ID   POA1_YARLI              Reviewed;         169 AA.
AC   Q6CHN5;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, 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=YALI0A06908g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382127; CAG83752.2; -; Genomic_DNA.
DR   RefSeq; XP_499826.2; XM_499826.2.
DR   AlphaFoldDB; Q6CHN5; -.
DR   SMR; Q6CHN5; -.
DR   EnsemblFungi; CAG83752; CAG83752; YALI0_A06908g.
DR   GeneID; 2906499; -.
DR   KEGG; yli:YALI0A06908g; -.
DR   VEuPathDB; FungiDB:YALI0_A06908g; -.
DR   HOGENOM; CLU_054419_1_2_1; -.
DR   InParanoid; Q6CHN5; -.
DR   OMA; IFGVPWE; -.
DR   Proteomes; UP000001300; Chromosome A.
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..169
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324914"
FT   DOMAIN          1..169
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   BINDING         13..15
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         28..30
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         35..40
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140..146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   169 AA;  18589 MW;  6C9D94210E877362 CRC64;
     MGYRLSALTY VQGDLFEESP RPAVLAHACN CLGSWGSGVA AGFKQKFPGA FVEYKRHCDK
     YSDDNSALLG TCQLIETHDA QTGELVYVAC LFTSVRFGAR VDGPEQIVKQ TKLAMQDLQK
     QLAKMSGPID GNSTVHMPKI NAGLFRVPWR DTEKVLEEVG QPCTVYVID