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Database: UniProt
Entry: A0A232EHX9_9HYME
LinkDB: A0A232EHX9_9HYME
Original site: A0A232EHX9_9HYME 
ID   A0A232EHX9_9HYME        Unreviewed;       690 AA.
AC   A0A232EHX9;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=TSAR_014068 {ECO:0000313|EMBL:OXU17944.1};
OS   Trichomalopsis sarcophagae.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Proctotrupomorpha;
OC   Chalcidoidea; Pteromalidae; Pteromalinae; Trichomalopsis.
OX   NCBI_TaxID=543379 {ECO:0000313|EMBL:OXU17944.1, ECO:0000313|Proteomes:UP000215335};
RN   [1] {ECO:0000313|EMBL:OXU17944.1, ECO:0000313|Proteomes:UP000215335}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Alberta {ECO:0000313|EMBL:OXU17944.1,
RC   ECO:0000313|Proteomes:UP000215335};
RC   TISSUE=Whole body {ECO:0000313|EMBL:OXU17944.1};
RX   PubMed=28648823; DOI=10.1016/j.cub.2017.05.032;
RA   Martinson E.O., Mrinalini, Kelkar Y.D., Chang C.H., Werren J.H.;
RT   "The Evolution of Venom by Co-option of Single-Copy Genes.";
RL   Curr. Biol. 27:2007-2013(2017).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-
CC         hexadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:36683, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:11032, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57379, ChEBI:CHEBI:74151;
CC         EC=2.3.1.225; Evidence={ECO:0000256|RuleBase:RU079119};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000256|RuleBase:RU079119}.
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:OXU17944.1}.
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DR   EMBL; NNAY01004405; OXU17944.1; -; Genomic_DNA.
DR   STRING; 543379.A0A232EHX9; -.
DR   Proteomes; UP000215335; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR22883:SF203; PALMITOYLTRANSFERASE; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119}; Membrane {ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000215335};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        190..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        250..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          148..290
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          46..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          545..607
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          642..690
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        552..572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        584..598
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  75901 MW;  063C30CE746CF244 CRC64;
     MSTAVRHAKR AQQPTAAPAA AQLHQHRSHP PRTSLVSLLL TPRDRTHATG AASLPANSRA
     AAAPSPTAVP RLARARRRRS XXXXXXXXXX LRPPVCAVVG SAFLVHLAAH LCALLLDPAE
     AEVRRQPASK VVSEFDRSKH LHVIENGRCH LCNVDASSKR TKHCSVCNKC VARFDHHCKW
     LNNCVGRRNY AAFIVCLVSA IVIALAVLGL VVAELSLVRL ESSLWAEHNA TDMDNVTLPL
     SLPLPGTGSL IVISIVGILS AIAAVLLIHL CFFHGYIACL GVTTYEYLRS KQHKQNAVAT
     NASSGATITE ENGRNGGIAA ACLNNRPSFC NQQQQPQQDA PLRYHFCETV NANDGSRSDS
     RNIYICSTHT STTTTAQISQ QSQNGCNTLQ TTTIQQRSDM EKERRNFHLY FSYDSRCNET
     QIELTSTQTV LNADGSQQQQ QIQQIQQFDR PPLELKPSTP SPVSCCFSIM GPSSTASLEK
     AKQRKLRQAN AELQLDERHH DGKPPLSARS CTTMRRIQTF LRTRLRKNAR QRAINAEACS
     ARKNKINPLT AGSESKEDDR SSKNEPIRCI AVEPREDSVS PLPPLPMVQQ QQQLQPPTKL
     PPLTLPSRHR LGKSELVLAD PASLAIVKRN QPHLRVRRAS LGHKRPRFKV GPHLAQSAQL
     SPIPESELSK PASPRSPPLN HFTFPPLNSS
//
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