ID   PPME1_CANGA             Reviewed;         386 AA.
AC   Q6FNL6;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Protein phosphatase methylesterase 1;
DE            Short=PME-1;
DE            EC=3.1.1.89;
GN   Name=PPE1; OrderedLocusNames=CAGL0J10736g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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; CR380956; CAG61129.1; -; Genomic_DNA.
DR   RefSeq; XP_448178.1; XM_448178.1.
DR   AlphaFoldDB; Q6FNL6; -.
DR   SMR; Q6FNL6; -.
DR   STRING; 5478.XP_448178.1; -.
DR   ESTHER; canga-ppme1; PPase_methylesterase_euk.
DR   PRIDE; Q6FNL6; -.
DR   EnsemblFungi; CAG61129; CAG61129; CAGL0J10736g.
DR   GeneID; 2889616; -.
DR   KEGG; cgr:CAGL0J10736g; -.
DR   CGD; CAL0133726; CAGL0J10736g.
DR   VEuPathDB; FungiDB:CAGL0J10736g; -.
DR   eggNOG; KOG2564; Eukaryota.
DR   HOGENOM; CLU_024818_3_0_1; -.
DR   InParanoid; Q6FNL6; -.
DR   OMA; WHIRSRT; -.
DR   Proteomes; UP000002428; Chromosome J.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; IEA:EnsemblFungi.
DR   GO; GO:0051723; F:protein methylesterase activity; IEA:InterPro.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:EnsemblFungi.
DR   GO; GO:1990577; P:C-terminal protein demethylation; IEA:EnsemblFungi.
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..386
FT                   /note="Protein phosphatase methylesterase 1"
FT                   /id="PRO_0000223662"
FT   REGION          20..48
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        194
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        222
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        348
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   386 AA;  43659 MW;  5A173BF7D0736E70 CRC64;
     MGDDLKRKIL LHNLSSNNPI LEKLKGGQEP NSNEEGSDSI GDLPSLKNDY KRQDNNSTNC
     TYIPPSQWNT YFRSNEHIKV QSRNIEFNTY YTVPSSILGP SLPVFIFHHG AGSSGLSFAN
     LARNLGDQLN NNCCCLSFDA RGHGGTKFID AKQAQNYFRD DFVDDFHTLV EYFVSEKLKH
     LPTEKLSIIF IGHSLGGSIC TFTYSKLSIE LKKQVIGVAM FDIVEEAATL ALEKVNHFLQ
     VTPNMFSGYE EAIDWHVSHE LSRLRESADI AIPALFKSTE SGKVVRITNL ETFRPFWRTW
     FSDLSKSFVS LPTCKLLILA GNDNLDRELI IGQMQGKYQL VVFQDSGHFI QEDTPRKTAL
     TLVDFWKRND NKNVVIKSNW GSSNKV