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O14094 (PPX1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 74. 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

Names and origin

Protein namesRecommended name:
Putative exopolyphosphatase

Short name=ExopolyPase
EC=3.6.1.11
Alternative name(s):
Metaphosphatase
Gene names
ORF Names:SPAC2F3.11
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

Sequence length384 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Degradation of inorganic polyphosphates By similarity.

Catalytic activity

(Polyphosphate)(n) + H2O = (polyphosphate)(n-1) + phosphate.

Cofactor

Binds 2 manganese ions per subunit Potential.

Sequence similarities

Belongs to the PPase class C family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 384384Putative exopolyphosphatase
PRO_0000158600

Sites

Metal binding401Manganese 1 By similarity
Metal binding421Manganese 2 By similarity
Metal binding1161Manganese 1 By similarity
Metal binding1161Manganese 2 By similarity
Metal binding1381Manganese 2 By similarity
Metal binding2001Manganese 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
O14094 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 643CC43C7AF185EA

FASTA38443,297
        10         20         30         40         50         60 
MKLGRFLENG REQIRNLLLN ASTVSSAPSF SFVSGNESAD LDSCASSIVY AYCLQRKQLG 

        70         80         90        100        110        120 
RIVVPFFNIP RKELRLRPEL SYLLNLASIS SDDIVFLDDI VKLPKRIFSN PIYLVDHNSL 

       130        140        150        160        170        180 
DRKDLENFNG SIAGIIDHHK DEGGSLHADP RIIEECGSCC TLVCRYFMPV IRSLYDSKVS 

       190        200        210        220        230        240 
ELHQTATNLA VLALGPILID TGNLKNEKTT DTDVKIVNDL CSFVPKDWVR DEFFDTLKEK 

       250        260        270        280        290        300 
KKSCKGFSFD DLLRRDLKQY FPDGIVVNYA SVGKGLDWIK KKRLGWEDEL KSFAEVQNSD 

       310        320        330        340        350        360 
LVIVGLSLSK NDEFGRQLIL YKRTERGAGL ADSFLKLSKQ NLGLEIIEEK DNGDLSMWNQ 

       370        380 
RNSAASRKKV VPLLMDSVKQ VASK 

« 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] [Europe PMC] [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: CAB16267.1.
PIRT38544.
RefSeqNP_594390.1. NM_001019812.2.

3D structure databases

ProteinModelPortalO14094.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278344. 42 interactions.
MINTMINT-4670429.
STRING4896.SPAC2F3.11-1.

Proteomic databases

PaxDbO14094.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC2F3.11.1; SPAC2F3.11.1:pep; SPAC2F3.11.
GeneID2541853.
KEGGspo:SPAC2F3.11.

Organism-specific databases

PomBaseSPAC2F3.11.

Phylogenomic databases

eggNOGCOG1227.
KOK01514.
OMAWILVDHN.
OrthoDBEOG7FNCH9.
PhylomeDBO14094.

Family and domain databases

InterProIPR004097. DHHA2.
IPR001667. Pesterase_RecJ.
[Graphical view]
PfamPF01368. DHH. 1 hit.
PF02833. DHHA2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802941.
PROO14094.

Entry information

Entry namePPX1_SCHPO
AccessionPrimary (citable) accession number: O14094
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 74 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names