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Database: UniProt
Entry: A0A182ESF1_ONCOC
LinkDB: A0A182ESF1_ONCOC
Original site: A0A182ESF1_ONCOC 
ID   A0A182ESF1_ONCOC        Unreviewed;       234 AA.
AC   A0A182ESF1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=NOO_LOCUS11070 {ECO:0000313|EMBL:VDM94822.1};
OS   Onchocerca ochengi (Filarial nematode worm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX   NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t11070-RA};
RN   [1] {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t11070-RA}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=22919073; DOI=10.1101/gr.138420.112;
RA   Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA   Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA   Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT   "Analysis of gene expression from the Wolbachia genome of a filarial
RT   nematode supports both metabolic and defensive roles within the
RT   symbiosis.";
RL   Genome Res. 22:2467-2477(2012).
RN   [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t11070-RA}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
RN   [3] {ECO:0000313|EMBL:VDM94822.1, ECO:0000313|Proteomes:UP000271087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-cysteinyl-[protein] + octadecanoyl-CoA = CoA + S-
CC         octadecanoyl-L-cysteinyl-[protein]; Xref=Rhea:RHEA:59740, Rhea:RHEA-
CC         COMP:10131, Rhea:RHEA-COMP:15434, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57394, ChEBI:CHEBI:143200;
CC         Evidence={ECO:0000256|ARBA:ARBA00023536};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59741;
CC         Evidence={ECO:0000256|ARBA:ARBA00023536};
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: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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}.
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DR   EMBL; UYRW01007180; VDM94822.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A182ESF1; -.
DR   STRING; 42157.A0A182ESF1; -.
DR   WBParaSite; nOo.2.0.1.t11070-RA; nOo.2.0.1.t11070-RA; nOo.2.0.1.g11070.
DR   Proteomes; UP000077448; Unassembled WGS sequence.
DR   Proteomes; UP000271087; Unassembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR12246:SF18; PALMITOYLTRANSFERASE; 1.
DR   PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR   Pfam; PF01529; DHHC; 2.
DR   PROSITE; PS50216; DHHC; 2.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119};
KW   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000271087};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        82..103
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        209..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          132..166
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   DOMAIN          193..230
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
SQ   SEQUENCE   234 AA;  26917 MW;  1E1323D1989FD083 CRC64;
     MALKHRKANS HEIETSNGTY MNLSVAEYQI IESPDWDDGS DCDIKRDLGK TMFRRLFHWG
     PLTAICITLI IGVAVTYVHL QWWPLTTVAS FLDLSLFLLF NYLTLINLSK SSFFGPGYAP
     YNWKPPKKED ESRLQYCRIC DGFKLPRAHH CSKCGRCVCK MDHHCRKYDC ISKKLDRIGR
     GGLELEQLLK RAWINNCVGH RNHALFVRFL ASATLGCIHA AIILSSTLYR FLSR
//
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