ID B8FUY8_DESHD Unreviewed; 818 AA. AC B8FUY8; DT 03-MAR-2009, integrated into UniProtKB/TrEMBL. DT 03-MAR-2009, sequence version 1. DT 27-MAR-2024, entry version 76. 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=Dhaf_0568 {ECO:0000313|EMBL:ACL18634.1}; OS Desulfitobacterium hafniense (strain DSM 10664 / DCB-2). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae; OC Desulfitobacterium. OX NCBI_TaxID=272564 {ECO:0000313|EMBL:ACL18634.1, ECO:0000313|Proteomes:UP000007726}; RN [1] {ECO:0000313|EMBL:ACL18634.1, ECO:0000313|Proteomes:UP000007726} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 10664 / DCB-2 {ECO:0000313|Proteomes:UP000007726}; RX PubMed=22316246; DOI=10.1186/1471-2180-12-21; RA Kim S.H., Harzman C., Davis J.K., Hutcheson R., Broderick J.B., Marsh T.L., RA Tiedje J.M.; RT "Genome sequence of Desulfitobacterium hafniense DCB-2, a Gram-positive RT anaerobe capable of dehalogenation and metal reduction."; RL BMC Microbiol. 12:21-21(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; CP001336; ACL18634.1; -; Genomic_DNA. DR RefSeq; WP_015942845.1; NC_011830.1. DR AlphaFoldDB; B8FUY8; -. DR KEGG; dhd:Dhaf_0568; -. DR HOGENOM; CLU_008325_0_0_9; -. DR Proteomes; UP000007726; 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:ACL18634.1}; 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 293..426 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 REGION 497..520 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..17 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..519 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 818 AA; 93510 MW; 13022B7E0FB5D16B CRC64; MRSKLNQYNQ KRNFTRTLEP EGITEMPQEG LRFVVQHHLA RRDHYDLRLE WDGAMLSWAV PKGPSYNTRD KRLAVQVEDH PLEYRHFEGT IPKGEYGGGV VMLWDEGFWE PYVDVDGGLH EGMLKFVLKG RRLKGRWALV RMKGKAGDKK DNWLLLKEKD DYVQTADGIS QFITSIRTGR TMTEIEEGEE EKFTRNPFSS TEVQLAKLVR HLPEGEGWLY ELKYDGYRIV AYLEGHRVRL MTRNGHDYTE RFQDVASSLA DWAEGRAMIL DGEMAITDPE GKTDFQALQN YLKNPRTKNL TYILFDLLAL DGADLRGHPL IHRKETLAAL LENAPPNLHY SRHVRGKGEE SFRAACEAGM EGIIGKKADA LYSGTRNGDW IKLKCDQRQE FIIVGYTLSQ KRISGISSLL LGIYEGRELV YAGRAGTGLK ESDMEELEEK FKDIRRSSAP FKPAPKPRAN ERITWVEPEL VVEVKFADWT EENLLRQASF KGLRADKNPR EIRRERADEE KDDGELQLQP PAPERKSLMK INTNSMIIEG IKISSPDKVI FTDPEITKVD MIRYYAKVAE RMLPYVSRRI LSIVRCPKGV AQTCFYKKHP GPGSQGVVTI PILTSDGTTE DYFYIENPSG LIAEAQMGTL EFHIWGSRVD ELEKPDLMVF DLDPDEGMEL GTVRQGVRDL KTILAELSLN SYLKTSGGKG YHVVVPLKPA VSWGVFHDFA QGVAQVMEQK WPDRYTSNVR KAKRTNRIFI DWIRNGRGAT SIAPYSLRAR RGAKVSMPIT WEELDTVAPD GVDMAEALRR IQDSDPWEGF FRNQQRLQ //