ID   C0NML3_AJECG            Unreviewed;       275 AA.
AC   C0NML3;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=HCBG_03990 {ECO:0000313|EMBL:EEH07111.1};
OS   Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432)
OS   (Darling's disease fungus) (Histoplasma capsulatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX   NCBI_TaxID=447093 {ECO:0000313|EMBL:EEH07111.1, ECO:0000313|Proteomes:UP000001631};
RN   [1] {ECO:0000313|Proteomes:UP000001631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G186AR / H82 / ATCC MYA-2454 / RMSCC 2432
RC   {ECO:0000313|Proteomes:UP000001631};
RA   Champion M., Cuomo C.A., Ma L.-J., Henn M.R., Sil A., Goldman B.,
RA   Young S.K., Kodira C.D., Zeng Q., Koehrsen M., Alvarado L., Berlin A.,
RA   Borenstein D., Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heiman D., Hepburn T., Howarth C., Jen D., Larson L.,
RA   Lewis B., Mehta T., Park D., Pearson M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Klein B., McEwen J.G., Puccia R., Goldman G.H., Felipe M.S., Nino-Vega G.,
RA   San-Blas G., Taylor J., Mendoza L., Galagan J.E., Nusbaum C., Birren B.W.;
RT   "The genome sequence of Ajellomyces capsulatus strain G186AR.";
RL   Submitted (FEB-2009) 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}.
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DR   EMBL; GG663367; EEH07111.1; -; Genomic_DNA.
DR   AlphaFoldDB; C0NML3; -.
DR   STRING; 447093.C0NML3; -.
DR   VEuPathDB; FungiDB:I7I50_11967; -.
DR   HOGENOM; CLU_049413_2_2_1; -.
DR   InParanoid; C0NML3; -.
DR   OrthoDB; 1424864at2759; -.
DR   Proteomes; UP000001631; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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:UP000001631};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT   DOMAIN          7..165
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
SQ   SEQUENCE   275 AA;  30743 MW;  30F24E2B9C03F38E CRC64;
     MEFPALHIVE PQSTHTHTVI LLHGRSSDGV EFAEDLFDSQ TSDNKSLAAH FPSCRWVFPT
     SRDRWSSVFR EELTAWFDVY SLSNPCEQQD LQVDGLREST LYILEIVNRE IDLLGGKSER
     VFLGGISQGM ATALWALLCS PGRIKGRIGA FFGMCGWLPF ANKIQDLQLS DEAATQTARS
     MIPKIFLDII QCEGPQASVV EAETMLSTPL LLLHGTDDAW IDVELGRQAQ ACLDKLGMKV
     DWKEYLGAEN EGHWIKQPEG LDVLVQFLEA TWGGR
//