ID G0W3G4_NAUDC Unreviewed; 765 AA. AC G0W3G4; DT 19-OCT-2011, integrated into UniProtKB/TrEMBL. DT 19-OCT-2011, sequence version 1. DT 27-MAR-2024, entry version 53. DE RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617}; DE EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617}; GN Name=NDAI0A01940 {ECO:0000313|EMBL:CCD22352.1}; GN OrderedLocusNames=NDAI_0A01940 {ECO:0000313|EMBL:CCD22352.1}; OS Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 / NBRC OS 0211 / NRRL Y-12639) (Saccharomyces dairenensis). OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Naumovozyma. OX NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD22352.1, ECO:0000313|Proteomes:UP000000689}; RN [1] {ECO:0000313|EMBL:CCD22352.1, ECO:0000313|Proteomes:UP000000689} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 10597 / BCRC 20456 / CBS 421 / NBRC 0211 / NRRL Y-12639 RC {ECO:0000313|Proteomes:UP000000689}; RX PubMed=22123960; DOI=10.1073/pnas.1112808108; RA Gordon J.L., Armisen D., Proux-Wera E., OhEigeartaigh S.S., Byrne K.P., RA Wolfe K.H.; RT "Evolutionary erosion of yeast sex chromosomes by mating-type switching RT accidents."; RL Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011). 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 ECO:0000256|RuleBase:RU000617}; CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000256|ARBA:ARBA00007572, ECO:0000256|RuleBase:RU004196}. 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; HE580267; CCD22352.1; -; Genomic_DNA. DR RefSeq; XP_003667595.1; XM_003667547.1. DR AlphaFoldDB; G0W3G4; -. DR STRING; 1071378.G0W3G4; -. DR GeneID; 11494225; -. DR KEGG; ndi:NDAI_0A01940; -. DR eggNOG; KOG0967; Eukaryota. DR HOGENOM; CLU_005138_4_1_1; -. DR OMA; WIKYKRD; -. DR OrthoDB; 961at2759; -. DR Proteomes; UP000000689; Chromosome 1. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IEA:UniProtKB-EC. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; 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; cd07900; Adenylation_DNA_ligase_I_Euk; 1. DR CDD; cd07969; OBF_DNA_ligase_I; 1. DR Gene3D; 3.30.1490.70; -; 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 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:SF4; DNA LIGASE 1; 1. DR PANTHER; PTHR45674; DNA LIGASE 1/3 FAMILY MEMBER; 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; PS00333; DNA_LIGASE_A2; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU000617}; KW DNA damage {ECO:0000256|RuleBase:RU000617}; KW DNA recombination {ECO:0000256|RuleBase:RU000617}; KW DNA repair {ECO:0000256|RuleBase:RU000617}; KW DNA replication {ECO:0000256|ARBA:ARBA00022705}; KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|RuleBase:RU000617}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, KW ECO:0000256|RuleBase:RU000617}; KW Reference proteome {ECO:0000313|Proteomes:UP000000689}. FT DOMAIN 509..646 FT /note="ATP-dependent DNA ligase family profile" FT /evidence="ECO:0000259|PROSITE:PS50160" FT REGION 20..141 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 24..60 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 62..94 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 95..110 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 118..140 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 765 AA; 85961 MW; B2183F7D9EE8185B CRC64; MLRQLGTTRI LLPNLRPIRY ITMPPATPSS SSSSSSSSAR ENNVSKGRKQ QATLGRFFSS INHKKPTKDT ALKNESKEET KEENKDDSDS IPRKKIRLST SSSSPSIMAE SKPKSPIKLN TERSSSPASA SASTTPTPIV ADHTLDPKTA VSKPFLCAIP YKEVCQLFQE IETTSSRLSI IKLCSDFLIK IMKQDPQNLI PVTYLFINKL GPDYEPGLEL GLGEGLLMKT ISESCGKSLT QIRAQYRELG DLGQIALEAR NVQPTMFKPK PLTVGEVFNN LKMIAKAAGK DSQTKKIKLI KRMLTACEDG VEAKFLIRSL ESKLRIGLAE KTVLISLSKA LLVKEFDANK DFDMELLETA EGKIRDAFCQ VPNYEIVINS CLQYGIMNLN EHCSLRPGIP LKPMLAKPTK AINEILDRFQ GETFTSEYKY DGERAQVHLL EDGTMRIYSR NGENMTERYP EIHIGDFVKD RNETKTLILD CEAVAWDKEQ QKILPFQVLS TRKRKDVLAK DVKVRVCLFA FDILCHNSNK LINYSLKERR EILHRVTTPA PGEFQYATEL TTSNLDELQK FLDQSVNDSC EGLMVKMLEG EESHYEPSKR SRNWLKLKKD YLEGIGDSLD LCVLGAYYGR GKRTGTYGGF LLGCYNDNTG EFETCCKIGT GFSDEMLQQL HEKLKATVID GPKATYIYDS SAEPDVWFEP SLLFEVLTAD LSLSPIYKAG SSAYDKGVSL RFPRFIRIRE DKGVEDATSS EQIIELYENQ SHRSS //