQL FFQKHLELGQ MAGVRQLDAA LWPKHPELIE IAGPLGLLSA AQMNVVEFHT WNGLKTLIGK PDRMTFDLDP GEGVGWPMVL QAAELMRVVL DELGLAPFCK TSGGKGLHVV VPLKRQYDWD TIKDFSQAIV RHMARTLPQM FVAKSGPDNR VGRIFIDYLR NGFGATTICA WSVRARPGMG VSVPVEWQEV PTLTSGAQWT LRNIHARLDR GNDPWAAYAK AAKSPGAAMK LLGFRVR //