ID PPME1_YARLI Reviewed; 419 AA.
AC Q6CGE1;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN Name=PPE1; OrderedLocusNames=YALI0A20086g;
OS Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Dipodascaceae; Yarrowia.
OX NCBI_TaxID=284591;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLIB 122 / E 150;
RX PubMed=15229592; DOI=10.1038/nature02579;
RA Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA Weissenbach J., Wincker P., Souciet J.-L.;
RT "Genome evolution in yeasts.";
RL Nature 430:35-44(2004).
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}.
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DR EMBL; CR382127; CAG84209.1; -; Genomic_DNA.
DR RefSeq; XP_500271.1; XM_500271.1.
DR AlphaFoldDB; Q6CGE1; -.
DR SMR; Q6CGE1; -.
DR STRING; 284591.Q6CGE1; -.
DR ESTHER; yarli-ppme1; PPase_methylesterase_euk.
DR MEROPS; S33.B12; -.
DR EnsemblFungi; CAG84209; CAG84209; YALI0_A20086g.
DR GeneID; 2906043; -.
DR KEGG; yli:YALI0A20086g; -.
DR VEuPathDB; FungiDB:YALI0_A20086g; -.
DR HOGENOM; CLU_024818_3_1_1; -.
DR InParanoid; Q6CGE1; -.
DR OMA; EAHHTSM; -.
DR OrthoDB; 169198at2759; -.
DR Proteomes; UP000001300; Chromosome A.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
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; Reference proteome; Serine esterase.
FT CHAIN 1..419
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000223670"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 230
FT /evidence="ECO:0000250"
FT ACT_SITE 256
FT /evidence="ECO:0000250"
FT ACT_SITE 383
FT /evidence="ECO:0000250"
SQ SEQUENCE 419 AA; 46200 MW; AFE3EA8D52E627D4 CRC64;
MSQLHRGMHK KPGMFPPKEV LEEVDAGSGS DTETEETVEC TEEEEEQDET DGLGDLGMPP
PKKTTKSAAS PTVPAPALIP SLSHLIGLEG KQPSRKYAPA EWPQYFKQKI SVARDNDTFN
VLYTPPDDSE APVYVFHHGA GSCAESFALL SVRLREMMHE ERFQLAATAK IRDENKLPGM
IAFDARGHGF TEVESTDYSL EAFTNDFAFI VANVVAEFGL TNNLILVGHS LGGAVVTNAC
HLKLIQHPVI GLAVLDVVEG TAIESLASMQ QILNSRPKSF PTVEKGIEWT VQSHTIRNRE
SACVSVPPTL ISQHDGPGMT WRTDLMLTKP YWKGWFTGLS EKFISCAPAK LLILAGTDRL
DKDLMVGQMQ GKYQLIVFQE SGHFVQEDAP DKTALSLIDF WKRNDKVNKT VPLFGAFRA
//
