ID   PFA3_KLULA              Reviewed;         325 AA.
AC   Q6CPU8;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Palmitoyltransferase PFA3;
DE            EC=2.3.1.225;
DE   AltName: Full=Protein fatty acyltransferase 3;
GN   Name=PFA3; OrderedLocusNames=KLLA0E02068g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
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}.
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DR   EMBL; CR382125; CAG99128.1; -; Genomic_DNA.
DR   RefSeq; XP_454041.1; XM_454041.1.
DR   AlphaFoldDB; Q6CPU8; -.
DR   SMR; Q6CPU8; -.
DR   STRING; 28985.XP_454041.1; -.
DR   DNASU; 2894120; -.
DR   EnsemblFungi; CAG99128; CAG99128; KLLA0_E02069g.
DR   GeneID; 2894120; -.
DR   KEGG; kla:KLLA0_E02069g; -.
DR   eggNOG; KOG1315; Eukaryota.
DR   HOGENOM; CLU_027721_0_0_1; -.
DR   InParanoid; Q6CPU8; -.
DR   OMA; DFPTRSD; -.
DR   Proteomes; UP000000598; Chromosome E.
DR   GO; GO:0000329; C:fungal-type vacuole membrane; IEA:EnsemblFungi.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018345; P:protein palmitoylation; IEA:EnsemblFungi.
DR   GO; GO:0042144; P:vacuole fusion, non-autophagic; IEA:EnsemblFungi.
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..325
FT                   /note="Palmitoyltransferase PFA3"
FT                   /id="PRO_0000212956"
FT   TOPO_DOM        1..5
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        27..35
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        36..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        57..146
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        168..185
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        186..206
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        207..325
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          103..153
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ   SEQUENCE   325 AA;  37933 MW;  EB814ED28147DE97 CRC64;
     MLLDRIGFYF PKALSNFLIL YTCCICFSRI DILPRIVNVV LLITLSSFAL YTYWKIIRVG
     AGSPLEYSFL KIQSIDNVLN RTEQPPDIIK DNCIFVKRDG SFRFCQTCEI WKPDRCHHCS
     KCNKCFLKMD HHCPWFASCV GFRNQKFFVQ FLAYTTVYSL YVLLMTSAQL YSWFRQMKYK
     SELLDLHLLV VWVLSVIAAI ATFAFTTYTI WLVTKNETTI EQYEWGNIRH DLEIYGDSIN
     CNMGSVDNVF DLGSRSANFN CVMGASWAEL LLPIQVRADD PFDPYANQGL FFPVQSDTYR
     IYRESVNLQQ RLITRLTLRP SIEHI