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Database: UniProt
Entry: A0A439CNX7_9PEZI
LinkDB: A0A439CNX7_9PEZI
Original site: A0A439CNX7_9PEZI 
ID   A0A439CNX7_9PEZI        Unreviewed;       241 AA.
AC   A0A439CNX7;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 10.
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=EKO27_g11232 {ECO:0000313|EMBL:RWA03871.1};
OS   Xylaria grammica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Xylariomycetidae; Xylariales; Xylariaceae; Xylaria.
OX   NCBI_TaxID=363999 {ECO:0000313|EMBL:RWA03871.1, ECO:0000313|Proteomes:UP000286045};
RN   [1] {ECO:0000313|EMBL:RWA03871.1, ECO:0000313|Proteomes:UP000286045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IHI A82 {ECO:0000313|EMBL:RWA03871.1,
RC   ECO:0000313|Proteomes:UP000286045};
RA   Buettner E., Kellner H.;
RT   "Draft genome sequence of Xylaria grammica IHI A82.";
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RWA03871.1}.
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DR   EMBL; RYZI01000683; RWA03871.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A439CNX7; -.
DR   STRING; 363999.A0A439CNX7; -.
DR   Proteomes; UP000286045; 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:UP000286045};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT   DOMAIN          12..228
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
SQ   SEQUENCE   241 AA;  26297 MW;  375D12D46DA934E5 CRC64;
     MAMPRAKPLL FSASAKHTAT VIFLHGLGDT GFGWASAVEG WIRGNKLDEV KWVLPHAPRM
     PITAAEGMPM PGWFDITALN GAIDDIRARQ DEPGLLQTRE YVNGLIQSEI DAGIPANRIV
     LGGFSQGGAM ALLTALTAKA KLAGVVGLSC WLPLDSKFHN LVRESDFNHD TPIYMAHGTV
     DRVVPTAFGQ LSYEILKRQN FPVTMKSIPG MAHSACQEEL DEVEAFLHSR LPPQEEKKSE
     L
//
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