PPME1_CANAL
ID PPME1_CANAL Reviewed; 360 AA.
AC Q5ALW7; A0A1D8PGC4;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN Name=PPE1; OrderedLocusNames=CAALFM_C201520WA;
GN ORFNames=CaO19.1459, CaO19.9034;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION.
RX PubMed=16011244;
RA Cao F., Chen J.Y.;
RT "Cloning and functional study of CaPPe1 in Candida albicans by using
RT Saccharomyces cerevisiae model system.";
RL Shi Yan Sheng Wu Xue Bao 38:119-125(2005).
CC -!- FUNCTION: Demethylates proteins that have been reversibly
CC carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit
CC (By similarity). Involved in the regulation of filamentous growth.
CC {ECO:0000250, ECO:0000269|PubMed:16011244}.
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; CP017624; AOW27198.1; -; Genomic_DNA.
DR RefSeq; XP_722509.1; XM_717416.1.
DR AlphaFoldDB; Q5ALW7; -.
DR SMR; Q5ALW7; -.
DR STRING; 237561.Q5ALW7; -.
DR ESTHER; canal-ppme1; PPase_methylesterase_euk.
DR GeneID; 3635802; -.
DR KEGG; cal:CAALFM_C201520WA; -.
DR CGD; CAL0000196033; PPE1.
DR VEuPathDB; FungiDB:C2_01520W_A; -.
DR eggNOG; KOG2564; Eukaryota.
DR HOGENOM; CLU_024818_3_1_1; -.
DR InParanoid; Q5ALW7; -.
DR OMA; WHIRSRT; -.
DR OrthoDB; 911863at2759; -.
DR PRO; PR:Q5ALW7; -.
DR Proteomes; UP000000559; Chromosome 2.
DR GO; GO:0005763; C:mitochondrial small ribosomal subunit; IEA:EnsemblFungi.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:EnsemblFungi.
DR GO; GO:1990577; P:C-terminal protein demethylation; IEA:EnsemblFungi.
DR GO; GO:0006482; P:protein demethylation; IBA:GO_Central.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
DR InterPro; IPR016812; PPase_methylesterase_euk.
DR PANTHER; PTHR14189; PTHR14189; 1.
DR Pfam; PF12146; Hydrolase_4; 1.
DR PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Reference proteome; Serine esterase.
FT CHAIN 1..360
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000223661"
FT REGION 26..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 167
FT /evidence="ECO:0000250"
FT ACT_SITE 192
FT /evidence="ECO:0000250"
FT ACT_SITE 316
FT /evidence="ECO:0000250"
SQ SEQUENCE 360 AA; 40450 MW; 74931F993C22B79F CRC64;
MSELHKAFLR RIKEQETALG LSGLVDEDDI PEPAVMPPTG NSSSTANTED ETILRDYKQF
KETNFIQEFY ENELGHKFKT YYKPSKKPGS ILFCHHGAGS SSMTFGNLVN HIEDESVGIF
LFDTRGHGES VATSDFSLDT LVQDVSFVLE QFSSKHQQTS IFLLGHSLGG AVLAKYSTLY
PSDILKGLIL LDIVEEAAVQ SLNAMPSFIA RRPLSFPSLS KAISWHMNFL LFNEKSARLS
VPDLFTDKLT WITDLNATQP YWQTWFSGLS ENFLGFKGPK LLMLSTHESL DKQLMIGQMQ
GKYQLVVFKN NEKSGHFVHE DLPNHVAVCL TDYIKRAVAP EIFMKEDLGV VPKWGGKINK