PDE1_SCHPO
ID PDE1_SCHPO Reviewed; 346 AA.
AC P36599;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 138.
DE RecName: Full=3',5'-cyclic-nucleotide phosphodiesterase;
DE Short=PDEase;
DE EC=3.1.4.17;
GN Name=cgs2; Synonyms=pde1; ORFNames=SPCC285.09c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1657594; DOI=10.1002/j.1460-2075.1991.tb04945.x;
RA Devoti J., Seydoux G., Beach D., McLeod M.;
RT "Interaction between ran1+ protein kinase and cAMP dependent protein kinase
RT as negative regulators of fission yeast meiosis.";
RL EMBO J. 10:3759-3768(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
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; S64907; AAB20315.1; -; Genomic_DNA.
DR EMBL; CU329672; CAA20848.1; -; Genomic_DNA.
DR PIR; S22442; S22442.
DR RefSeq; NP_588337.1; NM_001023328.2.
DR AlphaFoldDB; P36599; -.
DR SMR; P36599; -.
DR BioGRID; 275777; 54.
DR STRING; 4896.SPCC285.09c.1; -.
DR MaxQB; P36599; -.
DR PaxDb; P36599; -.
DR EnsemblFungi; SPCC285.09c.1; SPCC285.09c.1:pep; SPCC285.09c.
DR GeneID; 2539207; -.
DR KEGG; spo:SPCC285.09c; -.
DR PomBase; SPCC285.09c; cgs2.
DR VEuPathDB; FungiDB:SPCC285.09c; -.
DR eggNOG; ENOG502RFKK; Eukaryota.
DR HOGENOM; CLU_016658_2_0_1; -.
DR InParanoid; P36599; -.
DR OMA; FNWSAWP; -.
DR PhylomeDB; P36599; -.
DR PRO; PR:P36599; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IMP:PomBase.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IMP:PomBase.
DR GO; GO:0006198; P:cAMP catabolic process; ISM:PomBase.
DR GO; GO:0046069; P:cGMP catabolic process; IBA:GO_Central.
DR GO; GO:0106072; P:negative regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:0110034; P:negative regulation of adenylate cyclase-activating glucose-activated G protein-coupled receptor signaling pathway; IMP:PomBase.
DR GO; GO:1902660; P:negative regulation of glucose mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0051447; P:negative regulation of meiotic cell cycle; IMP:PomBase.
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; 2.
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; Reference proteome.
FT CHAIN 1..346
FT /note="3',5'-cyclic-nucleotide phosphodiesterase"
FT /id="PRO_0000206790"
SQ SEQUENCE 346 AA; 38650 MW; E3EAC5F7F191FA90 CRC64;
MHAALEIKEA EFQTDQVVGL VENSFTLYSL GQNGGPLESC CSSHLISDGA FQEIISLDGG
SHLSALVELI QSKHLSVDSW SSITKYDNYT VENESYAKAW HLSEQRIKTF LITHCHLDHI
YGAVINSAMF GPQNPRTIVG LNYVIDTLKK HVFNNLLWPS LDKAGFINFQ VVEPSMYTSL
TTTLSILPFP VNHGSSFGQE LKSSAFLFRN NLSDRYFLAF GDVEPDMVAS EPLNIHIWRA
CSSLIAQRKL SHILIECSTP DIPDTLLFGH FCPRHLVNEL CILQSLVQSY GVIMPTLTCL
LTHLKSHPLQ SANPADVILE QLESLSSKSS LSVTFKILQR GQFYKF
