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O43049 (PPT1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Serine/threonine-protein phosphatase T
Short name=PPT
EC=3.1.3.16
Gene names
Name:ppt1
ORF Names:SPBC3F6.01c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length473 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90. Dephosphorylation positively regulates the Hsp90 chaperone machinery By similarity.

Catalytic activity

A phosphoprotein + H2O = a protein + phosphate.

Cofactor

Binds 1 iron ion per subunit By similarity.

Binds 1 manganese ion per subunit By similarity.

Subcellular location

Nucleus By similarity.

Domain

The TPR repeats mediate protein-protein interactions with substrate proteins, but also autoinhibit PPT phosphatase activity By similarity.

Sequence similarities

Belongs to the PPP phosphatase family. PP-5 (PP-T) subfamily.

Contains 3 TPR repeats.

Ontologies

Keywords
   Cellular componentNucleus
   DomainRepeat
TPR repeat
   LigandIron
Manganese
Metal-binding
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein dephosphorylation

Inferred from sequence orthology. Source: PomBase

signal transduction

Non-traceable author statement. Source: PomBase

   Cellular_componentcytoplasm

Inferred from sequence orthology. Source: PomBase

nucleus

Inferred from sequence orthology. Source: PomBase

protein complex

Non-traceable author statement. Source: PomBase

   Molecular_functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein serine/threonine phosphatase activity

Inferred from sequence orthology. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 473473Serine/threonine-protein phosphatase T
PRO_0000363378

Regions

Repeat5 – 3834TPR 1
Repeat40 – 7233TPR 2
Repeat73 – 10634TPR 3
Region159 – 472314Catalytic By similarity

Sites

Active site2791Proton donor By similarity
Metal binding2171Iron By similarity
Metal binding2191Iron By similarity
Metal binding2461Iron By similarity
Metal binding2461Manganese By similarity
Metal binding2781Manganese By similarity
Metal binding3271Manganese By similarity
Metal binding4041Manganese By similarity

Sequences

Sequence LengthMass (Da)Tools
O43049 [UniParc].

Last modified May 1, 1999. Version 2.
Checksum: 752AB4B13E1702FC

FASTA47353,291
        10         20         30         40         50         60 
MAKEALELKN EANKFLKEGH IVQAIDLYTK AIELDSTNAI LYSNRSLAHL KSEDYGLAIN 

        70         80         90        100        110        120 
DASKAIECDP EYAKAYFRRA TAHIAIFQPK EAVGDFRKAL ALAPSDPAAR KKLRECEQLV 

       130        140        150        160        170        180 
KRIRFQEAIH NTEPPSPLAN INIEDMDIPS DYDGVILEKQ ITKEFVEDMK ERFCQGKKLP 

       190        200        210        220        230        240 
LKFAYSILRD LKELLEKTPS LIDIPVKGDE TLVICGDTHG QYFDLLNIFK LHGPPSPTNK 

       250        260        270        280        290        300 
YLFNGDFVDR GSWSTEVAFT LYAYKLLYPD AVFINRGNHE TDDMNKVYGF EGECRSKYNE 

       310        320        330        340        350        360 
RTFNIFSETF SLLPLGSLIS DSYLVVHGGL FSDDNVTLDQ LRNIDRFSKK QPGQSGLMME 

       370        380        390        400        410        420 
MLWTDPQPAP GRGPSKRGVG LQFGPDVSKR FCEANGLKAV IRSHEVRDQG YEVEHDGYCI 

       430        440        450        460        470 
TVFSAPNYCD STGNLGAVIK VKEDMELDFH QFEAVPHPNI RPMAYANGLL SGM

« 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAA17690.2.
PIRT40391.
RefSeqNP_596740.1. NM_001022666.2.

3D structure databases

HSSPHSSP built from PDB template 1S95 based on UniProtKB P53041.
ProteinModelPortalO43049.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPBC3F6.01c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC3F6.01c.1; SPBC3F6.01c.1:pep; SPBC3F6.01c.
GeneID2541004.
KEGGspo:SPBC3F6.01c.

Organism-specific databases

PomBaseSPBC3F6.01c.

Phylogenomic databases

eggNOGCOG0639.
HOGENOMHOG000172698.
KOK04460.
OMAGERTECA.
OrthoDBEOG4BZR9Z.

Family and domain databases

Gene3D1.25.40.10. 1 hit.
InterProIPR004843. Metallo_PEstase_dom.
IPR013235. PPP_dom.
IPR006186. Ser/Thr-sp_prot-phosphatase.
IPR011236. Ser/Thr_PPase_5.
IPR001440. TPR-1.
IPR013026. TPR-contain_dom.
IPR011990. TPR-like_helical.
IPR019734. TPR_repeat.
[Graphical view]
PANTHERPTHR11668:SF12. PTHR11668:SF12. 1 hit.
PfamPF00149. Metallophos. 1 hit.
PF08321. PPP5. 1 hit.
PF00515. TPR_1. 1 hit.
[Graphical view]
PIRSFPIRSF033096. PPPtase_5. 1 hit.
PRINTSPR00114. STPHPHTASE.
SMARTSM00156. PP2Ac. 1 hit.
SM00028. TPR. 3 hits.
[Graphical view]
PROSITEPS00125. SER_THR_PHOSPHATASE. 1 hit.
PS50005. TPR. 3 hits.
PS50293. TPR_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802118.

Entry information

Entry namePPT1_SCHPO
AccessionPrimary (citable) accession number: O43049
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 103 of the entry and version 2 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

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