ID   PFA3_CANGA              Reviewed;         332 AA.
AC   Q6FW70;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Palmitoyltransferase PFA3;
DE            EC=2.3.1.225;
DE   AltName: Full=Protein fatty acyltransferase 3;
GN   Name=PFA3; OrderedLocusNames=CAGL0D02508g;
OS   Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL
OS   Y-65) (Yeast) (Torulopsis glabrata).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Nakaseomyces;
OC   Nakaseomyces/Candida clade.
OX   NCBI_TaxID=284593;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65;
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; CR380950; CAG58435.1; -; Genomic_DNA.
DR   RefSeq; XP_445524.1; XM_445524.1.
DR   AlphaFoldDB; Q6FW70; -.
DR   SMR; Q6FW70; -.
DR   STRING; 5478.XP_445524.1; -.
DR   DNASU; 2886970; -.
DR   EnsemblFungi; CAG58435; CAG58435; CAGL0D02508g.
DR   GeneID; 2886970; -.
DR   KEGG; cgr:CAGL0D02508g; -.
DR   eggNOG; KOG1315; Eukaryota.
DR   HOGENOM; CLU_027721_0_0_1; -.
DR   InParanoid; Q6FW70; -.
DR   OMA; DFPTRSD; -.
DR   Proteomes; UP000002428; Chromosome D.
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..332
FT                   /note="Palmitoyltransferase PFA3"
FT                   /id="PRO_0000212952"
FT   TOPO_DOM        1..13
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        14..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        35..37
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        38..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        59..147
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        148..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        169..188
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        210..332
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          104..154
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ   SEQUENCE   332 AA;  38432 MW;  929FA622615E2318 CRC64;
     MNLVNNFSKL FPRCLTTGLY LWSLYAIVVC IHVIRARVVL PLVFTIAMVA LYTYAKLIYV
     GPGTTKEYSI LRVYDLNAAE SGFELPPEML VKRSYTQKRN GRFRVCKSCS SWKPDRCHHC
     STCNVCVLKM DHHCPWFAGC VGYRNQKFFI QFLIYCTVYS ILVLILSSME IYTWFKGEFF
     EVELINFTLL SLWLLALVVS ISITIFTVFS ISQVCQNQTT IELYSLRRYN EEVAFLNEFS
     NEPIKGTINI FDLGKKLINW EEVMGYSLIE WALPISRRPS SLDLEGSHSH GLFFNVNKNV
     SKTMNESVDL QDRLLRRLTP RSSLDVDRSN FV