ID B1HPE2_LYSSC Unreviewed; 605 AA. AC B1HPE2; DT 29-APR-2008, integrated into UniProtKB/TrEMBL. DT 29-APR-2008, sequence version 1. DT 27-MAR-2024, entry version 80. 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=Bsph_3075 {ECO:0000313|EMBL:ACA40588.1}; OS Lysinibacillus sphaericus (strain C3-41). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus. OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA40588.1, ECO:0000313|Proteomes:UP000002164}; RN [1] {ECO:0000313|EMBL:ACA40588.1, ECO:0000313|Proteomes:UP000002164} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA40588.1, RC ECO:0000313|Proteomes:UP000002164}; RX PubMed=18296527; DOI=10.1128/JB.01652-07; RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M., RA Berry C., Yuan Z.; RT "Complete genome sequence of the mosquitocidal bacterium Bacillus RT sphaericus C3-41 and comparison with those of closely related Bacillus RT species."; RL J. Bacteriol. 190:2892-2902(2008). 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; CP000817; ACA40588.1; -; Genomic_DNA. DR RefSeq; WP_012294672.1; NC_010382.1. DR AlphaFoldDB; B1HPE2; -. DR EnsemblBacteria; ACA40588; ACA40588; Bsph_3075. DR KEGG; lsp:Bsph_3075; -. DR HOGENOM; CLU_008325_0_2_9; -. DR Proteomes; UP000002164; 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; cd04866; LigD_Pol_like_3; 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 InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR014146; LigD_ligase_dom. DR InterPro; IPR033652; LigD_Pol-like_3. DR InterPro; IPR014145; LigD_pol_dom. DR InterPro; IPR014143; NHEJ_ligase_prk. 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; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF21686; LigD_Prim-Pol; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 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:ACA40588.1}; 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 15..205 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|Pfam:PF01068" FT DOMAIN 336..584 FT /note="DNA ligase D polymerase" FT /evidence="ECO:0000259|Pfam:PF21686" SQ SEQUENCE 605 AA; 70532 MW; 5FFA5C63F6450C11 CRC64; MKPMLLTEAN EIPIGDDWLY ETKYDGFRCL LIWDEQPILI SRNGRNLNHS FPEIIDYCHQ IHASVKAFLP LIFDGELVYL SNPYKSEFSV VQQRGRMQNQ DVIAKHAQAF PMRLLVFDML MIKGESFSNR YLKTRKEQLA KLAAKVKLPN VDDQDGKVIQ IVQAKEESNI LWQAIKVYNG EGMVAKKKTS KWLDNTRSSH WLKIKNWRYV TVIVTQYDHS NGYFQGSIYD GGNLREVVTF KHGMKEEEHQ TLVAFFQAQG QRKKELWELE PSICVDIACI DFDGSKLREP KFHAFRLELT PDICQWQHMQ RQLFPIPETV PITHPDKPVW PEIGVTKDHY LSYLQSVSPY LLPFLQDRPL TLIRYPHGVP GESFYQKSRP DKLPDFVGTA MMDEIDYMVC NNLETLLWLG NQLALEWHIP FQTRQTMNPT EIVFDLDPPS TDHFSLAIAG ALDLKGIIDY FQLQSFVKTS GGKGLQLYIP LPANKFTYEE VRVFTEFACR FLCQQKPHLY TIERLKKNRH NKLYLDYVQH AEGKTIIAPY STRGNELGLV ATPLHWEEVN DDLKPYYFSI PAVMERMKKI SNPFKYFREV GEQQDFQAVL DRINE //