ID   PDE1_CANAX              Reviewed;         426 AA.
AC   P32782;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   25-MAY-2022, entry version 71.
DE   RecName: Full=3',5'-cyclic-nucleotide phosphodiesterase;
DE            Short=3':5'-CNP;
DE            Short=PDEase;
DE            EC=3.1.4.17;
GN   Name=PDE1;
OS   Candida albicans (Yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX   NCBI_TaxID=5476;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 11651 / B792 / 171D;
RX   PubMed=8075796; DOI=10.1099/13500872-140-7-1533;
RA   Hoyer L.L., Cieslinski L.B., McLaughlin M.M., Torphy T.J., Livi G.P.,
RA   Shatzman A.R.;
RT   "A Candida albicans cyclic nucleotide phosphodiesterase: cloning and
RT   expression in Saccharomyces cerevisiae and biochemical characterization of
RT   the recombinant enzyme.";
RL   Microbiology 140:1533-1542(1994).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a nucleoside 3',5'-cyclic phosphate + H2O = a nucleoside 5'-
CC         phosphate + H(+); Xref=Rhea:RHEA:14653, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57867, ChEBI:CHEBI:58464; EC=3.1.4.17;
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase class-II
CC       family. {ECO:0000305}.
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DR   EMBL; L12045; AAA34355.2; -; Genomic_DNA.
DR   AlphaFoldDB; P32782; -.
DR   SMR; P32782; -.
DR   VEuPathDB; FungiDB:C5_02290W_A; -.
DR   VEuPathDB; FungiDB:CAWG_04611; -.
DR   GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0006198; P:cAMP catabolic process; IEA:InterPro.
DR   CDD; cd07735; class_II_PDE_MBL-fold; 1.
DR   Gene3D; 3.60.15.10; -; 1.
DR   InterPro; IPR024225; cAMP-PdiesteraseII_CS.
DR   InterPro; IPR000396; Pdiesterase2.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   PANTHER; PTHR28283; PTHR28283; 1.
DR   Pfam; PF02112; PDEase_II; 1.
DR   PIRSF; PIRSF000962; Cyc_nuc_PDEase; 1.
DR   PRINTS; PR00388; PDIESTERASE2.
DR   SUPFAM; SSF56281; SSF56281; 1.
DR   PROSITE; PS00607; PDEASE_II; 1.
PE   3: Inferred from homology;
KW   cAMP; Hydrolase.
FT   CHAIN           1..426
FT                   /note="3',5'-cyclic-nucleotide phosphodiesterase"
FT                   /id="PRO_0000206789"
FT   REGION          210..229
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   426 AA;  47982 MW;  A6F4581F2D2CEC75 CRC64;
     MSFEITILGS SGGPLEGSTC SILLKPANIS YHDIINDNLP DQVLCIDAGS GMGKLTEIIH
     QETTTKTSYC NFLQYYPDCE TVSYYYHPNV TITTPFSNFQ PGRPILHTQN IFNNLQNYLI
     SHSHLDHVCS VVINSAGFNK NMSNKILYGS HYTINAMQQH LFNGKVWPNM PSFKIVNLNY
     LESNRSERIG IYTVKMFDLS HGEFNKLTED KEDAQHHSNS NSNSNNIWGK RYDRRRSSIT
     TIPQNTSGLI IKNSEALNHH YLSSAFLITL EVPCTTKEPP PSILVFGDFE SDLTSKLSRN
     LFIWKSIASL ILRNQLKAIV LECSNCKEIA ANELYGHLTP KLLIYELKQL EHECKQLDTA
     TTSTEQPLLG LNVIVNHVKE PIADPNQESQ LHDPRKRILA ELNKLNEIEK LGCNISIALS
     GTSIIV