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Database: UniProt
Entry: A0A0J9WN66_FUSO4
LinkDB: A0A0J9WN66_FUSO4
Original site: A0A0J9WN66_FUSO4 
ID   A0A0J9WN66_FUSO4        Unreviewed;       204 AA.
AC   A0A0J9WN66;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Acyl-protein thioesterase 1 {ECO:0000256|ARBA:ARBA00014923};
DE            EC=3.1.2.22 {ECO:0000256|ARBA:ARBA00012423};
DE   AltName: Full=Palmitoyl-protein hydrolase {ECO:0000256|ARBA:ARBA00031195};
GN   ORFNames=FOXG_08202 {ECO:0000313|EMBL:KNB06747.1};
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:KNB06747.1, ECO:0000313|Proteomes:UP000009097};
RN   [1] {ECO:0000313|EMBL:KNB06747.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB06747.1};
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:KNB06747.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4287 {ECO:0000313|EMBL:KNB06747.1};
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: Hydrolyzes fatty acids from S-acylated cysteine residues in
CC       proteins with a strong preference for palmitoylated G-alpha proteins
CC       over other acyl substrates. Mediates the deacylation of G-alpha
CC       proteins such as GPA1 in vivo, but has weak or no activity toward
CC       palmitoylated Ras proteins. Has weak lysophospholipase activity in
CC       vitro; however such activity may not exist in vivo.
CC       {ECO:0000256|ARBA:ARBA00029392}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) +
CC         hexadecanoate + L-cysteinyl-[protein]; Xref=Rhea:RHEA:19233,
CC         Rhea:RHEA-COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:7896,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:74151; EC=3.1.2.22;
CC         Evidence={ECO:0000256|ARBA:ARBA00000072};
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000256|ARBA:ARBA00006499}.
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DR   EMBL; DS231705; KNB06747.1; -; Genomic_DNA.
DR   RefSeq; XP_018244792.1; XM_018386997.1.
DR   AlphaFoldDB; A0A0J9WN66; -.
DR   GeneID; 28949850; -.
DR   KEGG; fox:FOXG_08202; -.
DR   VEuPathDB; FungiDB:FOXG_08202; -.
DR   OrthoDB; 4670340at2759; -.
DR   Proteomes; UP000009097; Unassembled WGS sequence.
DR   GO; GO:0052689; F:carboxylic ester hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR   PANTHER; PTHR10655:SF17; PALMITOYL-PROTEIN HYDROLASE; 1.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009097};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT   DOMAIN          15..198
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
SQ   SEQUENCE   204 AA;  22298 MW;  2449955A99433F18 CRC64;
     MAGQVLLRTG AAIEKLSEVK FILPHAPEIP ITVNMGMRMP GWFDVKQLGG DVDSLVRNED
     TEGIKRSQKY FHDLIQEEVN SGIPPERIVL GGFSQGGAMS LLAGLTCTSK LGGIVGLSSW
     LLLSKTFADL VKPTDANRQT PVMMFHGDAD PIVPFQRGKL SADLLKELGY DVTFKTYPGM
     GHSACLEELD EVEAFLRKQL PPKN
//
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