ID   PFA5_CANGA              Reviewed;         352 AA.
AC   Q6FMP5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   25-MAY-2022, entry version 97.
DE   RecName: Full=Palmitoyltransferase PFA5;
DE            EC=2.3.1.225;
DE   AltName: Full=Protein fatty acyltransferase 5;
GN   Name=PFA5; OrderedLocusNames=CAGL0K06347g;
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   -!- 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: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; CR380957; CAG61460.1; -; Genomic_DNA.
DR   RefSeq; XP_448499.1; XM_448499.1.
DR   AlphaFoldDB; Q6FMP5; -.
DR   STRING; 5478.XP_448499.1; -.
DR   EnsemblFungi; CAG61460; CAG61460; CAGL0K06347g.
DR   GeneID; 2890431; -.
DR   KEGG; cgr:CAGL0K06347g; -.
DR   CGD; CAL0133845; CAGL0K06347g.
DR   VEuPathDB; FungiDB:CAGL0K06347g; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   HOGENOM; CLU_064801_0_0_1; -.
DR   InParanoid; Q6FMP5; -.
DR   OMA; YCVWIGT; -.
DR   Proteomes; UP000002428; Chromosome K.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:EnsemblFungi.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0018345; P:protein palmitoylation; 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.
FT   CHAIN           1..352
FT                   /note="Palmitoyltransferase PFA5"
FT                   /id="PRO_0000212976"
FT   TRANSMEM        12..32
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        195..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          114..164
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        144
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   352 AA;  41128 MW;  2CB697C2D1096BF2 CRC64;
     MGFAEWRLRN KYWTIYIVPL VVLLLMIYGT WAYCHKLCYE RVYRDFGHKA TAIGLICTCC
     VLDALIIAIW VLIVSCGPGH QPGVAPHLLV DSADLENTTV APNCYQSDPH GYPVWCSNCQ
     SLKVGRTKHS SHQGHCVPRF DHYCVWLGAV IGFKNYRLFV QFVFYFAVLL MIVWITISVY
     IRDIRQYHAR LNANLIVLLI ISGIGWLMTS GLFVSYIYYM SQNLTSIEVI DLKKRKRTPE
     LSMQRLYCYY NSDDHYRYVV KLDNDFKGSV YKKHWLKNIK EFMGSNPMLW FIPLPQYWHE
     SPLANGERDV NTIVSPYQEE VGPHTIDYIK KRIESGEYIH KFKEPGREKT HL