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Database: UniProt
Entry: A0A0K3C9E5_RHOTO
LinkDB: A0A0K3C9E5_RHOTO
Original site: A0A0K3C9E5_RHOTO 
ID   A0A0K3C9E5_RHOTO        Unreviewed;       288 AA.
AC   A0A0K3C9E5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-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   Name=FGENESH: predicted gene_3.666 {ECO:0000313|EMBL:CTR06354.1};
GN   ORFNames=AAT19DRAFT_13503 {ECO:0000313|EMBL:PRQ76481.1},
GN   BN2166_0022150 {ECO:0000313|EMBL:CTR06354.1};
OS   Rhodotorula toruloides (Yeast) (Rhodosporidium toruloides).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Microbotryomycetes; Sporidiobolales; Sporidiobolaceae; Rhodotorula.
OX   NCBI_TaxID=5286 {ECO:0000313|EMBL:CTR06354.1, ECO:0000313|Proteomes:UP000199069};
RN   [1] {ECO:0000313|EMBL:CTR06354.1, ECO:0000313|Proteomes:UP000199069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Single colony {ECO:0000313|EMBL:CTR06354.1};
RA   Cajimat M.N.B., Milazzo M.L., Fulhorst C.F.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:PRQ76481.1, ECO:0000313|Proteomes:UP000239560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 0880 {ECO:0000313|EMBL:PRQ76481.1,
RC   ECO:0000313|Proteomes:UP000239560};
RX   PubMed=29521624;
RA   Coradetti S.T., Pinel D., Geiselman G., Ito M., Mondo S., Reilly M.C.,
RA   Cheng Y.F., Bauer S., Grigoriev I., Gladden J.M., Simmons B.A., Brem R.,
RA   Arkin A.P., Skerker J.M.;
RT   "Functional genomics of lipid metabolism in the oleaginous yeast
RT   Rhodosporidium toruloides.";
RL   Elife 7:0-0(2018).
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; CWKI01000003; CTR06354.1; -; Genomic_DNA.
DR   EMBL; LCTV02000003; PRQ76481.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K3C9E5; -.
DR   STRING; 5286.A0A0K3C9E5; -.
DR   OMA; CTHAPIR; -.
DR   OrthoDB; 4670340at2759; -.
DR   Proteomes; UP000199069; Unassembled WGS sequence.
DR   Proteomes; UP000239560; 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:UP000199069};
KW   Serine esterase {ECO:0000256|ARBA:ARBA00022487};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           37..288
FT                   /note="Acyl-protein thioesterase 1"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5033227079"
FT   DOMAIN          65..283
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
SQ   SEQUENCE   288 AA;  31897 MW;  48D4DEC99A944E6D CRC64;
     MRYTYNAPTG PARWILLAVA ALTLFLLLRP APPSETGETE DVSEMLKMYP TASDAETDTE
     VLGIGRHSAT VIFLHGLGGS AAMVFPLMEV IRPKLWQVSW LMPNSPRIPI TAAEGKVGPA
     WFDIDSFPEK TDLDPPLPTH EDEVAMKKAV DRVHKLIQGE LDRGIDSDRI VLAGFSQGCA
     ISLLAGLSSK EKLGGLMCMS GWLPLADQLK NGKHPYQTSH ANQLPVWMGH GDADQTIRHG
     WGLKTLDLLH GMGFKDVEFH TYSGLTHWTR ADELQDMRKW LQKRLPPT
//
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