UNG_YEAST
ID UNG_YEAST Reviewed; 359 AA.
AC P12887; D6VZF3; E9P912;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Uracil-DNA glycosylase {ECO:0000255|HAMAP-Rule:MF_03166};
DE Short=UDG {ECO:0000255|HAMAP-Rule:MF_03166};
DE EC=3.2.2.27 {ECO:0000255|HAMAP-Rule:MF_03166};
DE Flags: Precursor;
GN Name=UNG1 {ECO:0000255|HAMAP-Rule:MF_03166}; OrderedLocusNames=YML021C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=2644266; DOI=10.1016/s0021-9258(19)81654-x;
RA Percival K.J., Klein M.B., Burgers P.M.J.;
RT "Molecular cloning and primary structure of the uracil-DNA glycosylase gene
RT from Saccharomyces cerevisiae.";
RL J. Biol. Chem. 264:2593-2598(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169872;
RA Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL Nature 387:90-93(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 204626 / S288c / A364A;
RX PubMed=7031606; DOI=10.1093/nar/9.21.5797;
RA Crosby B., Prakash L., Davis H., Hinkle D.C.;
RT "Purification and characterization of a uracil-DNA glycosylase from the
RT yeast, Saccharomyces cerevisiae.";
RL Nucleic Acids Res. 9:5797-5809(1981).
RN [6]
RP FUNCTION, AND INDUCTION.
RX PubMed=1938887; DOI=10.1128/jb.173.21.6807-6810.1991;
RA Impellizzeri K.J., Anderson B., Burgers P.M.;
RT "The spectrum of spontaneous mutations in a Saccharomyces cerevisiae
RT uracil-DNA-glycosylase mutant limits the function of this enzyme to
RT cytosine deamination repair.";
RL J. Bacteriol. 173:6807-6810(1991).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=11812822; DOI=10.1093/nar/29.24.4935;
RA Chatterjee A., Singh K.K.;
RT "Uracil-DNA glycosylase-deficient yeast exhibit a mitochondrial mutator
RT phenotype.";
RL Nucleic Acids Res. 29:4935-4940(2001).
RN [8]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [9]
RP INDUCTION.
RX PubMed=17934734; DOI=10.1007/s00294-007-0159-5;
RA Lucaccioni A., Pavlov Y.I., Achilli A., Babudri N.;
RT "High rate of starvation-associated mutagenesis in Ung(-) yeast caused by
RT the overproduction of human activation-induced deaminase.";
RL Curr. Genet. 52:239-245(2007).
CC -!- FUNCTION: Excises uracil residues from the DNA which can arise as a
CC result of misincorporation of dUMP residues by DNA polymerase or due to
CC deamination of cytosine. Not involved in strand-directed mismatch
CC repair. {ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:11812822,
CC ECO:0000269|PubMed:1938887, ECO:0000269|PubMed:2644266,
CC ECO:0000269|PubMed:7031606}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded
CC DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03166,
CC ECO:0000269|PubMed:7031606};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5-8. {ECO:0000269|PubMed:7031606};
CC -!- INTERACTION:
CC P12887; P15873: POL30; NbExp=4; IntAct=EBI-2097931, EBI-12993;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03166,
CC ECO:0000269|PubMed:11812822}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03166,
CC ECO:0000269|PubMed:11812822}.
CC -!- INDUCTION: Induced in late G1 and early S phase of the cell cycle.
CC {ECO:0000269|PubMed:17934734, ECO:0000269|PubMed:1938887}.
CC -!- MISCELLANEOUS: Present with 4820 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC UNG family. {ECO:0000255|HAMAP-Rule:MF_03166}.
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DR EMBL; J04470; AAA35195.1; -; Genomic_DNA.
DR EMBL; Z46659; CAA86634.1; -; Genomic_DNA.
DR EMBL; AY693020; AAT93039.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA09877.1; -; Genomic_DNA.
DR PIR; A31425; A31425.
DR RefSeq; NP_013691.1; NM_001182379.1.
DR AlphaFoldDB; P12887; -.
DR SMR; P12887; -.
DR BioGRID; 35148; 73.
DR DIP; DIP-8264N; -.
DR ELM; P12887; -.
DR IntAct; P12887; 1.
DR STRING; 4932.YML021C; -.
DR iPTMnet; P12887; -.
DR MaxQB; P12887; -.
DR PaxDb; P12887; -.
DR PRIDE; P12887; -.
DR EnsemblFungi; YML021C_mRNA; YML021C; YML021C.
DR GeneID; 854987; -.
DR KEGG; sce:YML021C; -.
DR SGD; S000004483; UNG1.
DR VEuPathDB; FungiDB:YML021C; -.
DR eggNOG; KOG2994; Eukaryota.
DR GeneTree; ENSGT00390000003405; -.
DR HOGENOM; CLU_032162_2_2_1; -.
DR InParanoid; P12887; -.
DR OMA; PDNGYLM; -.
DR BioCyc; YEAST:G3O-32624-MON; -.
DR Reactome; R-SCE-110329; Cleavage of the damaged pyrimidine.
DR PRO; PR:P12887; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; P12887; protein.
DR GO; GO:0005739; C:mitochondrion; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:SGD.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
DR GO; GO:0006281; P:DNA repair; IMP:SGD.
DR CDD; cd10027; UDG-F1-like; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR HAMAP; MF_00148; UDG; 1.
DR InterPro; IPR002043; UDG_fam1.
DR InterPro; IPR018085; Ura-DNA_Glyclase_AS.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR11264; PTHR11264; 1.
DR Pfam; PF03167; UDG; 1.
DR SMART; SM00986; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR TIGRFAMs; TIGR00628; ung; 1.
DR PROSITE; PS00130; U_DNA_GLYCOSYLASE; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Hydrolase; Mitochondrion; Nucleus;
KW Reference proteome; Transit peptide.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 22..359
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000036085"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03166"
FT CONFLICT 173
FT /note="L -> S (in Ref. 4; AAT93039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 359 AA; 40471 MW; CC06971E05FE7751 CRC64;
MWCMRRLPTN SVMTVARKRK QTTIEDFFGT KKSTNEAPNK KGKSGATFMT ITNGAAIKTE
TKAVAKEANT DKYPANSNAK DVYSKNLSSN LRTLLSLELE TIDDSWFPHL MDEFKKPYFV
KLKQFVTKEQ ADHTVFPPAK DIYSWTRLTP FNKVKVVIIG QDPYHNFNQA HGLAFSVKPP
TPAPPSLKNI YKELKQEYPD FVEDNKVGDL THWASQGVLL LNTSLTVRAH NANSHSKHGW
ETFTKRVVQL LIQDREADGK SLVFLLWGNN AIKLVESLLG STSVGSGSKY PNIMVMKSVH
PSPLSASRGF FGTNHFKMIN DWLYNTRGEK MIDWSVVPGT SLREVQEANA RLESESKDP
