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Protein

Protein phosphatase methylesterase 1

Gene

ppe1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Demethylates proteins that have been reversibly carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit (By similarity).By similarity

Catalytic activityi

[Phosphatase 2A protein]-leucine methyl ester + H2O = [phosphatase 2A protein]-leucine + methanol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei153 – 1531By similarity
Active sitei178 – 1781By similarity
Active sitei304 – 3041By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Serine esterase

Protein family/group databases

ESTHERischpo-ppme1. PPase_methylesterase_euk.
MEROPSiS33.A38.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein phosphatase methylesterase 1 (EC:3.1.1.89)
Short name:
PME-1
Gene namesi
Name:ppe1
ORF Names:SPBP4H10.17c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBP4H10.17c.
PomBaseiSPBP4H10.17c.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 341341Protein phosphatase methylesterase 1PRO_0000223669Add
BLAST

Proteomic databases

MaxQBiQ9P7D2.

Interactioni

Protein-protein interaction databases

BioGridi277882. 19 interactions.
MINTiMINT-4705204.

Structurei

3D structure databases

ProteinModelPortaliQ9P7D2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AB hydrolase superfamily.Curated

Phylogenomic databases

HOGENOMiHOG000212435.
InParanoidiQ9P7D2.
KOiK13617.
OMAiELMVGQM.
PhylomeDBiQ9P7D2.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR016812. PPase_methylesterase_euk.
[Graphical view]
PANTHERiPTHR14189. PTHR14189. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF022950. PPase_methylesterase_euk. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9P7D2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAFRKEELSQ TLYENESEQS SETKELMLNN EESLSDWRNY FDEKLTIPGE
60 70 80 90 100
SGALNGTING YLTLPQPDGC LLVLQHGAGS SAMSFAPVTQ ELLSNSDNKV
110 120 130 140 150
GFLALDLRAH GETTLEPESD MSLETLSKDF THAVSYVQRM FELDEKIILV
160 170 180 190 200
GHSLGGAICA YCAFQKTIPN TSGLVVIDVV EGTAMEALGF MKTYLSNRPT
210 220 230 240 250
SFKSIDDAIS WHIKTLVTRN RLSACITVPS LLVQQEDGTF VWRTDLYKTS
260 270 280 290 300
PYWMDWFKGL SDKFLRAPYG RMLIVAGTDR LDKTLTIGQM QGKYQLEILP
310 320 330 340
ETGHFVHEDV PAKISSLLLN FWHRNQPLVL PPKVGATPVL Q
Length:341
Mass (Da):38,092
Last modified:October 1, 2000 - v1
Checksum:iD1E1B8A428A42B78
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB83175.1.
RefSeqiNP_596191.1. NM_001022110.2.

Genome annotation databases

EnsemblFungiiSPBP4H10.17c.1; SPBP4H10.17c.1:pep; SPBP4H10.17c.
GeneIDi2541371.
KEGGispo:SPBP4H10.17c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329671 Genomic DNA. Translation: CAB83175.1.
RefSeqiNP_596191.1. NM_001022110.2.

3D structure databases

ProteinModelPortaliQ9P7D2.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277882. 19 interactions.
MINTiMINT-4705204.

Protein family/group databases

ESTHERischpo-ppme1. PPase_methylesterase_euk.
MEROPSiS33.A38.

Proteomic databases

MaxQBiQ9P7D2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBP4H10.17c.1; SPBP4H10.17c.1:pep; SPBP4H10.17c.
GeneIDi2541371.
KEGGispo:SPBP4H10.17c.

Organism-specific databases

EuPathDBiFungiDB:SPBP4H10.17c.
PomBaseiSPBP4H10.17c.

Phylogenomic databases

HOGENOMiHOG000212435.
InParanoidiQ9P7D2.
KOiK13617.
OMAiELMVGQM.
PhylomeDBiQ9P7D2.

Miscellaneous databases

NextBioi20802480.
PROiQ9P7D2.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR016812. PPase_methylesterase_euk.
[Graphical view]
PANTHERiPTHR14189. PTHR14189. 1 hit.
PfamiPF12697. Abhydrolase_6. 1 hit.
[Graphical view]
PIRSFiPIRSF022950. PPase_methylesterase_euk. 1 hit.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.
    , 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 nameiPPME1_SCHPO
AccessioniPrimary (citable) accession number: Q9P7D2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: October 1, 2000
Last modified: November 11, 2015
This is version 83 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

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 one 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.