ID DNLI_PERMH Reviewed; 582 AA. AC C0QSL7; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 1. DT 27-MAR-2024, entry version 82. DE RecName: Full=Probable DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407}; DE EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407}; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407}; GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407}; GN OrderedLocusNames=PERMA_1901; OS Persephonella marina (strain DSM 14350 / EX-H1). OC Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae; OC Persephonella. OX NCBI_TaxID=123214; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14350 / EX-H1; RX PubMed=19136599; DOI=10.1128/jb.01645-08; RA Reysenbach A.-L., Hamamura N., Podar M., Griffiths E., Ferreira S., RA Hochstein R., Heidelberg J., Johnson J., Mead D., Pohorille A., RA Sarmiento M., Schweighofer K., Seshadri R., Voytek M.A.; RT "Complete and draft genome sequences of six members of the Aquificales."; RL J. Bacteriol. 191:1992-1993(2009). CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA during DNA CC replication, DNA recombination and DNA repair. {ECO:0000255|HAMAP- CC Rule:MF_00407}. 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:0000255|HAMAP-Rule:MF_00407}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00407}; CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000255|HAMAP-Rule:MF_00407}. 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; CP001230; ACO03229.1; -; Genomic_DNA. DR RefSeq; WP_012675468.1; NC_012440.1. DR AlphaFoldDB; C0QSL7; -. DR SMR; C0QSL7; -. DR STRING; 123214.PERMA_1901; -. DR PaxDb; 123214-PERMA_1901; -. DR KEGG; pmx:PERMA_1901; -. DR eggNOG; COG1793; Bacteria. DR HOGENOM; CLU_005138_6_0_0; -. DR OrthoDB; 9802472at2; -. DR Proteomes; UP000001366; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-UniRule. DR CDD; cd07901; Adenylation_DNA_ligase_Arch_LigB; 1. DR CDD; cd07969; OBF_DNA_ligase_I; 1. DR Gene3D; 1.10.3260.10; DNA ligase, ATP-dependent, N-terminal domain; 1. DR Gene3D; 3.30.470.30; DNA ligase/mRNA capping enzyme; 1. DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1. DR HAMAP; MF_00407; DNA_ligase; 1. DR InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc. DR InterPro; IPR000977; DNA_ligase_ATP-dep. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR012308; DNA_ligase_ATP-dep_N. DR InterPro; IPR036599; DNA_ligase_N_sf. DR InterPro; IPR012340; NA-bd_OB-fold. DR NCBIfam; TIGR00574; dnl1; 1. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 1. DR PANTHER; PTHR45674:SF9; DNA LIGASE 3; 1. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR SUPFAM; SSF117018; ATP-dependent DNA ligase DNA-binding domain; 1. DR SUPFAM; SSF56091; DNA ligase/mRNA capping enzyme, catalytic domain; 1. DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1. DR PROSITE; PS00697; DNA_LIGASE_A1; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; DNA damage; DNA recombination; KW DNA repair; DNA replication; Ligase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1..582 FT /note="Probable DNA ligase" FT /id="PRO_1000134730" FT ACT_SITE 250 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 248 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 255 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 270 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 299 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 339 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 416 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" FT BINDING 422 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00407" SQ SEQUENCE 582 AA; 66893 MW; 86B7BDB3B593C637 CRC64; MEYTKLAQLY QILEETTSRI KMTQALVDLF KETPPELIDK VVYLSIGRIA PEYTGLDYNF SEKSAIKALS TVLNISEHDI QHQVLQTGDL GDAGKKLYEE KGVKPEGILT VEEVYRTLRE IAQTTGYGST KKKLQLFTEL LKKASPLEVK YLLRTITERL RLGIGDNTIM DALSIAFTGK KENREIIERA YNISSDLGYV ARILAEKGLD AVKNIKIEIG RPIRPMLAER MAIPSYILKK LGGKAGAEYK YDGERIQVHR KGDTFYLFSR RLENITDQFP DLIEFLKESI PEECIIELEA VVIDPSSGAI RPFQDLMNRR VKYVTRFHIM MYPIAGFIFD IMYLNGEDLT LKPYPERRKI LEENIKITER INLSERKIVD NVEDLESFFH QAIEDGCEGL VCKSLQKDSI YQAGKRGFLW IKYKRDYKSH LADTLDLVVV GAFYGKGART GYFGSLLMAC YDPETDQFKT VCKVGTGFKE DDFKKLDDLL KEHTLDHKHP RVNSILSADI WYEPFLVLEI TGAELTLSPV HTCGWDRIKI NRGLGLRFPR FTGRYRFDKR PEDATTEEEI INMYKNQIQI KS //