Skip Header

Contribute Send feedback
Read comments (?) or add your own

P87118 (IPYR2_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative inorganic pyrophosphatase C3A12.02
EC=3.6.1.1
Alternative name(s):
Pyrophosphate phosphohydrolase
Short name=PPase
Gene names
ORF Names:SPAC3A12.02
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

Diphosphate + H2O = 2 phosphate.

Cofactor

Binds 4 magnesium ions per subunit. Other metal ions can support activity, but at a lower rate. Two magnesium ions are required for the activation of the enzyme and are present before substrate binds, two additional magnesium ions form complexes with substrate and product By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the PPase family.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processaerobic respiration

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

phosphate-containing compound metabolic process

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

   Cellular componentmitochondrion

Inferred from direct assay. Source: GeneDB_Spombe

   Molecular functioninorganic diphosphatase activity

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

magnesium ion binding

Inferred from sequence or structural similarity. Source: GeneDB_Spombe

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Putative inorganic pyrophosphatase C3A12.02
PRO_0000137590

Sites

Metal binding1221Magnesium 1 By similarity
Metal binding1271Magnesium 1 By similarity
Metal binding1271Magnesium 2 By similarity
Metal binding1591Magnesium 1 By similarity
Binding site851Diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P87118 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: FBE4A7EEF9132212

FASTA28632,899
        10         20         30         40         50         60 
MASLAKNILQ FRSKITGKLN TPDFRVYCYK NNKPISFFHD VPLTSDKDTF NMVTEIPRWT 

        70         80         90        100        110        120 
QAKCEISLTS PFHPIKQDLK NGKLRYVANS FPYHGFIWNY GALPQTWEDP NVIDSRTKMK 

       130        140        150        160        170        180 
GDGDPLDVCE IGGSIGYIGQ IKQVKVLGAL GLIDQGETDW KILAIDINDP RAKLLNDISD 

       190        200        210        220        230        240 
VQNLMPRLLP CTRDWFAIYK IPDGKPKNRF FFDGNYLPKS DALDIIAQCH QHWKVSRDRK 

       250        260        270        280 
QYIKNFHNES VNNVDLINKI NSLKEEVSQN VSNYPSFPYF HTIPNL

« Hide

References

[1]"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. expand/collapse author list , 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: 11859360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAB08747.1.
PIRT38670.
RefSeqNP_593328.1. NM_001018759.1.

3D structure databases

ProteinModelPortalP87118.
SMRP87118. Positions 11-238.
ModBaseSearch...

Protein-protein interaction databases

STRINGP87118.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC3A12.02.1; SPAC3A12.02.1:pep; SPAC3A12.02.
GeneID2542957.
KEGGspo:SPAC3A12.02.
NMPDRfig|4896.1.peg.3298.

Organism-specific databases

GeneDB_SpombeSPAC3A12.02.

Phylogenomic databases

eggNOGfuNOG04419.
GeneTreeEFGT00050000006068.
HOGENOMHBG434750.
OMAMIDEGEM.
OrthoDBEOG486CPK.

Enzyme and pathway databases

BioCycSPOM-XXX-01:SPOM-XXX-01-001024-MONOMER.

Gene expression databases

ArrayExpressP87118.

Family and domain databases

InterProIPR008162. Pyrophosphatase.
[Graphical view]
Gene3DG3DSA:3.90.80.10. Pyrophosphatase. 1 hit.
KOK01507.
PANTHERPTHR10286. Pyrophosphatase. 1 hit.
PfamPF00719. Pyrophosphatase. 1 hit.
[Graphical view]
SUPFAMSSF50324. Pyrophosphatase. 1 hit.
PROSITEPS00387. PPASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameIPYR2_SCHPO
AccessionPrimary (citable) accession number: P87118
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: December 14, 2011
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents