ID A0A151GPM0_9HYPO Unreviewed; 1140 AA.
AC A0A151GPM0;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 16.
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=DCS_00138 {ECO:0000313|EMBL:KYK59011.1};
OS Drechmeria coniospora.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Drechmeria.
OX NCBI_TaxID=98403 {ECO:0000313|EMBL:KYK59011.1, ECO:0000313|Proteomes:UP000076580};
RN [1] {ECO:0000313|EMBL:KYK59011.1, ECO:0000313|Proteomes:UP000076580}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 6962 {ECO:0000313|EMBL:KYK59011.1,
RC ECO:0000313|Proteomes:UP000076580};
RX PubMed=26975455; DOI=10.1038/srep23122;
RA Zhang L., Zhou Z., Guo Q., Fokkens L., Miskei M., Pocsi I., Zhang W.,
RA Chen M., Wang L., Sun Y., Donzelli B.G., Gibson D.M., Nelson D.R.,
RA Luo J.G., Rep M., Liu H., Yang S., Wang J., Krasnoff S.B., Xu Y.,
RA Molnar I., Lin M.;
RT "Insights into Adaptations to a Near-Obligate Nematode Endoparasitic
RT Lifestyle from the Finished Genome of Drechmeria coniospora.";
RL Sci. Rep. 6:23122-23122(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KYK59011.1}.
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DR EMBL; LAYC01000001; KYK59011.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A151GPM0; -.
DR STRING; 98403.A0A151GPM0; -.
DR InParanoid; A0A151GPM0; -.
DR OrthoDB; 4670340at2759; -.
DR Proteomes; UP000076580; Chromosome 01.
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:UP000076580};
KW Serine esterase {ECO:0000256|ARBA:ARBA00022487};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..1140
FT /note="Acyl-protein thioesterase 1"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007580789"
FT DOMAIN 912..1132
FT /note="Phospholipase/carboxylesterase/thioesterase"
FT /evidence="ECO:0000259|Pfam:PF02230"
FT REGION 253..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 693..745
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 697..717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1140 AA; 123024 MW; 7C4950FBDE5449BC CRC64;
MRASSLALVA STVLGLQHVA AGKILLPAGG DPTAVEMSTD ARVVRHGAAA DGSNAVVLDD
AAEAKSLDRR DKQDPLPPDE LIKWMVENNV RNDCFFVTAA HLLDTTVEDI SRRAGVPLPR
PGVGGISLAE MFTALETLGL RFRAYTFQGT DETTGHGTPS AMRCRPGRSA FAGPTGRRVD
VMGLAYTRPD GSGHVVIIRH AFGTSRNAGT PYARCLDFQA KPGGLDVTRE VRRSNVCAYF
YVDFRTSSGA YVTGRRESVE QMNQRARLDS AEPMDYEPSG DEPGPSSAGE PMEVDEPPGD
GSDAVAVTEE PNSSLLPTDV VRDASSGGVD LSALSPETSN RILTDQLSQS ACAAMISLGI
IYTWRHQQKR WITEGQKSTI HKNNCKVLKS MVRPWSDRNA RCSRMSNLEF GFALSNDRFS
GTYDALQATL EGPAGSVTVP IAEGPSAGFS TWIPVDLKSA FGSDTIDIHA IKKISLSARG
LFFKLLGARN DWLKVQDIAL RARCATPGFD VEYHRLTGLN TWYQHPGGWF LAPFEWKSLA
TFDVGPKDWN MTPPCDTIRS LHYELKVANK AWAGTGDGLS FTLQGAKGRI AFAGPIKAGY
STSGMVDMMN MFGAKTVQIS AVRQISLLED FRGFVRDRWL LEGITLTAGC ANLPKQAMAM
KKFQTEYRWL GGDASNGTVW TGDMGPEDWM AVSETETETE TETKEGERRE TELQEAAMKD
SHGPPSADEG GKQEETEQPG HTWNCRSVDL TSSLPWFSWR TCMKSAADSR SICRLDLLLA
AVLMANEGSA GATSASGETN KRAISRIASA GTRANGKMAW RGTEAVRCSF QESEGGSVRT
AGFMHVWSRL RMLNPRLLFA LACALPVFAL LLSHLGVYKS PSAESATDSS SSSAPPTADV
MSSSVRRAAP LVFPAISRHT ATVIFIHGLG DTGAGWADAV EHWQRRQRLG EIKFILPNAP
VIPITMNNGF HMPGWFDIKT LGNAAASLDA KVDEDAAGIL QSRAYVHSLV EEEISAGIPS
ERVLLGGFSQ GGAMSIFAGL TAPVKIGGIV GLSSWLLLNQ TFGEHVPAGD INKATPVFMG
HGDRDPLVRH ELAQASEKAL KGMGYGVTLK TYRGMEHSAC LEELDEVAAF IESRLPPQGK
//
