ID   PPME1_ASPOR             Reviewed;         427 AA.
AC   Q2URJ0; Q2URJ1;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 2.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=Protein phosphatase methylesterase 1;
DE            Short=PME-1;
DE            EC=3.1.1.89;
GN   Name=ppe1; ORFNames=AO090005000808/AO090005000809;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
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   -!- SEQUENCE CAUTION:
CC       Sequence=BAE55824.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAE55825.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AP007151; BAE55824.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AP007151; BAE55825.1; ALT_SEQ; Genomic_DNA.
DR   AlphaFoldDB; Q2URJ0; -.
DR   SMR; Q2URJ0; -.
DR   STRING; 510516.Q2URJ0; -.
DR   ESTHER; aspor-ppme1; PPase_methylesterase_euk.
DR   EnsemblFungi; BAE55825; BAE55825; AO090005000809.
DR   Proteomes; UP000006564; Chromosome 1.
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   SUPFAM; SSF53474; SSF53474; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome; Serine esterase.
FT   CHAIN           1..427
FT                   /note="Protein phosphatase methylesterase 1"
FT                   /id="PRO_0000223660"
FT   REGION          1..49
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          402..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        207
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        233
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        364
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   427 AA;  46896 MW;  C335D29965B42C3F CRC64;
     MSELQKSFAK AKLAKLPPEA PPFSMHPPRD EDDSESASST GTVVPSPSRQ LFARSRGSTC
     GVIFRLLAIL THPRSNSVET LNWTDFFTQE LFLIQETDSA RITHHVYLTP PTNSGPLFVM
     HHGAGSSGLS FATCAEEIRK ILPKAGILSI DARDHGQTST YTETGEGKVE LDLSLETLNR
     DLVFIVRETQ SKMGWESLPD IVLVGHSLGG AVITDVAKKG ELGPKVLAYA VLDVVEGSAM
     DALQSMEKYL STRPTRFPSL ASGIEWHTRS RTIRNRTSAR VSVPSLLYEE AAPTDPSKPW
     VWRTNLAETK PFWENWFIGL SKKFLEARGG KLLLLAGTDR LDKELMIGQM QGKYQLQVFP
     EAGHFVQEDQ PVKTAQVLVD FYKRNDRSAL VLPPKVADMQ ASAAMKQGAE AGAVPPFGRG
     QGSSHKP