ID A0A292Z1H4_9PSEU Unreviewed; 802 AA. AC A0A292Z1H4; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 12-OCT-2022, entry version 18. DE RecName: Full=DNA ligase {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|RuleBase:RU000618}; DE EC=6.5.1.2 {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|RuleBase:RU000618}; DE AltName: Full=Polydeoxyribonucleotide synthase [NAD(+)] {ECO:0000256|HAMAP-Rule:MF_01588}; GN Name=ligA {ECO:0000256|HAMAP-Rule:MF_01588}; GN ORFNames=TOK_0694 {ECO:0000313|EMBL:GAY12300.1}; OS Pseudonocardia sp. N23. OC Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae; OC Pseudonocardia; unclassified Pseudonocardia. OX NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY12300.1, ECO:0000313|Proteomes:UP000222857}; RN [1] {ECO:0000313|EMBL:GAY12300.1, ECO:0000313|Proteomes:UP000222857} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=N23 {ECO:0000313|EMBL:GAY12300.1, RC ECO:0000313|Proteomes:UP000222857}; RA Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.; RT "Characterization of newly isolated Pseudonocardia sp. N23 with high 1,4- RT dioxane-degrading ability."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA ligase that catalyzes the formation of phosphodiester CC linkages between 5'-phosphoryl and 3'-hydroxyl groups in double- CC stranded DNA using NAD as a coenzyme and as the energy source for the CC reaction. It is essential for DNA replication and repair of damaged CC DNA. {ECO:0000256|HAMAP-Rule:MF_01588}. CC -!- CATALYTIC ACTIVITY: CC Reaction=NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho- CC (deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta- CC nicotinamide D-nucleotide.; EC=6.5.1.2; CC Evidence={ECO:0000256|ARBA:ARBA00034005, ECO:0000256|HAMAP- CC Rule:MF_01588, ECO:0000256|RuleBase:RU000618}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01588}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01588}; CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01588}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GAY12300.1}. 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; BEGX01000114; GAY12300.1; -; Genomic_DNA. DR EnsemblBacteria; GAY12300; GAY12300; TOK_0694. DR Proteomes; UP000222857; Unassembled WGS sequence. DR GO; GO:0003911; F:DNA ligase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR CDD; cd00114; LIGANc; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.10190; -; 1. DR HAMAP; MF_01588; DNA_ligase_A; 1. DR InterPro; IPR001357; BRCT_dom. DR InterPro; IPR036420; BRCT_dom_sf. DR InterPro; IPR041663; DisA/LigA_HHH. DR InterPro; IPR018239; DNA_ligase_AS. DR InterPro; IPR033136; DNA_ligase_CS. DR InterPro; IPR001679; DNAligase. DR InterPro; IPR013839; DNAligase_adenylation. DR InterPro; IPR013840; DNAligase_N. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004150; NAD_DNA_ligase_OB. DR InterPro; IPR010994; RuvA_2-like. DR InterPro; IPR004149; Znf_DNAligase_C4. DR Pfam; PF00533; BRCT; 1. DR Pfam; PF01653; DNA_ligase_aden; 1. DR Pfam; PF03120; DNA_ligase_OB; 1. DR Pfam; PF03119; DNA_ligase_ZBD; 1. DR Pfam; PF12826; HHH_2; 1. DR PIRSF; PIRSF001604; LigA; 1. DR SMART; SM00292; BRCT; 1. DR SMART; SM00532; LIGANc; 1. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52113; SSF52113; 1. DR TIGRFAMs; TIGR00575; dnlj; 1. DR PROSITE; PS50172; BRCT; 1. DR PROSITE; PS01055; DNA_LIGASE_N1; 1. DR PROSITE; PS01056; DNA_LIGASE_N2; 1. PE 3: Inferred from homology; KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|HAMAP- KW Rule:MF_01588}; KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|HAMAP- KW Rule:MF_01588}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705, ECO:0000256|HAMAP- KW Rule:MF_01588}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_01588}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_01588}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01588}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_01588}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01588}; KW Reference proteome {ECO:0000313|Proteomes:UP000222857}; KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01588}. FT DOMAIN 709..781 FT /note="BRCT" FT /evidence="ECO:0000259|PROSITE:PS50172" FT REGION 1..20 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 570..631 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 582..615 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 127 FT /note="N6-AMP-lysine intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 46..50 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 95..96 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 125 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 148 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 188 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 304 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 328 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 422 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 425 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 441 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" FT BINDING 447 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01588" SQ SEQUENCE 802 AA; 85794 MW; BD2EF7A684395D02 CRC64; MSTDSPAGTA PRPAPDADRE RHAALATEIA DHQFRYYVLD APVLSDGQFD ELWRELVGLE ERYPDLITAD SPTQKVGSRF ATEFVAHDHL ERMLSLDNAF SADELRGWAE RVGREVGADA HYLCELKIDG LAVNLLYENG KLVRALTRGD GRTGEDVTLN MRTLAEVPEM LTGTAEFPVP ELVEVRGEVY FRLEDFQALN ASLVEAGKPP FANPRNTAAG SLRQKDPRVT GSRNLRLICH GLGKREGFNP ERLSQAYDAL RTWGLPVSER TKIVQGIDDV VAHVEYWGEH RHDIEHEIDG VVVKVDEVAL QRRLGATSRA PRWAIAFKYP PEEVTTKLLD IQVNVGRTGR VTPFAFMEPV VVAGSTVSLA TLHNADEVRR KGVLIGDRVV IRKAGDVIPE VLGPIIDVRD GTERAFVMPT HCPECGTELA QQKAGDVDIR CPNARSCPAQ LRERLFHIAG RGAFDIEALG YKAATALLEA GVVTDEGDVF SLTEEDLLQV DLFRTKAGVL SANGRKLLDN LEKAKDRPLW RVLVGLSIRH VGPTAAQALA REFGSLEAIE EAAARAAEET AKAGVEITSD GSSDEPDADF VPDVDSVPDA VEEPDAVEEP DAVEEPAAAG DSGAGDSGAD AGADAAEAAA VAAAKAERDA TRARAKAVAA ALAPIAGGEG VGPTIAAALR DWFTVDWHRD VVAKWRAAGV RTVDEVDASI PRTLDGLSIV ITGSMAGWSR DEAKEAIAAR GGRAAGSVSK KTAFLVAGDA PGSKYDKALE LGVPILDEAG LGVLLASGPE EAEKVATLAP TD //