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Database: UniProt
Entry: Q0CWI5_ASPTN
LinkDB: Q0CWI5_ASPTN
Original site: Q0CWI5_ASPTN 
ID   Q0CWI5_ASPTN            Unreviewed;       403 AA.
AC   Q0CWI5;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Protein phosphatase methylesterase 1 {ECO:0000256|ARBA:ARBA00020672, ECO:0000256|PIRNR:PIRNR022950};
DE            Short=PME-1 {ECO:0000256|PIRNR:PIRNR022950};
DE            EC=3.1.1.- {ECO:0000256|PIRNR:PIRNR022950};
GN   ORFNames=ATEG_01949 {ECO:0000313|EMBL:EAU36911.1};
OS   Aspergillus terreus (strain NIH 2624 / FGSC A1156).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=341663 {ECO:0000313|EMBL:EAU36911.1, ECO:0000313|Proteomes:UP000007963};
RN   [1] {ECO:0000313|Proteomes:UP000007963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIH 2624 / FGSC A1156 {ECO:0000313|Proteomes:UP000007963};
RA   Birren B.W., Lander E.S., Galagan J.E., Nusbaum C., Devon K., Henn M.,
RA   Ma L.-J., Jaffe D.B., Butler J., Alvarez P., Gnerre S., Grabherr M.,
RA   Kleber M., Mauceli E.W., Brockman W., Rounsley S., Young S.K., LaButti K.,
RA   Pushparaj V., DeCaprio D., Crawford M., Koehrsen M., Engels R.,
RA   Montgomery P., Pearson M., Howarth C., Larson L., Luoma S., White J.,
RA   Alvarado L., Kodira C.D., Zeng Q., Oleary S., Yandava C., Denning D.W.,
RA   Nierman W.C., Milne T., Madden K.;
RT   "Annotation of the Aspergillus terreus NIH2624 genome.";
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Demethylates proteins that have been reversibly
CC       carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit.
CC       {ECO:0000256|ARBA:ARBA00024741}.
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         Evidence={ECO:0000256|ARBA:ARBA00000906};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008645, ECO:0000256|PIRNR:PIRNR022950}.
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DR   EMBL; CH476596; EAU36911.1; -; Genomic_DNA.
DR   RefSeq; XP_001211127.1; XM_001211127.1.
DR   AlphaFoldDB; Q0CWI5; -.
DR   STRING; 341663.Q0CWI5; -.
DR   ESTHER; asptn-q0cwi5; PPase_methylesterase_euk.
DR   EnsemblFungi; EAU36911; EAU36911; ATEG_01949.
DR   GeneID; 4316554; -.
DR   VEuPathDB; FungiDB:ATEG_01949; -.
DR   eggNOG; KOG2564; Eukaryota.
DR   HOGENOM; CLU_024818_3_0_1; -.
DR   OMA; EAHHTSM; -.
DR   OrthoDB; 169198at2759; -.
DR   Proteomes; UP000007963; Unassembled WGS sequence.
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   PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR022950};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007963};
KW   Serine esterase {ECO:0000256|PIRNR:PIRNR022950}.
FT   DOMAIN          100..357
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
FT   REGION          19..55
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          383..403
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        188
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        214
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        345
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
SQ   SEQUENCE   403 AA;  44036 MW;  A95A7B78A39E7582 CRC64;
     MSELQKSFAK AKLAKLPVEP PMSAMDALEE EDSSGSSTGT VTPSPSKRLF ARPDRESASS
     TLSWTDFFAQ ELFLREDVAN TQITHHVYLT PPTGSGPLFV MHHGAGSSGL SFATCAEEIR
     KLLPTAGVLS LDARDHGQTT VTAADGHSPV ALDLSLDTLN RDLVFVVRAT QSHMAWDSLP
     DLVLVGHSLG GAVITDVARK GELGPKVLAY AVLDVVEGSA MDALQSMEQY LSTRPSRFPS
     LTSGIEWHTR SRTLRNRTSA RVSVPSLLYE EEASSDPSKP WVWRTNLAET KPFWENWFIG
     LSRKFLEARG GKLLLLAGTD RLDKELMIGQ MQGKYQLQVL PEAGHFIQED QPAKTAQILV
     DFYKRNDRSA LVLPPKVADM QASAAMKKGG SMGNPLGRPQ DHK
//
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