TDG_SCHPO
ID TDG_SCHPO Reviewed; 325 AA.
AC O59825;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=G/U mismatch-specific uracil DNA glycosylase;
DE EC=3.2.2.28;
DE AltName: Full=Uracil mismatch repair protein;
GN Name=thp1; ORFNames=SPCC965.05c;
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], AND FUNCTION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=12711670; DOI=10.1093/nar/gkg344;
RA Hardeland U., Bentele M., Jiricny J., Schaer P.;
RT "The versatile thymine DNA-glycosylase: a comparative characterization of
RT the human, Drosophila and fission yeast orthologs.";
RL Nucleic Acids Res. 31:2261-2271(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Zhu X., Zhao Y.;
RT "An ortholog of thymine mismatch repair enzyme gene in Schizosaccharomyces
RT pombe.";
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
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: Removes uracil from G/U mispairs in ssDNA. Also corrects G/G
CC mispairs. Does not catalyze the removal of thymine from G/T mispairs.
CC {ECO:0000269|PubMed:12711670}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Specifically hydrolyzes mismatched double-stranded DNA and
CC polynucleotides, releasing free uracil.; EC=3.2.2.28;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG) superfamily.
CC TDG/mug family. {ECO:0000305}.
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DR EMBL; AJ277958; CAB93678.1; -; Genomic_DNA.
DR EMBL; AF288481; AAG01021.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA19065.1; -; Genomic_DNA.
DR PIR; T41658; T41658.
DR RefSeq; NP_588515.1; NM_001023504.2.
DR AlphaFoldDB; O59825; -.
DR SMR; O59825; -.
DR BioGRID; 275995; 5.
DR STRING; 4896.SPCC965.05c.1; -.
DR iPTMnet; O59825; -.
DR MaxQB; O59825; -.
DR PaxDb; O59825; -.
DR PRIDE; O59825; -.
DR EnsemblFungi; SPCC965.05c.1; SPCC965.05c.1:pep; SPCC965.05c.
DR GeneID; 2539432; -.
DR KEGG; spo:SPCC965.05c; -.
DR PomBase; SPCC965.05c; thp1.
DR VEuPathDB; FungiDB:SPCC965.05c; -.
DR eggNOG; KOG4120; Eukaryota.
DR HOGENOM; CLU_042829_1_0_1; -.
DR InParanoid; O59825; -.
DR OMA; DYICENP; -.
DR PhylomeDB; O59825; -.
DR BRENDA; 3.2.2.27; 5613.
DR Reactome; R-SPO-110329; Cleavage of the damaged pyrimidine.
DR Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-SPO-5221030; TET1,2,3 and TDG demethylate DNA.
DR PRO; PR:O59825; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0097507; F:hypoxanthine DNA N-glycosylase activity; IDA:PomBase.
DR GO; GO:0097509; F:oxanine DNA N-glycosylase activity; IDA:PomBase.
DR GO; GO:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; IBA:GO_Central.
DR GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:PomBase.
DR GO; GO:0097508; F:xanthine DNA N-glycosylase activity; IDA:PomBase.
DR GO; GO:0006285; P:base-excision repair, AP site formation; IBA:GO_Central.
DR CDD; cd10028; UDG-F2_TDG_MUG; 1.
DR Gene3D; 3.40.470.10; -; 1.
DR InterPro; IPR015637; MUG/TDG.
DR InterPro; IPR003310; TDG-like_euk.
DR InterPro; IPR005122; Uracil-DNA_glycosylase-like.
DR InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
DR PANTHER; PTHR12159; PTHR12159; 1.
DR Pfam; PF03167; UDG; 1.
DR SUPFAM; SSF52141; SSF52141; 1.
DR TIGRFAMs; TIGR00584; mug; 1.
PE 3: Inferred from homology;
KW DNA damage; DNA repair; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..325
FT /note="G/U mismatch-specific uracil DNA glycosylase"
FT /id="PRO_0000185779"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 325 AA; 36574 MW; 0B3F55C43683D92B CRC64;
MNDIETRDTG TKNDNSSEFN LSVKSHKRKR SFDDENLELE ESREETSGGI LKKAKTQSFS
ESLERFRFAH AGSNNEYRKT DVVKNSDTDN GLLKSAVETI TLENGLRNRR VNVTKKSTLK
ASVKKSTLKK KNEVDPALLQ GVPDYICENP YAIIVGLNPG ITSSLKGHAF ASPSNRFWKM
LNKSKLLEGN AEFTYLNDKD LPAHGLGITN LCARPSSSGA DLRKEEMQDG ARILYEKVKR
YRPQVGLFIS GKGIWEEMYK MLTGKKLPKT FVFGWQPEKF GDANVFVGIS SSGRAAGYSD
EKKQNLWNLF AEEVNRHREI VKHAV
