PPME1_CRYNB
ID PPME1_CRYNB Reviewed; 422 AA.
AC P0CO63; Q55N08; Q5KBD8;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 25-MAY-2022, entry version 37.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN Name=PPE1; OrderedLocusNames=CNBH2760;
OS Cryptococcus neoformans var. neoformans serotype D (strain B-3501A)
OS (Filobasidiella neoformans).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=283643;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B-3501A;
RX PubMed=15653466; DOI=10.1126/science.1103773;
RA Loftus B.J., Fung E., Roncaglia P., Rowley D., Amedeo P., Bruno D.,
RA Vamathevan J., Miranda M., Anderson I.J., Fraser J.A., Allen J.E.,
RA Bosdet I.E., Brent M.R., Chiu R., Doering T.L., Donlin M.J., D'Souza C.A.,
RA Fox D.S., Grinberg V., Fu J., Fukushima M., Haas B.J., Huang J.C.,
RA Janbon G., Jones S.J.M., Koo H.L., Krzywinski M.I., Kwon-Chung K.J.,
RA Lengeler K.B., Maiti R., Marra M.A., Marra R.E., Mathewson C.A.,
RA Mitchell T.G., Pertea M., Riggs F.R., Salzberg S.L., Schein J.E.,
RA Shvartsbeyn A., Shin H., Shumway M., Specht C.A., Suh B.B., Tenney A.,
RA Utterback T.R., Wickes B.L., Wortman J.R., Wye N.H., Kronstad J.W.,
RA Lodge J.K., Heitman J., Davis R.W., Fraser C.M., Hyman R.W.;
RT "The genome of the basidiomycetous yeast and human pathogen Cryptococcus
RT neoformans.";
RL Science 307:1321-1324(2005).
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; AAEY01000042; EAL19177.1; -; Genomic_DNA.
DR RefSeq; XP_773824.1; XM_768731.1.
DR AlphaFoldDB; P0CO63; -.
DR SMR; P0CO63; -.
DR ESTHER; cryne-ppme1; PPase_methylesterase_euk.
DR EnsemblFungi; EAL19177; EAL19177; CNBH2760.
DR GeneID; 4937799; -.
DR KEGG; cnb:CNBH2760; -.
DR VEuPathDB; FungiDB:CNBH2760; -.
DR HOGENOM; CLU_024818_3_1_1; -.
DR Proteomes; UP000001435; Chromosome 8.
DR GO; GO:0051723; F:protein methylesterase activity; IEA:InterPro.
DR GO; GO:0006482; P:protein demethylation; IEA:InterPro.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
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 SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Hydrolase; Serine esterase.
FT CHAIN 1..422
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000410137"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 207
FT /evidence="ECO:0000250"
FT ACT_SITE 234
FT /evidence="ECO:0000250"
FT ACT_SITE 371
FT /evidence="ECO:0000250"
SQ SEQUENCE 422 AA; 45639 MW; 429202F29178B7B8 CRC64;
MSDMFRKSVL NKLPHLPPTR APWADESEPI EEIDEEDEQL DGIGEFKPAT MGPSKHDTQD
YSPLSASTFF AQAAEVQPPS TPCTFRVYLT PPNLSIASTN AGTPPGPSGL RTQQQTNRHG
TYLVCHHGGG ASGLGFAPLA REVKAKGNGE MGVLAFDCRG HGKTSTSDPN LELDLSHDTL
LSDFMAIIEM MFPDPKESPS LILLGHSMGA APVVSAAPEL QKKGYTIPGV VVLDVVEGTA
VESLPLMKSV LSKRPESFRS VIDAIYWHVT SNSIRNVESA RVSVPHIIVP APSSSSSDPS
ANPGGKQVWR TNLVGTEPYW EGWYKGLSQR FLRTKCARLL VLAGQERLDR ELMVGQMQGK
FQLEVMSDVG HYLHEDNPAG LAATLITFWH RNTRVLVLPP KIGAPGPGAR GGPVEVKQVG
QQ