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Database: UniProt
Entry: G0RCA4_HYPJQ
LinkDB: G0RCA4_HYPJQ
Original site: G0RCA4_HYPJQ 
ID   G0RCA4_HYPJQ            Unreviewed;       396 AA.
AC   G0RCA4;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
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=TRIREDRAFT_104400 {ECO:0000313|EMBL:EGR51190.1};
OS   Hypocrea jecorina (strain QM6a) (Trichoderma reesei).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=431241 {ECO:0000313|Proteomes:UP000008984};
RN   [1] {ECO:0000313|EMBL:EGR51190.1, ECO:0000313|Proteomes:UP000008984}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QM6a {ECO:0000313|EMBL:EGR51190.1,
RC   ECO:0000313|Proteomes:UP000008984};
RX   PubMed=18454138; DOI=10.1038/nbt1403;
RA   Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E.,
RA   Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G.,
RA   Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I.,
RA   Larrondo L.F., de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B.,
RA   Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N.,
RA   Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A.,
RA   Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S.,
RA   Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.;
RT   "Genome sequencing and analysis of the biomass-degrading fungus Trichoderma
RT   reesei (syn. Hypocrea jecorina).";
RL   Nat. Biotechnol. 26:553-560(2008).
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; GL985058; EGR51190.1; -; Genomic_DNA.
DR   RefSeq; XP_006962728.1; XM_006962666.1.
DR   AlphaFoldDB; G0RCA4; -.
DR   STRING; 431241.G0RCA4; -.
DR   EnsemblFungi; EGR51190; EGR51190; TRIREDRAFT_104400.
DR   GeneID; 18480840; -.
DR   KEGG; tre:TRIREDRAFT_104400; -.
DR   VEuPathDB; FungiDB:TRIREDRAFT_104400; -.
DR   eggNOG; KOG2564; Eukaryota.
DR   HOGENOM; CLU_024818_3_0_1; -.
DR   OrthoDB; 169198at2759; -.
DR   Proteomes; UP000008984; 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:UP000008984};
KW   Serine esterase {ECO:0000256|PIRNR:PIRNR022950}.
FT   DOMAIN          115..364
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
FT   REGION          1..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..36
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        40..57
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        198
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        224
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
SQ   SEQUENCE   396 AA;  43158 MW;  B8EF3C2015FC7DF9 CRC64;
     MSDLQRAWAK SKLGLPPEPF DQLDEAEEDQ VPELPEGLDD DSSSASSVSS TGTIIPTPSQ
     KLFARPQGVA RGRTLEQIPW TTYFERELFL KSETNPDVTY HVYLSSPSDK GPLYVMHHGA
     GSSGLSFALV GAEIRKRLPN AGILAVDCRG HGSTTAPDGA ALDLRLDTLS SDLFAMVEGT
     KKQMGWKELP PIVLVGHSLG GAVVTDLAMS GKLGTALLAY AVLDVVEGSA MDALQSMQTY
     LSTRPGGFAT VESGIDWHIR TRTVRNAVSA RASVPALLVW DESKDASRPW RWRTNLAATQ
     PFWEDWFVGL SKKFLGARGG KLLLLAGTDR LDTELTIGQM QGKYALQVFP DAGHFIHEDK
     PEQTSVALVD FYRRNDRSAL VLPPKVSELL RQGKKV
//
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