ID   PFA5_DEBHA              Reviewed;         411 AA.
AC   Q6BP97;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-DEC-2008, sequence version 2.
DT   25-MAY-2022, entry version 86.
DE   RecName: Full=Palmitoyltransferase PFA5;
DE            EC=2.3.1.225;
DE   AltName: Full=Protein fatty acyltransferase 5;
GN   Name=PFA5; OrderedLocusNames=DEHA2E15356g;
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   -!- 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; CR382137; CAG88222.2; -; Genomic_DNA.
DR   RefSeq; XP_459973.2; XM_459973.1.
DR   AlphaFoldDB; Q6BP97; -.
DR   STRING; 4959.XP_459973.2; -.
DR   EnsemblFungi; CAG88222; CAG88222; DEHA2E15356g.
DR   GeneID; 2902806; -.
DR   KEGG; dha:DEHA2E15356g; -.
DR   VEuPathDB; FungiDB:DEHA2E15356g; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   HOGENOM; CLU_715709_0_0_1; -.
DR   InParanoid; Q6BP97; -.
DR   OMA; DLFFCDE; -.
DR   OrthoDB; 1491968at2759; -.
DR   Proteomes; UP000000599; Chromosome E.
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   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..411
FT                   /note="Palmitoyltransferase PFA5"
FT                   /id="PRO_0000212977"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        156..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        319..339
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          112..162
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        142
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   411 AA;  48840 MW;  FA1E03488D9451E4 CRC64;
     MVFDPKLFKY AWAKRVIPIC VILGLGYIDF ACFYALGYRE IYKFHSHGVA ISLWVILAWC
     EVCVIAYWVL LVVTGPGKAP RVKPFNLYSS EDTSDLTPVP DYFFCDESGY PFWCSQCQSI
     KLPRTLHSKD RNYCILKFDH YCVWVGTVIG QRNYKYFLNF LIWFLMFFIV TLIYLSRYTK
     SNYDRGTKDI DHNYIVLYIL SGYWILILSS LLAAHLWYVV HNMTTIDDMN IKKVKRYSRW
     TSNNDKTKRK DVRKIPGEET GIRYINIRYN DTRVIVQYTL NDFPFSFGFK RNWQNLWLNN
     NRTNGDFTQH ESSYSRKRLA ISFLLFLVPY VDLVYPSRER INVSDVEKST LDSLYSHRLI
     EYEQYNDRLN DKFLDYINSK IKNNEFHMPR YLSPLAEDQQ SSSEGSRPDN I