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Database: UniProt/TrEMBL
Entry: G0WG84_NAUDC
LinkDB: G0WG84_NAUDC
Original site: G0WG84_NAUDC 
ID   G0WG84_NAUDC            Unreviewed;       967 AA.
AC   G0WG84;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   07-JUN-2017, entry version 34.
DE   RecName: Full=DNA ligase {ECO:0000256|RuleBase:RU000617};
DE            EC=6.5.1.1 {ECO:0000256|RuleBase:RU000617};
GN   Name=NDAI0I02260 {ECO:0000313|EMBL:CCD26795.1};
GN   OrderedLocusNames=NDAI_0I02260 {ECO:0000313|EMBL:CCD26795.1};
OS   Naumovozyma dairenensis (strain ATCC 10597 / BCRC 20456 / CBS 421 /
OS   NBRC 0211 / NRRL Y-12639) (Saccharomyces dairenensis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Naumovozyma.
OX   NCBI_TaxID=1071378 {ECO:0000313|EMBL:CCD26795.1, ECO:0000313|Proteomes:UP000000689};
RN   [1] {ECO:0000313|EMBL:CCD26795.1, 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.,
RA   Byrne K.P., Wolfe K.H.;
RT   "Evolutionary erosion of yeast sex chromosomes by mating-type
RT   switching accidents.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:20024-20029(2011).
CC   -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n)-3'-hydroxyl +
CC       5'-phospho-(deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) +
CC       AMP + diphosphate. {ECO:0000256|RuleBase:RU000617}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family.
CC       {ECO:0000256|RuleBase:RU004196}.
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DR   EMBL; HE580275; CCD26795.1; -; Genomic_DNA.
DR   RefSeq; XP_003672038.1; XM_003671990.1.
DR   ProteinModelPortal; G0WG84; -.
DR   STRING; 1071378.XP_003672038.1; -.
DR   EnsemblFungi; CCD26795; CCD26795; NDAI_0I02260.
DR   GeneID; 11493806; -.
DR   KEGG; ndi:NDAI_0I02260; -.
DR   eggNOG; KOG0966; Eukaryota.
DR   eggNOG; COG1793; LUCA.
DR   KO; K10777; -.
DR   OrthoDB; EOG092C18KW; -.
DR   Proteomes; UP000000689; Chromosome 9.
DR   GO; GO:0032807; C:DNA ligase IV complex; IEA:EnsemblFungi.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:EnsemblFungi.
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:0051103; P:DNA ligation involved in DNA repair; IEA:InterPro.
DR   GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   GO; GO:0006303; P:double-strand break repair via nonhomologous end joining; IEA:EnsemblFungi.
DR   GO; GO:0001302; P:replicative cell aging; IEA:EnsemblFungi.
DR   Gene3D; 3.40.50.10190; -; 2.
DR   InterPro; IPR001357; BRCT_dom.
DR   InterPro; IPR000977; DNA_ligase_ATP-dep.
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; IPR029710; LIG4.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   PANTHER; PTHR10459:SF84; PTHR10459:SF84; 1.
DR   Pfam; PF16589; BRCT_2; 1.
DR   Pfam; PF01068; DNA_ligase_A_M; 1.
DR   Pfam; PF04675; DNA_ligase_A_N; 1.
DR   SMART; SM00292; BRCT; 2.
DR   SUPFAM; SSF50249; SSF50249; 2.
DR   SUPFAM; SSF52113; SSF52113; 3.
DR   TIGRFAMs; TIGR00574; dnl1; 1.
DR   PROSITE; PS50172; BRCT; 2.
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|RuleBase:RU000617};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000689};
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|RuleBase:RU000617};
KW   Ligase {ECO:0000256|RuleBase:RU000617};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU000617};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000689}.
FT   DOMAIN      386    518       DNA_LIGASE_A3. {ECO:0000259|PROSITE:
FT                                PS50160}.
FT   DOMAIN      711    809       BRCT. {ECO:0000259|PROSITE:PS50172}.
FT   DOMAIN      870    966       BRCT. {ECO:0000259|PROSITE:PS50172}.
SQ   SEQUENCE   967 AA;  111020 MW;  1AEC5828055FDA79 CRC64;
     MDGKAVTPTL DNDTRPATPH NFAPSPSFRW LCDELFVKLE RIQQASTSKA SKEFQKPINV
     QYYEVIQHFI NLWRKTVGND IYPALILILP YRDRRIYNVR DYTLIKAICS YLKLPKNSFT
     EKRLLSWKQR AGRSVRLSSF IVSEIKKRKS EPQVGTREEI TIDKLNQCLD SLSEERNSKG
     SMGYRGLSDS PTFVFCLENM TFVELQFFFD IILKSRVIGG HEHKFLNVWH PDAQDYLSVV
     SDLKTVANKL WDPAVHLKND DLTINVGSPF APQSAKKLSI SYEKICAKLK HDFFIEEKMD
     GERIQLHYQD YGNKLSFLSR RGTDYTYLYG ESIKDGTVSK YLHLDNNVQN CVLDGEMVTF
     DKERNALLPF GLVKSSARSI ITQEGVANEG YRPLLMVFDL VYLNGVSLVN IPLYQRKLYL
     EKIFTPERHI VELLRSKRCS DERSIKNALE HAISIGSEGV VLKHYNSRYT VASRNDDWIK
     VKPEYLEQFG ENMDLIVIGK DPGKKDSLMC GLAVVEEDEP EIDEDGNEIV NLDSQDSIGE
     GEDKEGNEIE REKTIKRFVS FCSIANGISQ EEFKYIGRIT KGCWKKSDEI PPPSDLLEFG
     SRVPAEWIDP KDSIVIEVKA RSLNNDEEAT KKFKTGITLY GGYCRQIRED KDWKTCYTLS
     ELRRMKRFKL GSNKRANNDA THALDSSKRR KARRIDYGFE KYFEQTPTTL DQSRIFDGLY
     FYVISDVVDA TGSRVSREEL YDKILNRGGV IVHNVIAKHH GENQFRILCG KYTAECQSLI
     DRGYDIIEPQ WVLDCIKDDM LLKLEPKYCF NVSEELMKIA KRRVDGFGDS FEAQISEDSF
     SRLIERNVRS LRNAPPSIQY DMVDTVPLFL FYGRTILLRI KDKALFTKLK VQIRLYGGKT
     TGDLASCNLV VIQQNEIAVA KDVRSSLLKL TSDTDKPPVL PYIVTPEWID SSISEGCQVP
     EEDHPVV
//
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