ID   POA1_YEAS7              Reviewed;         177 AA.
AC   A6ZKW8;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   03-AUG-2022, entry version 53.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
DE            EC=3.2.2.-;
DE   AltName: Full=[Protein ADP-ribosylglutamate] hydrolase;
GN   Name=POA1; ORFNames=SCY_0238;
OS   Saccharomyces cerevisiae (strain YJM789) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=307796;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJM789;
RX   PubMed=17652520; DOI=10.1073/pnas.0701291104;
RA   Wei W., McCusker J.H., Hyman R.W., Jones T., Ning Y., Cao Z., Gu Z.,
RA   Bruno D., Miranda M., Nguyen M., Wilhelmy J., Komp C., Tamse R., Wang X.,
RA   Jia P., Luedi P., Oefner P.J., David L., Dietrich F.S., Li Y., Davis R.W.,
RA   Steinmetz L.M.;
RT   "Genome sequencing and comparative analysis of Saccharomyces cerevisiae
RT   strain YJM789.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:12825-12830(2007).
CC   -!- FUNCTION: Highly specific phosphatase involved in the metabolism of
CC       ADP-ribose 1''-phosphate (Appr1p) which is produced as a consequence of
CC       tRNA splicing. Removes ADP-ribose from glutamate residues in proteins
CC       bearing a single ADP-ribose moiety. Inactive towards proteins bearing
CC       poly-ADP-ribose (By similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ADP-beta-D-ribose 1''-phosphate + H2O = ADP-D-ribose +
CC         phosphate; Xref=Rhea:RHEA:25029, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57967, ChEBI:CHEBI:58753; EC=3.1.3.84;
CC   -!- SIMILARITY: Belongs to the POA1 family. {ECO:0000305}.
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DR   EMBL; AAFW02000011; EDN64637.1; -; Genomic_DNA.
DR   AlphaFoldDB; A6ZKW8; -.
DR   SMR; A6ZKW8; -.
DR   EnsemblFungi; EDN64637; EDN64637; SCY_0238.
DR   HOGENOM; CLU_054419_1_2_1; -.
DR   Proteomes; UP000007060; Unassembled WGS sequence.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.220.10; -; 1.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   Pfam; PF01661; Macro; 1.
DR   SMART; SM00506; A1pp; 1.
DR   SUPFAM; SSF52949; SSF52949; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protein phosphatase.
FT   CHAIN           1..177
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324915"
FT   DOMAIN          1..177
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   BINDING         9..11
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         24..26
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         31..36
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         147..153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   177 AA;  19938 MW;  006E55E9E598887A CRC64;
     MSNITYVKGN ILKPKSYARI LIHSCNCNGS WGGGIAYQLA LRYPKAEKDY VEVCEKYGSN
     LLGKCILLPS YENSDLLICC LFTSSFGGSS HGEKQSILNY TKLALDKLKT FREAKDKTRT
     SEDSIGDYLN GHIKYPIGEY KLEMPQINSG IFGVPWKETE RVLEEFSGDM SFTVYQL