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 08-NOV-2023, entry version 67.
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 Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR PANTHER; PTHR14189:SF0; PROTEIN PHOSPHATASE METHYLESTERASE 1; 1.
DR PANTHER; PTHR14189; PROTEIN PHOSPHATASE METHYLESTERASE-1 RELATED; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 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
//
