ID   PFA5_KLULA              Reviewed;         349 AA.
AC   Q6CRV3;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Palmitoyltransferase PFA5;
DE            EC=2.3.1.225;
DE   AltName: Full=Protein fatty acyltransferase 5;
GN   Name=PFA5; OrderedLocusNames=KLLA0D06149g;
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   -!- 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; CR382124; CAH00432.1; -; Genomic_DNA.
DR   RefSeq; XP_453336.1; XM_453336.1.
DR   AlphaFoldDB; Q6CRV3; -.
DR   STRING; 28985.XP_453336.1; -.
DR   EnsemblFungi; CAH00432; CAH00432; KLLA0_D06149g.
DR   GeneID; 2892851; -.
DR   KEGG; kla:KLLA0_D06149g; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   HOGENOM; CLU_064801_0_0_1; -.
DR   InParanoid; Q6CRV3; -.
DR   OMA; YCVWIGT; -.
DR   Proteomes; UP000000598; Chromosome D.
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..349
FT                   /note="Palmitoyltransferase PFA5"
FT                   /id="PRO_0000212980"
FT   TRANSMEM        19..39
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        170..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          126..176
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   ACT_SITE        156
FT                   /note="S-palmitoyl cysteine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   349 AA;  40321 MW;  6317199DFA781E15 CRC64;
     MAWSLGTLRV TSHPYFRLLI PFLTVLLQCY GVWAFCHQFC YLQLYQRRNA KGACIGLIIV
     VLSLTFLIWY IWALMLVLGP GRQPTIPPFK IIPDSEIRTV SSESAVPDNS IAPPDIYPCD
     ERGYPIWCSN CQSLKMSRTH HSTKVGYCVP RFDHYCVWIG TVLGRLNYKL FVQFTFYLDL
     VVLILMISIA TQMRQMKGSA NGNVYAVFAL ACCALLMAGP LFLTHIYYMC YNRTSIEIIE
     VNNKAKASRK FFCIYNPCDG YRYVIQFCPG ENQDFWNKGN ILTNLKEFLG PNYLSWFIPS
     ILTHKQSYGK SSANYYDLIG DCNEVMSEKF QKYMIDKIER KEYVTRLVV