ID   POA1_DEBHA              Reviewed;         179 AA.
AC   Q6BPN4;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
GN   Name=POA1; OrderedLocusNames=DEHA2E12188g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382137; CAG88075.2; -; Genomic_DNA.
DR   RefSeq; XP_459836.2; XM_459836.1.
DR   AlphaFoldDB; Q6BPN4; -.
DR   SMR; Q6BPN4; -.
DR   STRING; 4959.XP_459836.2; -.
DR   EnsemblFungi; CAG88075; CAG88075; DEHA2E12188g.
DR   GeneID; 2901966; -.
DR   KEGG; dha:DEHA2E12188g; -.
DR   VEuPathDB; FungiDB:DEHA2E12188g; -.
DR   eggNOG; ENOG502S60W; Eukaryota.
DR   HOGENOM; CLU_054419_1_2_1; -.
DR   InParanoid; Q6BPN4; -.
DR   OMA; NCQGSWG; -.
DR   OrthoDB; 1416296at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
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_0000324907"
FT   DOMAIN          1..179
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         149..155
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   179 AA;  19741 MW;  56237CA25E3B4C45 CRC64;
     MIKYIKGDLF THTPSSRSAI SIFAHACNCR GSWGGGIATV FYRKFPSAYK IYADYCSTHA
     DDPSKLLGTT LLIPSSSSDP GNENGQKIVY VACLFTSDFY GKKKLTPGDI AANTDLSMKD
     LDTQLESLKE EKEIESTDQG EVVVNMPKIN AGLFAVPWEI TEDVLNKFNN LHINVYVVD