UNG_SCHPO
ID UNG_SCHPO Reviewed; 322 AA.
AC O74834;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 137.
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};
GN Name=ung1; ORFNames=SPCC1183.06;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=SP223;
RX PubMed=12810074; DOI=10.1016/s0006-291x(03)01036-2;
RA Elder R.T., Zhu X., Priet S., Chen M., Yu M., Navarro J.-M., Sire J.,
RA Zhao Y.;
RT "A fission yeast homologue of the human uracil-DNA-glycosylase and their
RT roles in causing DNA damage after overexpression.";
RL Biochem. Biophys. Res. Commun. 306:693-700(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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. {ECO:0000255|HAMAP-Rule:MF_03166,
CC ECO:0000269|PubMed:12810074}.
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 -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03166}.
CC Nucleus {ECO:0000255|HAMAP-Rule:MF_03166, ECO:0000269|PubMed:12810074}.
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; AF174292; AAD51974.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA21086.1; -; Genomic_DNA.
DR PIR; T40846; T40846.
DR RefSeq; NP_587889.1; NM_001022881.2.
DR AlphaFoldDB; O74834; -.
DR SMR; O74834; -.
DR BioGRID; 275436; 15.
DR STRING; 4896.SPCC1183.06.1; -.
DR iPTMnet; O74834; -.
DR MaxQB; O74834; -.
DR PaxDb; O74834; -.
DR PRIDE; O74834; -.
DR EnsemblFungi; SPCC1183.06.1; SPCC1183.06.1:pep; SPCC1183.06.
DR GeneID; 2538855; -.
DR KEGG; spo:SPCC1183.06; -.
DR PomBase; SPCC1183.06; ung1.
DR VEuPathDB; FungiDB:SPCC1183.06; -.
DR eggNOG; KOG2994; Eukaryota.
DR HOGENOM; CLU_032162_2_2_1; -.
DR InParanoid; O74834; -.
DR OMA; PDNGYLM; -.
DR PhylomeDB; O74834; -.
DR Reactome; R-SPO-110329; Cleavage of the damaged pyrimidine.
DR PRO; PR:O74834; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:PomBase.
DR GO; GO:0006284; P:base-excision repair; IMP:PomBase.
DR GO; GO:0097510; P:base-excision repair, AP site formation via deaminated base removal; IBA:GO_Central.
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 3: Inferred from homology;
KW DNA damage; DNA repair; Hydrolase; Mitochondrion; Nucleus;
KW Reference proteome.
FT CHAIN 1..322
FT /note="Uracil-DNA glycosylase"
FT /id="PRO_0000176171"
FT ACT_SITE 142
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03166"
SQ SEQUENCE 322 AA; 36705 MW; 367EB5E53733F80C CRC64;
MTVLNTTDKR KADDTVNKLD GKLKQPRLDN FFKTNTSSPA LKDTQVLDNK ENNSVSKFNK
EKWAENLTPA QRKLLQLEID TLESSWFDAL KDEFLKPYFL NLKEFLMKEW QSQRVFPPKE
DIYSWSHHTP LHKTKVILLG QDPYHNIGQA HGLCFSVRPG IPCPPSLVNI YKAIKIDYPD
FVIPKTGYLV PWADQGILML NASLTVRAHQ AASHSGKGWE TFTSAVLQVA LNRNRKGLVI
LAWGTPAAKR LQGLPLKAHY VLRSVHPSPL SAHRGFFECH HFKKTNEWLE EQYGPEKCIN
WSAVSEQKAK IKSSELESSS TE
