TPP1_YEAST
ID TPP1_YEAST Reviewed; 238 AA.
AC Q03796; D6VZX7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Polynucleotide 3'-phosphatase {ECO:0000303|PubMed:11278831};
DE EC=3.1.3.32 {ECO:0000269|PubMed:11278831};
DE AltName: Full=2'(3')-polynucleotidase;
DE AltName: Full=DNA 3'-phosphatase;
DE AltName: Full=Three prime phosphatase;
GN Name=TPP1; OrderedLocusNames=YMR156C; ORFNames=YM8520.05C;
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 [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 [2]
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 [3]
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 [4]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=11278831; DOI=10.1074/jbc.m011075200;
RA Vance J.R., Wilson T.E.;
RT "Uncoupling of 3'-phosphatase and 5'-kinase functions in budding yeast.
RT Characterization of Saccharomyces cerevisiae DNA 3'-phosphatase (TPP1).";
RL J. Biol. Chem. 276:15073-15081(2001).
CC -!- FUNCTION: Dephosphorylate DNA's 3'-phosphate termini. Has a role in the
CC repair of breaks in single-stranded DNA. {ECO:0000269|PubMed:11278831}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 3'end (2'-deoxyribonucleotide 3'-phosphate)-DNA + H2O = a
CC 3'-end 2'-deoxyribonucleotide-DNA + phosphate; Xref=Rhea:RHEA:14113,
CC Rhea:RHEA-COMP:13863, Rhea:RHEA-COMP:13864, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:138147, ChEBI:CHEBI:138148;
CC EC=3.1.3.32; Evidence={ECO:0000269|PubMed:11278831};
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DNA 3' phosphatase family. {ECO:0000305}.
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DR EMBL; Z49705; CAA89792.1; -; Genomic_DNA.
DR EMBL; AY557979; AAS56305.1; -; Genomic_DNA.
DR EMBL; BK006946; DAA10051.1; -; Genomic_DNA.
DR PIR; S54514; S54514.
DR RefSeq; NP_013877.1; NM_001182659.1.
DR AlphaFoldDB; Q03796; -.
DR SMR; Q03796; -.
DR BioGRID; 35331; 59.
DR IntAct; Q03796; 4.
DR MINT; Q03796; -.
DR STRING; 4932.YMR156C; -.
DR MaxQB; Q03796; -.
DR PaxDb; Q03796; -.
DR PRIDE; Q03796; -.
DR EnsemblFungi; YMR156C_mRNA; YMR156C; YMR156C.
DR GeneID; 855188; -.
DR KEGG; sce:YMR156C; -.
DR SGD; S000004765; TPP1.
DR VEuPathDB; FungiDB:YMR156C; -.
DR eggNOG; KOG2134; Eukaryota.
DR GeneTree; ENSGT00940000159302; -.
DR HOGENOM; CLU_014938_0_0_1; -.
DR OMA; KPEIGMW; -.
DR BioCyc; YEAST:G3O-32846-MON; -.
DR PRO; PR:Q03796; -.
DR Proteomes; UP000002311; Chromosome XIII.
DR RNAct; Q03796; protein.
DR GO; GO:0005634; C:nucleus; IC:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0046404; F:polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central.
DR GO; GO:0046403; F:polynucleotide 3'-phosphatase activity; IDA:SGD.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR GO; GO:0046939; P:nucleotide phosphorylation; IBA:GO_Central.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR013954; PNK3P.
DR InterPro; IPR006551; Polynucleotide_phosphatase.
DR Pfam; PF08645; PNK3P; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01664; DNA-3'-Pase; 1.
PE 1: Evidence at protein level;
KW DNA damage; DNA repair; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..238
FT /note="Polynucleotide 3'-phosphatase"
FT /id="PRO_0000065580"
SQ SEQUENCE 238 AA; 27383 MW; ABE35B947077D687 CRC64;
MSHKLTILPF LIKFTPKFPQ SIDHDEHGLN VYAFDLDHTI IKPKSPNISF SRSASDWQFI
NFNSKKSTLD YLCNIIDNDP TAVIVIFSNQ GGVITVPRTS KSCTKYTNKI LLFLKAIKND
ERGETLSHRL WLYAAPKRPK TFAANHSKIT FASLGESYNN DPNIFEKVRK PMTGMVEFFK
RDLESAYRVS EQISPIKLNW IYYCGDAAGR KKDFSDSDIK FAENLHVEFK YPEEIFHG
