ID   POA1_LODEL              Reviewed;         160 AA.
AC   A5E287;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
DE            EC=3.2.2.-;
DE   AltName: Full=[Protein ADP-ribosylglutamate] hydrolase;
GN   Name=POA1; ORFNames=LELG_03724;
OS   Lodderomyces elongisporus (strain ATCC 11503 / CBS 2605 / JCM 1781 / NBRC
OS   1676 / NRRL YB-4239) (Yeast) (Saccharomyces elongisporus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade;
OC   Lodderomyces.
OX   NCBI_TaxID=379508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11503 / BCRC 21390 / CBS 2605 / JCM 1781 / NBRC 1676 / NRRL
RC   YB-4239;
RX   PubMed=19465905; DOI=10.1038/nature08064;
RA   Butler G., Rasmussen M.D., Lin M.F., Santos M.A.S., Sakthikumar S.,
RA   Munro C.A., Rheinbay E., Grabherr M., Forche A., Reedy J.L., Agrafioti I.,
RA   Arnaud M.B., Bates S., Brown A.J.P., Brunke S., Costanzo M.C.,
RA   Fitzpatrick D.A., de Groot P.W.J., Harris D., Hoyer L.L., Hube B.,
RA   Klis F.M., Kodira C., Lennard N., Logue M.E., Martin R., Neiman A.M.,
RA   Nikolaou E., Quail M.A., Quinn J., Santos M.C., Schmitzberger F.F.,
RA   Sherlock G., Shah P., Silverstein K.A.T., Skrzypek M.S., Soll D.,
RA   Staggs R., Stansfield I., Stumpf M.P.H., Sudbery P.E., Srikantha T.,
RA   Zeng Q., Berman J., Berriman M., Heitman J., Gow N.A.R., Lorenz M.C.,
RA   Birren B.W., Kellis M., Cuomo C.A.;
RT   "Evolution of pathogenicity and sexual reproduction in eight Candida
RT   genomes.";
RL   Nature 459:657-662(2009).
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. Removes ADP-ribose from glutamate residues in proteins
CC       bearing a single ADP-ribose moiety. Inactive towards proteins bearing
CC       poly-ADP-ribose (By similarity). {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; CH981528; EDK45545.1; -; Genomic_DNA.
DR   RefSeq; XP_001524692.1; XM_001524642.1.
DR   AlphaFoldDB; A5E287; -.
DR   SMR; A5E287; -.
DR   STRING; 379508.A5E287; -.
DR   EnsemblFungi; EDK45545; EDK45545; LELG_03724.
DR   GeneID; 5231778; -.
DR   KEGG; lel:LELG_03724; -.
DR   VEuPathDB; FungiDB:LELG_03724; -.
DR   eggNOG; ENOG502S60W; Eukaryota.
DR   HOGENOM; CLU_054419_1_2_1; -.
DR   InParanoid; A5E287; -.
DR   OMA; IFGVPWE; -.
DR   OrthoDB; 1416296at2759; -.
DR   Proteomes; UP000001996; Unassembled WGS sequence.
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..160
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324908"
FT   DOMAIN          1..160
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   BINDING         8..10
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         130..136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   160 AA;  17738 MW;  D566AB2777FCCCD8 CRC64;
     MTVKYIRGDL FTHSAPTGKS IVLAHACNTG GSWGGGIAAV FARKYPKANR QYSEYCHKNS
     HLLGTSLLLK ADDYDKSKAY IACLFTSDFN QSPEQIVKYT DQSLQELAKQ LKSLPIETQN
     GNQVVNMPKI NSGIFGVPWE NTEAVLDKLD SLDFNVYVID