POA1_PICGU
ID POA1_PICGU Reviewed; 175 AA.
AC A5DR03;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 67.
DE RecName: Full=ADP-ribose 1''-phosphate phosphatase;
DE EC=3.1.3.84;
GN Name=POA1; ORFNames=PGUG_05704;
OS Meyerozyma guilliermondii (strain ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539
OS / NBRC 10279 / NRRL Y-324) (Yeast) (Candida guilliermondii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Meyerozyma.
OX NCBI_TaxID=294746;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 6260 / CBS 566 / DSM 6381 / JCM 1539 / NBRC 10279 / NRRL Y-324;
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. {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; CH408162; EDK41606.2; -; Genomic_DNA.
DR RefSeq; XP_001481941.1; XM_001481891.1.
DR AlphaFoldDB; A5DR03; -.
DR SMR; A5DR03; -.
DR EnsemblFungi; EDK41606; EDK41606; PGUG_05704.
DR GeneID; 5123896; -.
DR KEGG; pgu:PGUG_05704; -.
DR VEuPathDB; FungiDB:PGUG_05704; -.
DR eggNOG; ENOG502S60W; Eukaryota.
DR HOGENOM; CLU_054419_1_2_1; -.
DR InParanoid; A5DR03; -.
DR OMA; IFGVPWE; -.
DR OrthoDB; 1416296at2759; -.
DR Proteomes; UP000001997; 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..175
FT /note="ADP-ribose 1''-phosphate phosphatase"
FT /id="PRO_0000324911"
FT DOMAIN 1..175
FT /note="Macro"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00490"
FT BINDING 9..11
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 147..153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 175 AA; 19225 MW; 9B080A26CF3F5598 CRC64;
MSKLNYIKGD LFSHKSSASS ILAHACNCRG SWGAGVAAIF KKQFPSTYKL YVEHCKKHAS
NPSGLLGSTY LIKSESSDPG NSGRENVAYV ACMFTSDAFG RRKNSADDIV ENTDKSMLHL
ESQLAELAKT EPIEQQDGVN VVNMPKINAG LFNVPWEETE AVLKKHQVLI NVYVI
