ID S3CWT2_OPHP1 Unreviewed; 305 AA.
AC S3CWT2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=F503_03865 {ECO:0000313|EMBL:EPE05260.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE05260.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE05260.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE05260.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(2013).
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; KE148157; EPE05260.1; -; Genomic_DNA.
DR AlphaFoldDB; S3CWT2; -.
DR STRING; 1262450.S3CWT2; -.
DR VEuPathDB; FungiDB:F503_03865; -.
DR eggNOG; KOG2112; Eukaryota.
DR HOGENOM; CLU_049413_2_2_1; -.
DR OMA; HGTDDAY; -.
DR OrthoDB; 1424864at2759; -.
DR Proteomes; UP000016923; 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:UP000016923};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487}.
FT DOMAIN 70..193
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
SQ SEQUENCE 305 AA; 34009 MW; 24F19AE294C1D1C5 CRC64;
MVNVDLIEKG FGPVHIVEPQ AGHPHTHTAI LLHGRGSTGE EFAEELFETC LSHDRGPNIP
DDQRPTLADR LPTWRWVFPS SPSTWNAAFE ECMPAWFEAH SLADPTLRQD LQPPGLMASV
QHVEQMIDEE TKTLREAGHA SDARARLVLG GISLGGAVAL WALLGTKQPE QPLGGFAIAS
TWLPFAKEVE THLARGKARG EDEKEGSRFV QSFVAPLDRH LRQRQEQDQK TLSVLDTPVF
VGHGRDDAYV DIELGRQVEQ VLTGVGFTVQ WQEYEGAEQE GHWIKEPEEM DDLRTFFDVV
ASRAL
//
