ID   POA1_CANGA              Reviewed;         179 AA.
AC   Q6FXN3;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
GN   Name=POA1; OrderedLocusNames=CAGL0B04411g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380948; CAG58062.1; -; Genomic_DNA.
DR   RefSeq; XP_445162.1; XM_445162.1.
DR   AlphaFoldDB; Q6FXN3; -.
DR   SMR; Q6FXN3; -.
DR   STRING; 5478.XP_445162.1; -.
DR   EnsemblFungi; CAG58062; CAG58062; CAGL0B04411g.
DR   GeneID; 2886571; -.
DR   KEGG; cgr:CAGL0B04411g; -.
DR   CGD; CAL0127810; CAGL0B04411g.
DR   VEuPathDB; FungiDB:CAGL0B04411g; -.
DR   eggNOG; ENOG502S60W; Eukaryota.
DR   HOGENOM; CLU_054419_1_2_1; -.
DR   InParanoid; Q6FXN3; -.
DR   OMA; IFGVPWE; -.
DR   Proteomes; UP000002428; Chromosome B.
DR   GO; GO:0047407; F:ADP-ribosyl-[dinitrogen reductase] hydrolase activity; IEA:EnsemblFungi.
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..179
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324905"
FT   DOMAIN          1..179
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         149..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   179 AA;  19982 MW;  9B24E3DE8759C2E4 CRC64;
     MSNIHYIKGN ILKGRTYKRI IIHSCNANGA WGGGIAYQLA VKHPKAEEVY VDLCERFGQK
     LLGKCVVIPS YSDDDVLIGC LFTSIFGGAS HGSGTSIVDY TDKALSHFDE LLAKEQSKSD
     NANLDKEIEK LLKLKSGVLK DYKLEMPKIN SGIFGVPWPE TEEVLKKYDR SMNFTVYEL