ID A0A292Z1H4_9PSEU Unreviewed; 802 AA. AC A0A292Z1H4; DT 20-DEC-2017, integrated into UniProtKB/TrEMBL. DT 20-DEC-2017, sequence version 1. DT 28-MAR-2018, entry version 4. 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. 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 RT 1,4-dioxane-degrading ability."; RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: DNA ligase that catalyzes the formation of CC phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl CC groups in double-stranded DNA using NAD as a coenzyme and as the CC energy source for the reaction. It is essential for DNA CC replication and repair of damaged DNA. {ECO:0000256|HAMAP- CC Rule:MF_01588, ECO:0000256|SAAS:SAAS00919855}. CC -!- CATALYTIC ACTIVITY: NAD(+) + (deoxyribonucleotide)(n)-3'-hydroxyl CC + 5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) CC + AMP + beta-nicotinamide D-nucleotide. {ECO:0000256|HAMAP- CC Rule:MF_01588, ECO:0000256|RuleBase:RU000618, CC ECO:0000256|SAAS:SAAS00919872}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01588}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01588}; CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000256|SAAS:SAAS00919880}; CC -!- SIMILARITY: Belongs to the NAD-dependent DNA ligase family. LigA CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01588, CC ECO:0000256|SAAS:SAAS00919881}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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; cd00027; BRCT; 1. DR CDD; cd00114; LIGANc; 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; 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 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 Complete proteome {ECO:0000313|Proteomes:UP000222857}; KW DNA damage {ECO:0000256|HAMAP-Rule:MF_01588, KW ECO:0000256|RuleBase:RU000618, ECO:0000256|SAAS:SAAS00919866}; KW DNA repair {ECO:0000256|HAMAP-Rule:MF_01588, KW ECO:0000256|RuleBase:RU000618, ECO:0000256|SAAS:SAAS00919870}; KW DNA replication {ECO:0000256|HAMAP-Rule:MF_01588, KW ECO:0000256|RuleBase:RU000618, ECO:0000256|SAAS:SAAS00919852}; KW Ligase {ECO:0000256|HAMAP-Rule:MF_01588, KW ECO:0000256|RuleBase:RU000618, ECO:0000256|SAAS:SAAS00919871, KW ECO:0000313|EMBL:GAY12300.1}; KW Magnesium {ECO:0000256|HAMAP-Rule:MF_01588, KW ECO:0000256|SAAS:SAAS00919874}; KW Manganese {ECO:0000256|HAMAP-Rule:MF_01588, KW ECO:0000256|SAAS:SAAS00919865}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01588, KW ECO:0000256|SAAS:SAAS00919873}; KW NAD {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|RuleBase:RU000618, KW ECO:0000256|SAAS:SAAS00919857}; KW Reference proteome {ECO:0000313|Proteomes:UP000222857}; KW Zinc {ECO:0000256|HAMAP-Rule:MF_01588, ECO:0000256|SAAS:SAAS00919858}. FT DOMAIN 709 781 BRCT. {ECO:0000259|PROSITE:PS50172}. FT NP_BIND 46 50 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT NP_BIND 95 96 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT ACT_SITE 127 127 N6-AMP-lysine intermediate. FT {ECO:0000256|HAMAP-Rule:MF_01588}. FT METAL 422 422 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}. FT METAL 425 425 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}. FT METAL 441 441 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}. FT METAL 447 447 Zinc. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 125 125 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 148 148 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 188 188 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 304 304 NAD. {ECO:0000256|HAMAP-Rule:MF_01588}. FT BINDING 328 328 NAD. {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 //