ID   PPME1_ASHGO             Reviewed;         385 AA.
AC   Q74Z47;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 92.
DE   RecName: Full=Protein phosphatase methylesterase 1;
DE            Short=PME-1;
DE            EC=3.1.1.89;
GN   Name=PPE1; OrderedLocusNames=AGR359C;
OS   Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS   (Yeast) (Eremothecium gossypii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX   NCBI_TaxID=284811;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=15001715; DOI=10.1126/science.1095781;
RA   Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA   Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA   Gaffney T.D., Philippsen P.;
RT   "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT   cerevisiae genome.";
RL   Science 304:304-307(2004).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX   PubMed=23749448; DOI=10.1534/g3.112.002881;
RA   Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT   "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT   loci, numerous translocations, lack of transposons, and distinct gene
RT   duplications.";
RL   G3 (Bethesda) 3:1225-1239(2013).
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; AE016820; AAS54849.1; -; Genomic_DNA.
DR   RefSeq; NP_987025.1; NM_212087.1.
DR   AlphaFoldDB; Q74Z47; -.
DR   SMR; Q74Z47; -.
DR   STRING; 33169.AAS54849; -.
DR   ESTHER; ashgo-ppme1; PPase_methylesterase_euk.
DR   EnsemblFungi; AAS54849; AAS54849; AGOS_AGR359C.
DR   GeneID; 4623328; -.
DR   KEGG; ago:AGOS_AGR359C; -.
DR   eggNOG; KOG2564; Eukaryota.
DR   HOGENOM; CLU_024818_3_0_1; -.
DR   InParanoid; Q74Z47; -.
DR   OMA; WHIRSRT; -.
DR   Proteomes; UP000000591; Chromosome VII.
DR   GO; GO:0005763; C:mitochondrial small ribosomal subunit; IEA:EnsemblFungi.
DR   GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:EnsemblFungi.
DR   GO; GO:1990577; P:C-terminal protein demethylation; IEA:EnsemblFungi.
DR   GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
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..385
FT                   /note="Protein phosphatase methylesterase 1"
FT                   /id="PRO_0000223658"
FT   ACT_SITE        195
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        223
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        349
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   385 AA;  42841 MW;  539B1F7375683981 CRC64;
     MANNLQKQLF AKKFKDAEEV LRTMDDQGND AAPDTESDDL GELPAFGCGG IRPRRHASSM
     PVGDNDSWRK YFAVNEMFAI PERNFKFNTY YKLPQTTNAA SIPVFIMHHG AGSSGLTFAP
     LADELYTRLE GKCGIFSFDA RGHGETVPLD STLEVPYDLA TFTADFNAVI KTLQQRILQH
     KIPKEKLSIV LLGHSLGGSI CTTAFNAMES ALRSKVVGVA IFDIVEEAAI AALNNMSHHL
     ATTPTSFATM REAIEYYIEK GLSNLRSSAE VCVPALFHKT SRGKAVRITD LASFQKYWHT
     WFVGLSSRFV HLPTSKLLVL AGSDNLDKEL IIGQMQGKYQ LVVFQESGHF IQEDAPAKAA
     ITLIEFWRRN DNKNVVIKTN WGQWN