ID   POA1_PHANO              Reviewed;         183 AA.
AC   Q0UHC0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
GN   Name=POA1; ORFNames=SNOG_08844;
OS   Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS   blotch fungus) (Parastagonospora nodorum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC   Parastagonospora.
OX   NCBI_TaxID=321614;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173;
RX   PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA   Hane J.K., Lowe R.G.T., Solomon P.S., Tan K.-C., Schoch C.L.,
RA   Spatafora J.W., Crous P.W., Kodira C.D., Birren B.W., Galagan J.E.,
RA   Torriani S.F.F., McDonald B.A., Oliver R.P.;
RT   "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT   analysis of the wheat pathogen Stagonospora nodorum.";
RL   Plant Cell 19:3347-3368(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. {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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=EAT84012.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CH445337; EAT84012.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_001799148.1; XM_001799096.1.
DR   AlphaFoldDB; Q0UHC0; -.
DR   SMR; Q0UHC0; -.
DR   STRING; 321614.Q0UHC0; -.
DR   GeneID; 5976047; -.
DR   KEGG; pno:SNOG_08844; -.
DR   eggNOG; ENOG502S60W; Eukaryota.
DR   InParanoid; Q0UHC0; -.
DR   OrthoDB; 1416296at2759; -.
DR   Proteomes; UP000001055; Unassembled WGS sequence.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0140291; P:peptidyl-glutamate ADP-deribosylation; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..183
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324910"
FT   DOMAIN          8..183
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   BINDING         26..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         41..43
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         48..53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   183 AA;  20133 MW;  613A54EB87169B3D CRC64;
     MDAQSTKDQG PEGADAGTLS FTYHIGDMFE DAPENCLLIH ACNSQGHWGA GIAKAFKQKY
     PKAYTAHNKF CAKEHSKTQP VPTGSAQLLA PVDSGSQHWI GCLFTSAKYG KAKDKPDAIV
     KNTTASMSML LELVRMADGE VSEIRMCKIN SGKFGVPWEK TEEALKSIIL QEGWREKIEI
     WEP