ID G4RCU3_PELHB Unreviewed; 820 AA. AC G4RCU3; DT 14-DEC-2011, integrated into UniProtKB/TrEMBL. DT 14-DEC-2011, sequence version 1. DT 02-SEP-2026, entry version 67. 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=KKY_1733 {ECO:0000313|EMBL:AEQ51748.1}; OS Pelagibacterium halotolerans (strain DSM 22347 / JCM 15775 / CGMCC 1.7692 / OS B2). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Devosiaceae; Pelagibacterium. OX NCBI_TaxID=1082931 {ECO:0000313|EMBL:AEQ51748.1, ECO:0000313|Proteomes:UP000008850}; RN [1] {ECO:0000313|EMBL:AEQ51748.1, ECO:0000313|Proteomes:UP000008850} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 22347 / JCM 15775 / CGMCC 1.7692 / B2 RC {ECO:0000313|Proteomes:UP000008850}; RX PubMed=22156395; DOI=10.1128/JB.06343-11; RA Huo Y.Y., Cheng H., Han X.F., Jiang X.W., Sun C., Zhang X.Q., Zhu X.F., RA Liu Y.F., Li P.F., Ni P.X., Wu M.; RT "Complete genome sequence of Pelagibacterium halotolerans B2T."; RL J. Bacteriol. 194:197-198(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 -!- 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; CP003075; AEQ51748.1; -; Genomic_DNA. DR RefSeq; WP_014130897.1; NC_016078.1. DR AlphaFoldDB; G4RCU3; -. DR STRING; 1082931.KKY_1733; -. DR KEGG; phl:KKY_1733; -. DR PATRIC; fig|1082931.4.peg.1706; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_0_2_5; -. DR Proteomes; UP000008850; 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; 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; IPR052171; NHEJ_LigD. 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; BIFUNCTIONAL NON-HOMOLOGOUS END JOINING 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:AEQ51748.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000008850}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 307..391 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 183..204 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 186..195 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 820 AA; 90064 MW; 42AE66A94579F814 CRC64; MARARDLLKE YRAKRDFTKT SEPQGGKGAS SGNVFVVQKH DATRLHYDFR LEYEGVLKSW AVTRGPSTDP ADKRLAVRTE DHPLDYATFE GKIPQGEYGG GTVMLWDFGT WEPVEDANKG FKSGKLKIRL KGDRMKGDWA LIRMKPKSGE KRENWLLIKE HDDFATEGGS KLLDKSTSVS TGRKMSAIEK GEPPVRKSKT GGRSLPKFVE PQLATLVDSV PGGNDWLFEM KYDGYRCIAV ISGEDVRLYT RNGLDWTDTF ASLVAPMSLL TESSMLLDGE ICAFDENGKT SFSTLKSHLS EGGPLVYFAF DLLEIDGKSL RAKPLSERKA ALENVLGRRT RHDPVQFSPD ISGKGTEVFS AICKAGHEGI IAKHGAAPYR SGRGKSWLKV KCTLRQEFVI VGWSPSEKRR GVFASLLLAT QQDGKLVYRG RVGTGFPDDL RADLQAMLDK DARKTAPLTG VPRQMARGAR WVSPRHLAEI AYTELTPDGI LRHPSFLGLR EDKPAKGIGL EQPGKAEGGH TLSLTEDTGI AAAEKAGIKL SSPDKVLYPG QGVTKGKLAA YYASVAEAMM PYIANRPLSL VRCPAGRAKQ CFFQKHDTGG FAQGMDTVQI TEKDGKSDSY FTLDGLEGLL AGVQMGVLEF HIWGSRRDAI EKPDRIVFDI DPDEGLVFGD VKSAALDIRG RLADLGLETF AMVTGGKGIH VIAPIARRAE WPAVKAFAAG FAKQMAEDEP ERFTATLSKK ARKGKLFIDY LRNERGSTAI APYSTRAREG APVAVPVDWN EVERLNAANR FSLEAAVERA RDNAWPGYGK LRQSLPKSTK //