PPME1_EMENI
ID PPME1_EMENI Reviewed; 407 AA.
AC Q5BGN7; C8VUA3;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-FEB-2006, sequence version 2.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
GN Name=ppe1; ORFNames=AN0293;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=EAA65699.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AACD01000006; EAA65699.1; ALT_SEQ; Genomic_DNA.
DR EMBL; BN001308; CBF89786.1; -; Genomic_DNA.
DR RefSeq; XP_657897.1; XM_652805.1.
DR AlphaFoldDB; Q5BGN7; -.
DR SMR; Q5BGN7; -.
DR STRING; 162425.CADANIAP00002422; -.
DR ESTHER; emeni-ppme1; PPase_methylesterase_euk.
DR EnsemblFungi; CBF89786; CBF89786; ANIA_00293.
DR EnsemblFungi; EAA65699; EAA65699; AN0293.2.
DR GeneID; 2876071; -.
DR KEGG; ani:AN0293.2; -.
DR VEuPathDB; FungiDB:AN0293; -.
DR eggNOG; KOG2564; Eukaryota.
DR HOGENOM; CLU_024818_3_0_1; -.
DR InParanoid; Q5BGN7; -.
DR OMA; WHIRSRT; -.
DR OrthoDB; 911863at2759; -.
DR Proteomes; UP000000560; Chromosome VIII.
DR Proteomes; UP000005890; Unassembled WGS sequence.
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; 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; Reference proteome; Serine esterase.
FT CHAIN 1..407
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000223665"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 185
FT /evidence="ECO:0000250"
FT ACT_SITE 211
FT /evidence="ECO:0000250"
FT ACT_SITE 342
FT /evidence="ECO:0000250"
SQ SEQUENCE 407 AA; 44304 MW; DBAB023E152DF8B8 CRC64;
MSDLQKSFAK SKLAKLPPEP PPIPESVADE DDDSGSSTET VTPSPVKQLF ARPGGTRGFF
DQELYLQRRV NDLDIVHHVY LTSPTNSGPL FVMHHGAGSS GLSFANCAAE IRKILPNAGI
LSADARDHGS TSVKRASEDG EADPETARLD LSLDTLNQDL LFVIRETQAK MGWETLPDIV
LVGHSLGGAV ITDVAKKGEL GGKLLAYAVL DVVEGSAMDA LQSMETYLST RPSRFPSLPS
GIEWHTRSRT IRNRTSARVS VPSLLYHEDV PKDPSKPWVW RTNLAETKPF WEGWFVGLSR
KFLEARGGKL LLLAGTDRLD KELMIGQMQG KYQLQVFPDA GHFIQEDQPA RTAQILVDFY
KRNDRSALVL PPKVADMQAS AAMKKGAGAG VPLGKAEGGT TGSFKRS
