ID F3YU59_DESAF Unreviewed; 931 AA. AC F3YU59; DT 28-JUN-2011, integrated into UniProtKB/TrEMBL. DT 28-JUN-2011, sequence version 1. DT 27-MAR-2024, entry version 58. 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 ORFNames=Desaf_0308 {ECO:0000313|EMBL:EGJ48665.1}; OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay. OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales; OC Desulfovibrionaceae; Desulfocurvibacter. OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ48665.1, ECO:0000313|Proteomes:UP000007844}; RN [1] {ECO:0000313|EMBL:EGJ48665.1, ECO:0000313|Proteomes:UP000007844} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ48665.1, RC ECO:0000313|Proteomes:UP000007844}; RX PubMed=21642452; DOI=10.1128/JB.05223-11; RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C., RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J., RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V., RA Elias D.A.; RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio RT africanus Strain Walvis Bay."; RL J. Bacteriol. 193:4037-4038(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; CP003221; EGJ48665.1; -; Genomic_DNA. DR RefSeq; WP_014258520.1; NC_016629.1. DR AlphaFoldDB; F3YU59; -. DR STRING; 690850.Desaf_0308; -. DR KEGG; daf:Desaf_0308; -. DR eggNOG; COG1793; Bacteria. DR eggNOG; COG3285; Bacteria. DR HOGENOM; CLU_008325_0_0_7; -. DR Proteomes; UP000007844; 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:EGJ48665.1}; 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:UP000007844}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 400..537 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 188..221 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 200..217 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 931 AA; 101977 MW; A5A826C20A1691CC CRC64; MARLSEYWRK RDFSRTPEPS GRGPELESGR GFVIHKHKAR RLHYDLRLEL DGVLLSWAVP RGPSLDPGQK RLAVRVEDHP VEYGSFEGVI PQGEYGGGTV MLWDRGVWEP EGDPHEGLRQ GKLHFRLRGE KLSGGWILAH MSGKRAKEND WLLIKVRDEQ ANQRLDIETD RPESAVTGRT LAQIASSADR VWSGAGEHAS GTDSRRDVRD RERTGAEAEG VTIGTLDGDV RARIAGNVGP APPAAVEYAD TQPLPPPAQG QARPETLTIK NKTAESPRSP GLPDFAAMPG ARPGPMPEQI RPQLATLVDS PPAGEQWLHE IKFDGYRLLL IIDNSKARLM TRGGQDWTHR FPELARAAGG LTLRRAVLDG EAVVLDERGR PDFQALQNVL KGLSGGTLAM YLFDMPYAEG QDLSGCALIE RKEALRSVLG AIGQTPSPLR FSDHIVGKGK LVLENACQMG LEGIVSKRAD AHYEPRRAPT WLKSKCGHRQ EVVVAGWTDP KGQRTGFGAL LVGVHDRQGR LIYAGKVGTG YDTQVLGDLS GRLAGLATDD AAFADTHRVG SLADVHWVRP ELVAEVDFAG WTRDGIMRHP SFKGLREDKP PNEVVRENPM EPKARESMRK QHVPAKTGRA KGAIKLTHPR KVLVPYTGLT KIGLADYYRE VAGFMLPHVV GRPLSLVRCP GGLGEGCFFQ RHPAGGVPHG VQGVRVLEKG HERTWLSVSD LDGLLALVQL GVLEIHCWGA RNEDLERPDR LVFDLDPGED VEPARVTAAV LELREFLEGL GLTGFAKATG GKGFHIVLPL QRKPGWQELR EFARAVAEEL AVRKPGGFVS VAGKARRSGR IYIDWLRNAR GASSIAPYST RARPGAPVAV PLTWEELTAG FAPNSFDVQA VRSRVASLRA DPWEGFFSLR QGLSASMWRA LGRKRPAGSL I //