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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//