ID   POA1_VANPO              Reviewed;         180 AA.
AC   A7TJY9;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   02-OCT-2007, sequence version 1.
DT   03-AUG-2022, entry version 60.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
GN   Name=POA1; ORFNames=Kpol_1037p48;
OS   Vanderwaltozyma polyspora (strain ATCC 22028 / DSM 70294 / BCRC 21397 / CBS
OS   2163 / NBRC 10782 / NRRL Y-8283 / UCD 57-17) (Kluyveromyces polysporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Vanderwaltozyma.
OX   NCBI_TaxID=436907;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 22028 / DSM 70294 / BCRC 21397 / CBS 2163 / NBRC 10782 / NRRL
RC   Y-8283 / UCD 57-17;
RX   PubMed=17494770; DOI=10.1073/pnas.0608218104;
RA   Scannell D.R., Frank A.C., Conant G.C., Byrne K.P., Woolfit M., Wolfe K.H.;
RT   "Independent sorting-out of thousands of duplicated gene pairs in two yeast
RT   species descended from a whole-genome duplication.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:8397-8402(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}.
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DR   EMBL; DS480404; EDO17451.1; -; Genomic_DNA.
DR   RefSeq; XP_001645309.1; XM_001645259.1.
DR   AlphaFoldDB; A7TJY9; -.
DR   SMR; A7TJY9; -.
DR   STRING; 436907.A7TJY9; -.
DR   EnsemblFungi; EDO17451; EDO17451; Kpol_1037p48.
DR   GeneID; 5545671; -.
DR   KEGG; vpo:Kpol_1037p48; -.
DR   eggNOG; ENOG502S60W; Eukaryota.
DR   HOGENOM; CLU_054419_1_2_1; -.
DR   InParanoid; A7TJY9; -.
DR   OMA; IFGVPWE; -.
DR   OrthoDB; 1416296at2759; -.
DR   PhylomeDB; A7TJY9; -.
DR   Proteomes; UP000000267; 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; Reference proteome.
FT   CHAIN           1..180
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324913"
FT   DOMAIN          1..180
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   BINDING         12..14
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         27..29
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         34..39
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         151..157
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   180 AA;  20300 MW;  B38767BE3D15905F CRC64;
     MIEMNNISYI KGNILHGGNI PRILIHSCNC NGTWGGGIAY QLAVHYPEAE KIYTDICDDF
     GSELLGKCVL IPSFSDDSLL IGCLFTSVYG GSSHDTKNEI LKYTKLSLMQ LSLQLENNDS
     CIDTCLSEYN QLLISNIKHH LKDYKLEMPK INSGIFNVPW EETEKILKEL KPMEFTVFSI