ID L7JS94_TRAHO Unreviewed; 181 AA.
AC L7JS94;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=THOM_3161 {ECO:0000313|EMBL:ELQ73921.1};
OS Trachipleistophora hominis (Microsporidian parasite).
OC Eukaryota; Fungi; Fungi incertae sedis; Microsporidia; Pleistophoridae;
OC Trachipleistophora.
OX NCBI_TaxID=72359 {ECO:0000313|EMBL:ELQ73921.1, ECO:0000313|Proteomes:UP000011185};
RN [1] {ECO:0000313|EMBL:ELQ73921.1, ECO:0000313|Proteomes:UP000011185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23133373; DOI=10.1371/journal.ppat.1002979;
RA Heinz E., Williams T.A., Nakjang S., Noel C.J., Swan D.C., Goldberg A.V.,
RA Harris S.R., Weinmaier T., Markert S., Becher D., Bernhardt J., Dagan T.,
RA Hacker C., Lucocq J.M., Schweder T., Rattei T., Hall N., Hirt R.P.,
RA Embley T.M.;
RT "The genome of the obligate intracellular parasite Trachipleistophora
RT hominis: new insights into microsporidian genome dynamics and reductive
RT evolution.";
RL PLoS Pathog. 8:E1002979-E1002979(2012).
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; JH994097; ELQ73921.1; -; Genomic_DNA.
DR AlphaFoldDB; L7JS94; -.
DR VEuPathDB; MicrosporidiaDB:THOM_3161; -.
DR HOGENOM; CLU_1490013_0_0_1; -.
DR InParanoid; L7JS94; -.
DR OMA; CAWISGC; -.
DR Proteomes; UP000011185; 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; 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};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000011185};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 117..150
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 70..137
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
SQ SEQUENCE 181 AA; 21250 MW; E13FE459ADB38FCE CRC64;
MLIESILKRT IKVLELFLIT ITALYYITNL YICMRTRSLP SMYLLAVSLY YYIKTMRVHD
YVPPNKHVHG VCMRCHHLRY ASTHHCMLCD RCYDDRSHHC AWISGCVYGG NKNEFVFFVL
FAVLHGVCNL NVVTCFVVLM GCGFLVVYFL RGNRVAMDWR RAGYVLMPWL ERRAKVVDEE
C
//
