ID   POA1_CANAL              Reviewed;         156 AA.
AC   Q5A1V3; A0A1D8PN47; Q5A1P5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2017, sequence version 2.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
GN   Name=POA1; OrderedLocusNames=CAALFM_C501200WA;
GN   ORFNames=CaO19.1950, CaO19.9506;
OS   Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=237561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA   Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA   Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA   Scherer S.;
RT   "The diploid genome sequence of Candida albicans.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA   van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA   Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA   Chibana H., Nantel A., Magee P.T.;
RT   "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT   on the eight chromosomes.";
RL   Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=SC5314 / ATCC MYA-2876;
RX   PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA   Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT   "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT   specific measurements and provides a simple model for repeat and indel
RT   structure.";
RL   Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
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; CP017627; AOW29555.1; -; Genomic_DNA.
DR   RefSeq; XP_715713.2; XM_710620.2.
DR   AlphaFoldDB; Q5A1V3; -.
DR   SMR; Q5A1V3; -.
DR   STRING; 237561.Q5A1V3; -.
DR   GeneID; 3642657; -.
DR   KEGG; cal:CAALFM_C501200WA; -.
DR   CGD; CAL0000194527; orf19.9506.
DR   VEuPathDB; FungiDB:C5_01200W_A; -.
DR   eggNOG; ENOG502S60W; Eukaryota.
DR   HOGENOM; CLU_054419_1_2_1; -.
DR   InParanoid; Q5A1V3; -.
DR   OrthoDB; 1416296at2759; -.
DR   PRO; PR:Q5A1V3; -.
DR   Proteomes; UP000000559; Chromosome 5.
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   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..156
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324904"
FT   DOMAIN          1..156
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   BINDING         7..9
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         25..27
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         32..37
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         127..133
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   156 AA;  17453 MW;  F4FB0140D21B0BDC CRC64;
     MIQYIKGDLF THAIPAGKKV ILAHACNTHG SWGGGIAAVF RKKFPKSNNE YSQYCHKNSN
     LLGTSFIIES DQPNILIACL FTSDFNQTPE QIVHFTKQSI ADLARKVSDY KEVEKCDGKV
     AINMPKINAG IFGVPWEDTE SALQEFDNLH FNVYVI