ID   Q6MY76_ASPFM            Unreviewed;       447 AA.
AC   Q6MY76;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 55.
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=AfA33H4.085c {ECO:0000313|EMBL:CAF32127.1};
OS   Aspergillus fumigatus (Neosartorya fumigata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=746128 {ECO:0000313|EMBL:CAF32127.1};
RN   [1] {ECO:0000313|EMBL:CAF32127.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=14998527; DOI=10.1016/j.fgb.2003.12.003;
RA   Pain A., Woodward J., Quail M.A., Anderson M.J., Clark R., Collins M.,
RA   Fosker N., Fraser A., Harris D., Larke N., Murphy L., Humphray S.,
RA   O'Neil S., Pertea M., Price C., Rabbinowitsch E., Rajandream M-A.,
RA   Salzberg S., Saunders D., Seegar K., Sharp S., Warren T., Denning D.W.,
RA   Barrell B., Hall N.;
RT   "Insight into the genome of Aspergillus fumigatus: analysis of a 922 kb
RT   region encompassing the nitrate assimilation gene cluster.";
RL   Fungal Genet. Biol. 41:443-453(2004).
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; BX649607; CAF32127.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6MY76; -.
DR   ESTHER; aspfu-q6my76; LYsophospholipase_carboxylesterase.
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   Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT   DOMAIN          242..322
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
FT   REGION          220..256
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        223..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   447 AA;  48399 MW;  4E12794B3C0AEBF6 CRC64;
     MLAIMTYSAL WTLNVESGRL TGAGRLLRSL AAPQLILAAL TFSKHHVQII TRMSSGYPVW
     ASFLLLSYRR HDCSYGNNKA ELPHPGTDMT ITITQVYNNN ITLTPSQFQS PIHDASKMVP
     QLFPPRHVYF PSNPSHTSTV ILLHDTNSTG AELAAALDVS TTPATETATA GNPKSIFEHF
     PSCRWVFPSA QPRQIDICYA SRGNWINVDV DVAVAVDTDA NEDTDPGANS LQQPQPQLSP
     STKDVDNNYN NNADQNDDLE TCVEYILQVV EEEIIRLDGD SRRVVLGGFG QGMAVAIAAL
     LAAQRRLGGF VGVSGWVPHP ERIGSLAGRG RGLLVENEAR MGASEGSAGA DGVEVDPGAD
     SMLETPVLLS YLEDDPCVDI QTALTVDETL NRLGFVKVVW DACPSSPQGE GSLLHLHQLD
     TIMGFLTEVF DHEGSNLPQD DMLGYST
//