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PPME1_GIBZE
ID   PPME1_GIBZE             Reviewed;         400 AA.
AC   Q4IQC1; A0A0E0RMS4; V6QV46;
DT   21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2005, sequence version 1.
DT   25-MAY-2022, entry version 85.
DE   RecName: Full=Protein phosphatase methylesterase 1;
DE            Short=PME-1;
DE            EC=3.1.1.89;
GN   Name=PPE1; ORFNames=FGRRES_00587, FGSG_00587;
OS   Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084
OS   / PH-1) (Wheat head blight fungus) (Fusarium graminearum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium.
OX   NCBI_TaxID=229533;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=17823352; DOI=10.1126/science.1143708;
RA   Cuomo C.A., Gueldener U., Xu J.-R., Trail F., Turgeon B.G., Di Pietro A.,
RA   Walton J.D., Ma L.-J., Baker S.E., Rep M., Adam G., Antoniw J., Baldwin T.,
RA   Calvo S.E., Chang Y.-L., DeCaprio D., Gale L.R., Gnerre S., Goswami R.S.,
RA   Hammond-Kosack K., Harris L.J., Hilburn K., Kennell J.C., Kroken S.,
RA   Magnuson J.K., Mannhaupt G., Mauceli E.W., Mewes H.-W., Mitterbauer R.,
RA   Muehlbauer G., Muensterkoetter M., Nelson D., O'Donnell K., Ouellet T.,
RA   Qi W., Quesneville H., Roncero M.I.G., Seong K.-Y., Tetko I.V., Urban M.,
RA   Waalwijk C., Ward T.J., Yao J., Birren B.W., Kistler H.C.;
RT   "The Fusarium graminearum genome reveals a link between localized
RT   polymorphism and pathogen specialization.";
RL   Science 317:1400-1402(2007).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=20237561; DOI=10.1038/nature08850;
RA   Ma L.-J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.-J.,
RA   Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA   Houterman P.M., Kang S., Shim W.-B., Woloshuk C., Xie X., Xu J.-R.,
RA   Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA   Butchko R.A.E., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.J.,
RA   Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA   Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA   Kumar L., Lee Y.-H., Li L., Manners J.M., Miranda-Saavedra D.,
RA   Mukherjee M., Park G., Park J., Park S.-Y., Proctor R.H., Regev A.,
RA   Ruiz-Roldan M.C., Sain D., Sakthikumar S., Sykes S., Schwartz D.C.,
RA   Turgeon B.G., Wapinski I., Yoder O., Young S., Zeng Q., Zhou S.,
RA   Galagan J., Cuomo C.A., Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1;
RX   PubMed=26198851; DOI=10.1186/s12864-015-1756-1;
RA   King R., Urban M., Hammond-Kosack M.C.U., Hassani-Pak K.,
RA   Hammond-Kosack K.E.;
RT   "The completed genome sequence of the pathogenic ascomycete fungus Fusarium
RT   graminearum.";
RL   BMC Genomics 16:544-544(2015).
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; DS231663; ESU05789.1; -; Genomic_DNA.
DR   EMBL; HG970332; CEF72549.1; -; Genomic_DNA.
DR   RefSeq; XP_011316274.1; XM_011317972.1.
DR   AlphaFoldDB; Q4IQC1; -.
DR   SMR; Q4IQC1; -.
DR   STRING; 5518.FGSG_00587P0; -.
DR   ESTHER; gibze-ppme1; PPase_methylesterase_euk.
DR   EnsemblFungi; ESU05789; ESU05789; FGSG_00587.
DR   GeneID; 23548072; -.
DR   KEGG; fgr:FGSG_00587; -.
DR   VEuPathDB; FungiDB:FGRAMPH1_01G01497; -.
DR   eggNOG; KOG2564; Eukaryota.
DR   HOGENOM; CLU_024818_3_0_1; -.
DR   InParanoid; Q4IQC1; -.
DR   Proteomes; UP000070720; Chromosome 1.
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; Reference proteome; Serine esterase.
FT   CHAIN           1..400
FT                   /note="Protein phosphatase methylesterase 1"
FT                   /id="PRO_0000223666"
FT   REGION          1..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        41..64
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        202
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        228
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        358
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   400 AA;  43956 MW;  B59E3112C3C91A64 CRC64;
     MSDLQRTWAK AKFGASNDPF DEPQEEQGQD VLPELPEPVD DDSSSASSAS SVSSTGTIIP
     SPNQKLFARP QGVARGRTLE QIPWTTYFER EVSLKSEQDP EVIYHAYLTS PVGKGPLFVM
     HHGAGSSGLS FAVVASQIRK RISTAGILAL DCRGHGSTYA PEDKAFDMRL DTLSSDLYNV
     VQLTKTEMSW PEMPPIVLVG HSLGGAVVTD LAKSGKLGTS VLGYAVLDVV EGSAIDALQS
     MHTYLSTRPL GFATLQAGIE WHIRSRTIRN SISARTSVPA LLVFNENDDP TRPWRWRTNL
     GATQPYWEDW FVGLSKKFLE ARGGKMLLLA GTDRLDTELT IGQMQGKYAL QVFPEAGHFI
     HEDLPEKTAV SLVDFFRRND RTALVLPPKV SDLIKQGKRV
 
 
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