ID Q8STX3_ENCCU Unreviewed; 275 AA.
AC Q8STX3;
DT 01-JUN-2002, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN OrderedLocusNames=ECU09_0230 {ECO:0000313|EMBL:CAD26994.1};
OS Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Unikaryonidae;
OC Encephalitozoon.
OX NCBI_TaxID=284813 {ECO:0000313|EMBL:CAD26994.1, ECO:0000313|Proteomes:UP000000819};
RN [1] {ECO:0000313|EMBL:CAD26994.1, ECO:0000313|Proteomes:UP000000819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-M1 {ECO:0000313|EMBL:CAD26994.1,
RC ECO:0000313|Proteomes:UP000000819};
RX PubMed=11719806; DOI=10.1038/35106579;
RA Katinka M.D., Duprat S., Cornillot E., Metenier G., Thomarat F.,
RA Prensier G., Barbe V., Peyretaillade E., Brottier P., Wincker P.,
RA Delbac F., El Alaoui H., Peyret P., Saurin W., Gouy M., Weissenbach J.,
RA Vivares C.P.;
RT "Genome sequence and gene compaction of the eukaryote parasite
RT Encephalitozoon cuniculi.";
RL Nature 414:450-453(2001).
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|ARBA:ARBA00001870,
CC 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}.
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DR EMBL; AL590451; CAD26994.1; -; Genomic_DNA.
DR RefSeq; XP_955575.1; XM_950482.1.
DR AlphaFoldDB; Q8STX3; -.
DR STRING; 284813.Q8STX3; -.
DR VEuPathDB; MicrosporidiaDB:ECU09_0230; -.
DR HOGENOM; CLU_027721_6_0_1; -.
DR InParanoid; Q8STX3; -.
DR OMA; RMHIAWL; -.
DR OrthoDB; 6683at2759; -.
DR Proteomes; UP000000819; Chromosome IX.
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; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000000819};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:CAD26994.1};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 40..61
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 130..153
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 165..188
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 79..205
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
SQ SEQUENCE 275 AA; 31988 MW; D3F3B0C71C7D468F CRC64;
MSEIRPNYRM MLLVFSLMFT YTAPVSEIIL PANFVFKKAY VVALVLSSIF SMVYLVLSIV
YRGRVKYDLE TIALASHLQT KKFCRRCNNY KPERAHHCSS CGYCIKKMDH HCFWINNCVN
YDNQGHFIRF LFFTASANIL IFVYVSIESA AILLFNHSLE HRRDYYILVL SGMLSLVFLI
MTAFFLYLQM RLALSNTTFI EELKQESMSR LQGSSILRSP YDRGIMSNLI DTLGPPYTLF
LLGPFGDGIT FIKTYPAEYW PVPYDYHCIE DLMVI
//
