ID B2UGG9_RALPJ Unreviewed; 863 AA. AC B2UGG9; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 96. 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=Rpic_0501 {ECO:0000313|EMBL:ACD25656.1}; OS Ralstonia pickettii (strain 12J). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Ralstonia. OX NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD25656.1}; RN [1] {ECO:0000313|EMBL:ACD25656.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=12J {ECO:0000313|EMBL:ACD25656.1}; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C., RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.; RT "Complete sequence of chromosome1 of Ralstonia pickettii 12J."; RL Submitted (MAY-2008) 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; CP001068; ACD25656.1; -; Genomic_DNA. DR AlphaFoldDB; B2UGG9; -. DR STRING; 402626.Rpic_0501; -. DR KEGG; rpi:Rpic_0501; -. DR PATRIC; fig|402626.5.peg.1707; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_0_0_4; -. 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:ACD25656.1}; 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 319..415 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 1..31 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 189..225 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 538..560 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 863 AA; 95459 MW; 9DA970BC9A4BD386 CRC64; MPRHLADYRS KRDFTQTQEP AGARRKADEQ RDHGALHFVI QKHDATRLHY DFRLELDGTL KSWAVPKGPS LDPADKRLAV HVEDHPLDYA DFEGHIPEGQ YGGGDVIVWD RGTWRPHGDP RKAYRDGKLK FDLHGEKLHG AWALVRTHLH GTGRHPKEQW LLIKERDDQV RASSDYDVTQ ALPASVITGE NVGAKPKAKA DGRKTQRADP AQVQPPAGAV PGTLPKTLEP QLATLVDAPP RQGEWNYEVK FDGYRILARI DGNTVRLFSR NGRDWTAKLP RQARTLQALG LREAWLDGEV VVMGERGVPD FQALQNAFET AHAEHIAYYL FDIPFCNGMD LRGVPLRERR ALLERILDAA PGNLDREAVL FSGTFHAAPE DLLSSACSMS LEGVIGKRAD APYRAGRSPA WIKLKCGQRQ EFVIGGYSAP KGSRSGFGAL LLGVYDDAGK LRYAGRVGTG FNETSLHALH HELTGLTVDT PPFANPPTGS DARDVQWVKP ERVAEIAFAE WTREGIVRQA VFQGLRDDKL ARNIVREQAK PPSAAARKET RAVNAAERKV RPGAERIADV DVTHPDRVIE KASGTTKADL ARYYAGVAEW MLPHLRNRPT SLVRAPDGID GERFFQKHSA ALKLQGITQL DPSLDPGHPS LLAINSAEAL VGAVQMGTVE FHTWNALADR IEQPDRIVFD IDPDPALPFA RVIEATQLML AMLDELGLKA FLKTSGGHGM HVVVLLTRRE AAGWDTLKTF AQAVVQHMAA TFPDRFVAKM GPQNRVGKIF IDYLRNNRGA STVAAYSVRA RTGLPVSVPI RHDELEGLQS SAQWTLRTLP ERLAKLKGDP WAAYAGTRQS VTADMRKRVG ADD //