ID   POA1_PICST              Reviewed;         173 AA.
AC   A3LZD1;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
GN   Name=POA1; ORFNames=PICST_49619;
OS   Scheffersomyces stipitis (strain ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL
OS   Y-11545) (Yeast) (Pichia stipitis).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Scheffersomyces.
OX   NCBI_TaxID=322104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58785 / CBS 6054 / NBRC 10063 / NRRL Y-11545;
RX   PubMed=17334359; DOI=10.1038/nbt1290;
RA   Jeffries T.W., Grigoriev I.V., Grimwood J., Laplaza J.M., Aerts A.,
RA   Salamov A., Schmutz J., Lindquist E., Dehal P., Shapiro H., Jin Y.-S.,
RA   Passoth V., Richardson P.M.;
RT   "Genome sequence of the lignocellulose-bioconverting and xylose-fermenting
RT   yeast Pichia stipitis.";
RL   Nat. Biotechnol. 25:319-326(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; CP000501; ABN68136.2; -; Genomic_DNA.
DR   RefSeq; XP_001386165.2; XM_001386128.1.
DR   AlphaFoldDB; A3LZD1; -.
DR   SMR; A3LZD1; -.
DR   EnsemblFungi; ABN68136; ABN68136; PICST_49619.
DR   GeneID; 4840631; -.
DR   KEGG; pic:PICST_49619; -.
DR   eggNOG; ENOG502S60W; Eukaryota.
DR   HOGENOM; CLU_054419_1_2_1; -.
DR   InParanoid; A3LZD1; -.
DR   OMA; IFGVPWE; -.
DR   OrthoDB; 1416296at2759; -.
DR   Proteomes; UP000002258; Chromosome 7.
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..173
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324912"
FT   DOMAIN          1..173
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   BINDING         7..9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         26..28
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         33..38
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         145..151
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   173 AA;  18749 MW;  86C03A6065D2B5A0 CRC64;
     MIRYIKGDLL GHLPPSKSSV AVFAHACNCQ GVWGGGIAAV LRVKFPSTYP LYSGHCQEKG
     CDPHRLLGTS VVVPSQASDP GNIAGYPPKY IACLFTSDFA QTQEEIVAYT DSAIEALVDQ
     LKELQKTTAI ETGQSGKIVV NMPKINAGIF AVPWEKTEAV LKKYDVEFNV YVI