PPME1_CAEEL
ID PPME1_CAEEL Reviewed; 364 AA.
AC Q9BIB3;
DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Probable protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN ORFNames=B0464.9;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=7906398; DOI=10.1038/368032a0;
RA Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA Wilkinson-Sproat J., Wohldman P.;
RT "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT elegans.";
RL Nature 368:32-38(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. {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 ---------------------------------------------------------------------------
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; Z19152; CAC35809.1; -; Genomic_DNA.
DR RefSeq; NP_499084.1; NM_066683.3.
DR AlphaFoldDB; Q9BIB3; -.
DR SMR; Q9BIB3; -.
DR BioGRID; 46862; 5.
DR STRING; 6239.B0464.9; -.
DR ESTHER; caeel-ppme1; PPase_methylesterase_euk.
DR MEROPS; S33.B12; -.
DR EPD; Q9BIB3; -.
DR PaxDb; Q9BIB3; -.
DR PeptideAtlas; Q9BIB3; -.
DR EnsemblMetazoa; B0464.9.1; B0464.9.1; WBGene00007188.
DR GeneID; 181999; -.
DR KEGG; cel:CELE_B0464.9; -.
DR UCSC; B0464.9; c. elegans.
DR CTD; 181999; -.
DR WormBase; B0464.9; CE26705; WBGene00007188; -.
DR eggNOG; KOG2564; Eukaryota.
DR GeneTree; ENSGT00390000004396; -.
DR HOGENOM; CLU_024818_3_1_1; -.
DR InParanoid; Q9BIB3; -.
DR OMA; WHIRSRT; -.
DR OrthoDB; 911863at2759; -.
DR PhylomeDB; Q9BIB3; -.
DR Reactome; R-CEL-69273; Cyclin A/B1/B2 associated events during G2/M transition.
DR PRO; PR:Q9BIB3; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00007188; Expressed in embryo and 3 other tissues.
DR GO; GO:0051722; F:protein C-terminal methylesterase activity; ISS:UniProtKB.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
DR GO; GO:0006482; P:protein demethylation; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR000639; Epox_hydrolase-like.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR PANTHER; PTHR14189; PTHR14189; 1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00412; EPOXHYDRLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00120; LIPASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..364
FT /note="Probable protein phosphatase methylesterase 1"
FT /id="PRO_0000065085"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 164
FT /evidence="ECO:0000250"
FT ACT_SITE 190
FT /evidence="ECO:0000250"
FT ACT_SITE 316
FT /evidence="ECO:0000250"
SQ SEQUENCE 364 AA; 40222 MW; 03D419EA6DF4719B CRC64;
MSDDKLDTLP DLQSETSHVT TPHRQNDLLR QAVTHGRPPP VPSTSTSGKK REMSELPWSD
FFDEKKDANI DGDVFNVYIK GNEGPIFYLL HGGGYSGLTW ACFAKELATL ISCRVVAPDL
RGHGDTKCSD EHDLSKETQI KDIGAIFKNI FGEDDSPVCI VGHSMGGALA IHTLNAKMIS
SKVAALIVID VVEGSAMEAL GGMVHFLHSR PSSFPSIEKA IHWCLSSGTA RNPTAARVSM
PSQIREVSEH EYTWRIDLTT TEQYWKGWFE GLSKEFLGCS VPKMLVLAGV DRLDRDLTIG
QMQGKFQTCV LPKVGHCVQE DSPQNLADEV GRFACRHRIA QPKFSALASP PDPAILEYRK
RHHQ
