PPME1_SCHPO
ID PPME1_SCHPO Reviewed; 341 AA.
AC Q9P7D2;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 25-MAY-2022, entry version 110.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN Name=ppe1; ORFNames=SPBP4H10.17c;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit
CC (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[phosphatase 2A protein]-C-terminal L-leucine methyl ester +
CC H2O = [phosphatase 2A protein]-C-terminal L-leucine + H(+) +
CC methanol; Xref=Rhea:RHEA:48548, Rhea:RHEA-COMP:12134, Rhea:RHEA-
CC COMP:12135, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790,
CC ChEBI:CHEBI:90516, ChEBI:CHEBI:90517; EC=3.1.1.89;
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; CU329671; CAB83175.1; -; Genomic_DNA.
DR RefSeq; NP_596191.1; NM_001022110.2.
DR AlphaFoldDB; Q9P7D2; -.
DR SMR; Q9P7D2; -.
DR BioGRID; 277882; 19.
DR STRING; 4896.SPBP4H10.17c.1; -.
DR ESTHER; schpo-ppme1; PPase_methylesterase_euk.
DR MaxQB; Q9P7D2; -.
DR PaxDb; Q9P7D2; -.
DR EnsemblFungi; SPBP4H10.17c.1; SPBP4H10.17c.1:pep; SPBP4H10.17c.
DR GeneID; 2541371; -.
DR KEGG; spo:SPBP4H10.17c; -.
DR PomBase; SPBP4H10.17c; -.
DR VEuPathDB; FungiDB:SPBP4H10.17c; -.
DR eggNOG; KOG2564; Eukaryota.
DR HOGENOM; CLU_024818_3_0_1; -.
DR InParanoid; Q9P7D2; -.
DR OMA; WHIRSRT; -.
DR PhylomeDB; Q9P7D2; -.
DR Reactome; R-SPO-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR PRO; PR:Q9P7D2; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0051722; F:protein C-terminal methylesterase activity; ISS:PomBase.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
DR GO; GO:1990748; P:cellular detoxification; IC:PomBase.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR GO; GO:0030091; P:protein repair; IC:PomBase.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR PANTHER; PTHR14189; PTHR14189; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..341
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000223669"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 153
FT /evidence="ECO:0000250"
FT ACT_SITE 178
FT /evidence="ECO:0000250"
FT ACT_SITE 304
FT /evidence="ECO:0000250"
SQ SEQUENCE 341 AA; 38092 MW; D1E1B8A428A42B78 CRC64;
MAFRKEELSQ TLYENESEQS SETKELMLNN EESLSDWRNY FDEKLTIPGE SGALNGTING
YLTLPQPDGC LLVLQHGAGS SAMSFAPVTQ ELLSNSDNKV GFLALDLRAH GETTLEPESD
MSLETLSKDF THAVSYVQRM FELDEKIILV GHSLGGAICA YCAFQKTIPN TSGLVVIDVV
EGTAMEALGF MKTYLSNRPT SFKSIDDAIS WHIKTLVTRN RLSACITVPS LLVQQEDGTF
VWRTDLYKTS PYWMDWFKGL SDKFLRAPYG RMLIVAGTDR LDKTLTIGQM QGKYQLEILP
ETGHFVHEDV PAKISSLLLN FWHRNQPLVL PPKVGATPVL Q
