ID   PPME1_DEBHA             Reviewed;         390 AA.
AC   Q6BZG3;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Protein phosphatase methylesterase 1;
DE            Short=PME-1;
DE            EC=3.1.1.89;
GN   Name=PPE1; OrderedLocusNames=DEHA2A01562g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
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; CR382133; CAG84358.2; -; Genomic_DNA.
DR   RefSeq; XP_456406.2; XM_456406.1.
DR   AlphaFoldDB; Q6BZG3; -.
DR   SMR; Q6BZG3; -.
DR   STRING; 4959.XP_456406.2; -.
DR   ESTHER; debha-ppme1; PPase_methylesterase_euk.
DR   EnsemblFungi; CAG84358; CAG84358; DEHA2A01562g.
DR   GeneID; 2899326; -.
DR   KEGG; dha:DEHA2A01562g; -.
DR   VEuPathDB; FungiDB:DEHA2A01562g; -.
DR   eggNOG; KOG2564; Eukaryota.
DR   HOGENOM; CLU_024818_3_1_1; -.
DR   InParanoid; Q6BZG3; -.
DR   OMA; WHIRSRT; -.
DR   OrthoDB; 911863at2759; -.
DR   Proteomes; UP000000599; Chromosome A.
DR   GO; GO:0051723; F:protein methylesterase activity; IEA:InterPro.
DR   GO; GO:0006482; P:protein demethylation; IEA:InterPro.
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..390
FT                   /note="Protein phosphatase methylesterase 1"
FT                   /id="PRO_0000223664"
FT   DOMAIN          100..332
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   REGION          19..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        26..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        186
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        213
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        346
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   390 AA;  44250 MW;  D79D5F2989C12DC0 CRC64;
     MSGLHKQFLK KIKEQERAFG LSSLSEDPDE SESNSNYFSP TPQPPNELRT DINEERHGHI
     RETYNDTKRD VFPIADIYTD PRSGVRFQTY FKPPSSSNAP IFICHHGAGS SSMTFCKLAQ
     SLDNEYGKNN EYPGLFTYDM RGHGDSSTTI PPDYSLATIT NDCEFIIDEF HAKHALRSSI
     YLLGHSLGGS VLTSYLVANP DNAYKFKGLI VLDIVEETAI KALSAMPQFV RKRPTTFGDY
     QEAIDWHIKE SHLLHSEESA LVSVPDLLRE CPNGLIWKTN LQETEPFWET WFTGLSENFI
     NCGKTQHIAK LLVLSGHETL DTNLIIGQMQ GKYQLIVFNN TQNTGHFIQE DIPTQISISL
     VDFVRRNDSP NEYMKKEFGF VPKWGGKIHD