ID   PFA3_DEBHA              Reviewed;         405 AA.
AC   Q6BMV2; B5RU81;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Palmitoyltransferase PFA3;
DE            EC=2.3.1.225;
DE   AltName: Full=Protein fatty acyltransferase 3;
GN   Name=PFA3; OrderedLocusNames=DEHA2F02398g;
OS   Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990
OS   / NBRC 0083 / IGC 2968) (Yeast) (Torulaspora hansenii).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Debaryomyces.
OX   NCBI_TaxID=284592;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Palmitoyltransferase specific for VAC8. Palmitoylates VAC8 at
CC       one or more of its N-terminal cysteine residues, which is required for
CC       its proper membrane localization (By similarity). {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250}.
CC   -!- PTM: Autopalmitoylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA3
CC       subfamily. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CR382138; CAR66258.1; -; Genomic_DNA.
DR   RefSeq; XP_002770727.1; XM_002770681.1.
DR   AlphaFoldDB; Q6BMV2; -.
DR   SMR; Q6BMV2; -.
DR   STRING; 4959.XP_002770727.1; -.
DR   EnsemblFungi; CAR66258; CAR66258; DEHA2F02398g.
DR   GeneID; 8998861; -.
DR   KEGG; dha:DEHA2F02398g; -.
DR   VEuPathDB; FungiDB:DEHA2F02398g; -.
DR   eggNOG; KOG1315; Eukaryota.
DR   HOGENOM; CLU_027721_0_0_1; -.
DR   InParanoid; Q6BMV2; -.
DR   OMA; DFPTRSD; -.
DR   OrthoDB; 1491968at2759; -.
DR   Proteomes; UP000000599; Chromosome F.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005774; C:vacuolar membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW   Transferase; Transmembrane; Transmembrane helix; Vacuole.
FT   CHAIN           1..405
FT                   /note="Palmitoyltransferase PFA3"
FT                   /id="PRO_0000212953"
FT   TOPO_DOM        1..27
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        28..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        49..62
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        63..83
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        84..214
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        215..235
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        236..251
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        273..405
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          167..217
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ   SEQUENCE   405 AA;  47072 MW;  9067C67C8260BD1B CRC64;
     MLISHPRIMI RHAPWVTSIE TFCCSLATLF PKVFYTSVLT WSVYALIVHG CYDTLMTTQE
     TSIFAIAIGL IGLTLYILCL YTYFKVLRAG PGSPSDFEEL RIRNILSLSK PKYNSANPYD
     TNDNMATSAS LLANAEGVDE IESIESEQPP SEYMTLHMLK SNNSSYRYCT KCSVWKPDRC
     HHCSTCNRCV LRMDHHCPWF AMCVGFYNHK FFAQFLMYLT AYSGFDFVVS LSILWKFFAD
     EKYNDHYLSL NLVFLFVLSL AFFITVGGFS AFSLYLVFRN KTTIEFQENR WNFKNDKNGK
     SFQYEFDGSG KKKKLGNIFD LGCGRNWRSI MGPSWYYWLL PVTVTNKSID ARLENGINFE
     IDQDVYDRWC YNAQLQDQLN QQLADYKNRI RMEREANQTT DTNPF