ID A0A2J5HG60_9EURO Unreviewed; 253 AA.
AC A0A2J5HG60;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, 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=BDW42DRAFT_188970 {ECO:0000313|EMBL:PLN75932.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN75932.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) 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; KZ559632; PLN75932.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5HG60; -.
DR OrthoDB; 1424864at2759; -.
DR Proteomes; UP000235023; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; 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, ECO:0000313|EMBL:PLN75932.1};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT DOMAIN 38..148
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
SQ SEQUENCE 253 AA; 28511 MW; 58A2B271780AEF96 CRC64;
MEFPEPHIYL PQSFHTHTAI LFSSKTSKNQ NLASSLPNWR WVPNWRWVFP TSRDRWDTRF
QEEMCAWFDA YSLTDSLRES VLHIVGILED EIRLLGGTPS HVYLGGMSQG MATALCTLSC
ATGTGRIQGQ LGGFLGFCGW LPLPLGAQPK RLVSEYFLHT IFGSYNMSPG REVTSTSILS
TPVCLSHGTD DAWVPVEQGR QAAQISQQIT IQVEWDEFSG AEGDGHWIKE PEGFDQIVQF
VEKQCDRHQT ESQ
//
