ID F6F2G7_SPHCR Unreviewed; 835 AA. AC F6F2G7; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 02-SEP-2026, 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 ORFNames=Sphch_2999 {ECO:0000313|EMBL:AEG50629.1}; OS Sphingobium chlorophenolicum L-1. OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Sphingomonadales; Sphingobiaceae; Sphingobium. OX NCBI_TaxID=690566 {ECO:0000313|EMBL:AEG50629.1, ECO:0000313|Proteomes:UP000007150}; RN [1] {ECO:0000313|EMBL:AEG50629.1, ECO:0000313|Proteomes:UP000007150} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=L-1 {ECO:0000313|EMBL:AEG50629.1, RC ECO:0000313|Proteomes:UP000007150}; RG US DOE Joint Genome Institute; RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., RA Peters L., Daligault H., Han C., Tapia R., Land M., Hauser L., Kyrpides N., RA Ivanova N., Pagani I., Turner P., Copley S., Woyke T.; RT "Complete sequence of chromosome 2 of Sphingobium chlorophenolicum L-1."; RL Submitted (MAY-2011) 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; CP002799; AEG50629.1; -; Genomic_DNA. DR RefSeq; WP_013848861.1; NC_015594.1. DR AlphaFoldDB; F6F2G7; -. DR STRING; 690566.Sphch_2999; -. DR KEGG; sch:Sphch_2999; -. DR HOGENOM; CLU_008325_0_2_5; -. DR Proteomes; UP000007150; Chromosome 2. 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 NCBIfam; NF004628; PRK05972.1; 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:AEG50629.1}; 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:UP000007150}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 332..423 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 1..21 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 11..21 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 835 AA; 92014 MW; 3C04CB9C8FD3F46D CRC64; MAADPLAPYN AKRDFRRTRE PAGKVAKKGG NSFVVQKHAA TRLHWDFRLE IDGVLKSWAV TKGPSLDPAD KRLAVRTEDH PIDYGSFEGN IPKGEYGGGT VMLWDRGSWE PVPGKSADDL KDGHLHFILH GERMKGEWLL VRMKGRPGEK RENWLLRKID DGEAGKGDML VERALTSVLT DRSMAQIEAD AEATQSLKGS GKRAFSDKMR AAEVHNAKVR SKAGRKTGGG ALPRFVKPQL ATLVDSVPAG NDWLHEIKYD GYRMLIAVDG AKVKLFTRNG LDWTDKFGPL AESIAALDLP SALIDGEVVA LGEDGNPSFS ALQAVLKRGH GAQRADTPFH LFAFDLLFLD GMDLRPLPTI ERKERLEALL HDSQPPVHVA DHLIGAGEKL YRSLCDAGQE GIIAKRIDAP YRGDRTRNWV KVKCVRRQEF VLVGWTKSKA KGRPFSSLLL AQNEGGAMVY KGKVGTGFDA AAMEELAGAM APLAVDKAPL EVPRAEARGV QWIKPRLVAE VAFAEFTGDG RVRHGTFLGL RSDKPAKAVQ PERAEPAPLP QNGVTISNRE RIIFPEDGLT KGDLADYYAR VAPLMLPFAA NRPISLVRCP QGRAKKCFFQ KHDSGSFGDH VRQVPIREKD EGWEDYIYVE DADGLMACVQ MGTIEFHGWE SRADAVEKPD RMIFDLDPDE GMDFAKVRQA ARDIRDRLSD IGLVSFAMLS GGKGVHVVAP LTPGHDWDAH KDFASRFAQA LSAAEPDRFV ATMSKAKRKG RIFIDWLRNQ RGSTAVLPYS VRARPGAPVA VPIDWDELGG MKDAHPFGIR DAEKLLRRSR ELNGWGFAAQ GLPGL //