ID   POA1_NEOFI              Reviewed;         200 AA.
AC   A1D1B7;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE            EC=3.1.3.84;
GN   Name=poa1; ORFNames=NFIA_008880;
OS   Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164
OS   / JCM 1740 / NRRL 181 / WB 181) (Aspergillus fischerianus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=331117;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 1020 / DSM 3700 / CBS 544.65 / FGSC A1164 / JCM 1740 / NRRL 181
RC   / WB 181;
RX   PubMed=18404212; DOI=10.1371/journal.pgen.1000046;
RA   Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J.,
RA   Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H.,
RA   Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M.,
RA   Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J.,
RA   Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C.,
RA   White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H.,
RA   Wortman J.R., Jiang B., Denning D.W., Nierman W.C.;
RT   "Genomic islands in the pathogenic filamentous fungus Aspergillus
RT   fumigatus.";
RL   PLoS Genet. 4:E1000046-E1000046(2008).
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; DS027688; EAW22210.1; -; Genomic_DNA.
DR   RefSeq; XP_001264107.1; XM_001264106.1.
DR   AlphaFoldDB; A1D1B7; -.
DR   SMR; A1D1B7; -.
DR   STRING; 36630.CADNFIAP00001715; -.
DR   EnsemblFungi; EAW22210; EAW22210; NFIA_008880.
DR   GeneID; 4591214; -.
DR   KEGG; nfi:NFIA_008880; -.
DR   VEuPathDB; FungiDB:NFIA_008880; -.
DR   eggNOG; ENOG502S60W; Eukaryota.
DR   HOGENOM; CLU_054419_1_0_1; -.
DR   OMA; NCQGSWG; -.
DR   OrthoDB; 1416296at2759; -.
DR   Proteomes; UP000006702; 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..200
FT                   /note="ADP-ribose 1''-phosphate phosphatase"
FT                   /id="PRO_0000324909"
FT   DOMAIN          1..200
FT                   /note="Macro"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT   BINDING         15..17
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         29..31
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         36..41
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         169..175
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   200 AA;  21975 MW;  1F92A29BF145BFD4 CRC64;
     MDLPSVQSKI TEIEGDLFHA PDGAALIHAC NCQGSWGKGI AKAFKDKYPA AFAIYRSHCQ
     NLLSSPRYRF EPAVQSEESH ARSSRGVQLP EGTALIIPPQ KRDSEANGKK HWIICLFTSR
     GFGRAVSPPD VIVRNTELAV ADMTRQLAEL QAGQSSEEES VEELWSCRFN AGLFGVPWER
     SRTVLEDAGL EVTVVRPHGG