ID   PPME1_YARLI             Reviewed;         419 AA.
AC   Q6CGE1;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Protein phosphatase methylesterase 1;
DE            Short=PME-1;
DE            EC=3.1.1.89;
GN   Name=PPE1; OrderedLocusNames=YALI0A20086g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382127; CAG84209.1; -; Genomic_DNA.
DR   RefSeq; XP_500271.1; XM_500271.1.
DR   AlphaFoldDB; Q6CGE1; -.
DR   SMR; Q6CGE1; -.
DR   STRING; 4952.CAG84209; -.
DR   ESTHER; yarli-ppme1; PPase_methylesterase_euk.
DR   MEROPS; S33.B12; -.
DR   EnsemblFungi; CAG84209; CAG84209; YALI0_A20086g.
DR   GeneID; 2906043; -.
DR   KEGG; yli:YALI0A20086g; -.
DR   VEuPathDB; FungiDB:YALI0_A20086g; -.
DR   HOGENOM; CLU_024818_3_1_1; -.
DR   InParanoid; Q6CGE1; -.
DR   OMA; WHIRSRT; -.
DR   Proteomes; UP000001300; Chromosome A.
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..419
FT                   /note="Protein phosphatase methylesterase 1"
FT                   /id="PRO_0000223670"
FT   REGION          1..75
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..52
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        230
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        256
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        383
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   419 AA;  46200 MW;  AFE3EA8D52E627D4 CRC64;
     MSQLHRGMHK KPGMFPPKEV LEEVDAGSGS DTETEETVEC TEEEEEQDET DGLGDLGMPP
     PKKTTKSAAS PTVPAPALIP SLSHLIGLEG KQPSRKYAPA EWPQYFKQKI SVARDNDTFN
     VLYTPPDDSE APVYVFHHGA GSCAESFALL SVRLREMMHE ERFQLAATAK IRDENKLPGM
     IAFDARGHGF TEVESTDYSL EAFTNDFAFI VANVVAEFGL TNNLILVGHS LGGAVVTNAC
     HLKLIQHPVI GLAVLDVVEG TAIESLASMQ QILNSRPKSF PTVEKGIEWT VQSHTIRNRE
     SACVSVPPTL ISQHDGPGMT WRTDLMLTKP YWKGWFTGLS EKFISCAPAK LLILAGTDRL
     DKDLMVGQMQ GKYQLIVFQE SGHFVQEDAP DKTALSLIDF WKRNDKVNKT VPLFGAFRA