PPME1_NEUCR
ID PPME1_NEUCR Reviewed; 454 AA.
AC Q7SGG8;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 25-MAY-2022, entry version 92.
DE RecName: Full=Protein phosphatase methylesterase 1;
DE Short=PME-1;
DE EC=3.1.1.89;
DE AltName: Full=Pectin methylesterase 1;
GN Name=pme-1; Synonyms=ppe1; ORFNames=B20J13.050, NCU00954;
OS Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS FGSC 987).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX NCBI_TaxID=367110;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12655011; DOI=10.1093/nar/gkg293;
RA Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT genome sequence.";
RL Nucleic Acids Res. 31:1944-1954(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
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=EAA35911.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BX842629; CAE76324.1; -; Genomic_DNA.
DR EMBL; CM002236; EAA35911.2; ALT_INIT; Genomic_DNA.
DR RefSeq; XP_965147.2; XM_960054.2.
DR AlphaFoldDB; Q7SGG8; -.
DR SMR; Q7SGG8; -.
DR STRING; 5141.EFNCRP00000000641; -.
DR ESTHER; neucr-ppme1; PPase_methylesterase_euk.
DR PRIDE; Q7SGG8; -.
DR EnsemblFungi; EAA35911; EAA35911; NCU00954.
DR GeneID; 3881315; -.
DR KEGG; ncr:NCU00954; -.
DR HOGENOM; CLU_024818_3_0_1; -.
DR InParanoid; Q7SGG8; -.
DR Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR GO; GO:0051723; F:protein methylesterase activity; IBA:GO_Central.
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..454
FT /note="Protein phosphatase methylesterase 1"
FT /id="PRO_0000223668"
FT REGION 1..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 240
FT /evidence="ECO:0000250"
FT ACT_SITE 266
FT /evidence="ECO:0000250"
FT ACT_SITE 412
FT /evidence="ECO:0000250"
SQ SEQUENCE 454 AA; 48955 MW; F62366ACF9A8A396 CRC64;
MSELQKQWAK ARLGSQALGQ PPAEMPITTT MPEFNEADED KEMAGPSPGG FPFDDDSSSA
SSVSSTGTVI PSPGRALFAR PQGFASRSMD PIPWTTYFER ELFLKEEAGP DSGSRTSNKN
KPTSITYHAY LTSPVGKGPL FVTHHGAGSS GLSFAVLSSE IRKRLPNAGI LSLDARGHGS
TTVTAASSVP GEGDETTGQA PPPLDLSLST LASDLFTVIQ LTRTAMHWPE LPPIILVGHS
LGGAVVTELA KSYRLGPSLL GYAVLDVVEG CAMDALQSMQ TYLSTRPQGF ASLKDGIDWH
VRSRTIRNST SARTSVPGLL APVEELQRPE LQQLPRGVAG TQGTAKPWRW KTDLAATQPF
WEDWFVGLSK KFLEARGGKM LLLAGTDRLD TELTIGQMQG KYALQVFPEA GHFIHEDLPE
KTAIALVDFH RRNDRSQLVL PPKVSDLLAQ GKKV