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Protein

3',5'-cyclic-nucleotide phosphodiesterase

Gene

cgs2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

Nucleoside 3',5'-cyclic phosphate + H2O = nucleoside 5'-phosphate.

GO - Molecular functioni

  1. 3',5'-cyclic-AMP phosphodiesterase activity Source: PomBase

GO - Biological processi

  1. cAMP catabolic process Source: PomBase
  2. cellular response to glucose stimulus Source: PomBase
  3. cellular response to nitrogen starvation Source: PomBase
  4. negative regulation of adenylate cyclase activity Source: PomBase
  5. negative regulation of cAMP biosynthetic process Source: PomBase
  6. positive regulation of transcription from RNA polymerase II promoter Source: PomBase
  7. regulation of cAMP-mediated signaling Source: PomBase
  8. regulation of signal transduction involved in conjugation with cellular fusion Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

cAMP

Names & Taxonomyi

Protein namesi
Recommended name:
3',5'-cyclic-nucleotide phosphodiesterase (EC:3.1.4.17)
Short name:
PDEase
Gene namesi
Name:cgs2
Synonyms:pde1
ORF Names:SPCC285.09c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome III

Organism-specific databases

PomBaseiSPCC285.09c.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 3463463',5'-cyclic-nucleotide phosphodiesterasePRO_0000206790Add
BLAST

Proteomic databases

MaxQBiP36599.

Interactioni

Protein-protein interaction databases

BioGridi275777. 44 interactions.
MINTiMINT-4688853.
STRINGi4896.SPCC285.09c-1.

Structurei

3D structure databases

ProteinModelPortaliP36599.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5212.
InParanoidiP36599.
KOiK01120.
OMAiNVIVTHV.
OrthoDBiEOG7X6MB3.
PhylomeDBiP36599.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
IPR024225. cAMP-PdiesteraseII_CS.
IPR000396. Pdiesterase2.
[Graphical view]
PfamiPF02112. PDEase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF000962. Cyc_nuc_PDEase. 1 hit.
PRINTSiPR00388. PDIESTERASE2.
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00607. PDEASE_II. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P36599-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHAALEIKEA EFQTDQVVGL VENSFTLYSL GQNGGPLESC CSSHLISDGA
60 70 80 90 100
FQEIISLDGG SHLSALVELI QSKHLSVDSW SSITKYDNYT VENESYAKAW
110 120 130 140 150
HLSEQRIKTF LITHCHLDHI YGAVINSAMF GPQNPRTIVG LNYVIDTLKK
160 170 180 190 200
HVFNNLLWPS LDKAGFINFQ VVEPSMYTSL TTTLSILPFP VNHGSSFGQE
210 220 230 240 250
LKSSAFLFRN NLSDRYFLAF GDVEPDMVAS EPLNIHIWRA CSSLIAQRKL
260 270 280 290 300
SHILIECSTP DIPDTLLFGH FCPRHLVNEL CILQSLVQSY GVIMPTLTCL
310 320 330 340
LTHLKSHPLQ SANPADVILE QLESLSSKSS LSVTFKILQR GQFYKF
Length:346
Mass (Da):38,650
Last modified:June 1, 1994 - v1
Checksum:iE3EAC5F7F191FA90
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S64907 Genomic DNA. Translation: AAB20315.1.
CU329672 Genomic DNA. Translation: CAA20848.1.
PIRiS22442.
RefSeqiNP_588337.1. NM_001023328.2.

Genome annotation databases

EnsemblFungiiSPCC285.09c.1; SPCC285.09c.1:pep; SPCC285.09c.
GeneIDi2539207.
KEGGispo:SPCC285.09c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S64907 Genomic DNA. Translation: AAB20315.1.
CU329672 Genomic DNA. Translation: CAA20848.1.
PIRiS22442.
RefSeqiNP_588337.1. NM_001023328.2.

3D structure databases

ProteinModelPortaliP36599.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275777. 44 interactions.
MINTiMINT-4688853.
STRINGi4896.SPCC285.09c-1.

Proteomic databases

MaxQBiP36599.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC285.09c.1; SPCC285.09c.1:pep; SPCC285.09c.
GeneIDi2539207.
KEGGispo:SPCC285.09c.

Organism-specific databases

PomBaseiSPCC285.09c.

Phylogenomic databases

eggNOGiCOG5212.
InParanoidiP36599.
KOiK01120.
OMAiNVIVTHV.
OrthoDBiEOG7X6MB3.
PhylomeDBiP36599.

Miscellaneous databases

NextBioi20800377.

Family and domain databases

Gene3Di3.60.15.10. 1 hit.
InterProiIPR001279. Beta-lactamas-like.
IPR024225. cAMP-PdiesteraseII_CS.
IPR000396. Pdiesterase2.
[Graphical view]
PfamiPF02112. PDEase_II. 1 hit.
[Graphical view]
PIRSFiPIRSF000962. Cyc_nuc_PDEase. 1 hit.
PRINTSiPR00388. PDIESTERASE2.
SUPFAMiSSF56281. SSF56281. 1 hit.
PROSITEiPS00607. PDEASE_II. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Interaction between ran1+ protein kinase and cAMP dependent protein kinase as negative regulators of fission yeast meiosis."
    Devoti J., Seydoux G., Beach D., McLeod M.
    EMBO J. 10:3759-3768(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.

Entry informationi

Entry nameiPDE1_SCHPO
AccessioniPrimary (citable) accession number: P36599
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: January 7, 2015
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.