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Database: UniProt
Entry: A0A0J9U634_FUSO4
LinkDB: A0A0J9U634_FUSO4
Original site: A0A0J9U634_FUSO4 
ID   A0A0J9U634_FUSO4        Unreviewed;       336 AA.
AC   A0A0J9U634;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Protein phosphatase methylesterase 1 {ECO:0000256|ARBA:ARBA00020672, ECO:0000256|PIRNR:PIRNR022950};
DE            Short=PME-1 {ECO:0000256|PIRNR:PIRNR022950};
DE            EC=3.1.1.- {ECO:0000256|PIRNR:PIRNR022950};
GN   ORFNames=FOXG_00463 {ECO:0000313|EMBL:KNA94399.1};
OS   Fusarium oxysporum f. sp. lycopersici (strain 4287 / CBS 123668 / FGSC 9935
OS   / NRRL 34936) (Fusarium vascular wilt of tomato).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=426428 {ECO:0000313|EMBL:KNA94399.1, ECO:0000313|Proteomes:UP000009097};
RN   [1] {ECO:0000313|EMBL:KNA94399.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNA94399.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Ma L.-J., Jaffe D.,
RA   Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M., Mauceli E.,
RA   Brockman W., MacCallum I.A., Young S., LaButti K., DeCaprio D.,
RA   Crawford M., Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C.,
RA   Larson L., White J., O'Leary S., Kodira C., Zeng Q., Yandava C.,
RA   Alvarado L., Kistler C., Shim W.-B., Kang S., Woloshuk C.;
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KNA94399.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNA94399.1};
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., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
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., Mukherjee M.,
RA   Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA   Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA   Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA   Kistler H.C., Rep M.;
RT   "Comparative genomics reveals mobile pathogenicity chromosomes in
RT   Fusarium.";
RL   Nature 464:367-373(2010).
CC   -!- FUNCTION: Demethylates proteins that have been reversibly
CC       carboxymethylated. Demethylates the phosphatase PP2A catalytic subunit.
CC       {ECO:0000256|ARBA:ARBA00024741}.
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         Evidence={ECO:0000256|ARBA:ARBA00000906};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily.
CC       {ECO:0000256|ARBA:ARBA00008645, ECO:0000256|PIRNR:PIRNR022950}.
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DR   EMBL; DS231696; KNA94399.1; -; Genomic_DNA.
DR   RefSeq; XP_018232445.1; XM_018376823.1.
DR   AlphaFoldDB; A0A0J9U634; -.
DR   GeneID; 28942773; -.
DR   VEuPathDB; FungiDB:FOXG_00463; -.
DR   OrthoDB; 169198at2759; -.
DR   Proteomes; UP000009097; Unassembled WGS sequence.
DR   GO; GO:0051723; F:protein methylesterase activity; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR016812; PPase_methylesterase_euk.
DR   PANTHER; PTHR14189:SF0; PROTEIN PHOSPHATASE METHYLESTERASE 1; 1.
DR   PANTHER; PTHR14189; PROTEIN PHOSPHATASE METHYLESTERASE-1 RELATED; 1.
DR   Pfam; PF12697; Abhydrolase_6; 1.
DR   PIRSF; PIRSF022950; PPase_methylesterase_euk; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR022950};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009097};
KW   Serine esterase {ECO:0000256|PIRNR:PIRNR022950}.
FT   DOMAIN          55..305
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF12697"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        164
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
FT   ACT_SITE        294
FT                   /evidence="ECO:0000256|PIRSR:PIRSR022950-1"
SQ   SEQUENCE   336 AA;  36833 MW;  DAE24F0F08D5DCCD CRC64;
     MAGLTGYRVA RGRTLEQIPW TTYFERELSL KSEQEPEVVY HAYLTSPVGK GPLFVMHHGA
     GSSGLSFAVV ASEIKKRLST AGILAIDCRG HGSTNAPGDK ALDMRLDTLS SDLFSMVQLT
     RNEMAWSEMP PIVLVGHSLG GAVVTDLAKS GRLGTSVLGY AVLDVVEGSA IDALQSMHTY
     LSTRPLGFAT LQAGIEWHIR SRTIRNSISA RTSVPALLVF NENDDPTRPW RWRTNLGATQ
     PYWEGWFIGL SKKFLGAKGG KLLLLAGTDR LDTELTIGQM QGKYALQVFP EAGHFIHEDL
     PEKTAVSLVD FFRRNDRSAL VLPPKVSDLL KQGKRV
//
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