ID   PFA3_NEUCR              Reviewed;         622 AA.
AC   Q7S7C5;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 3.
DT   25-MAY-2022, entry version 101.
DE   RecName: Full=Palmitoyltransferase pfa3;
DE            EC=2.3.1.225;
DE   AltName: Full=Palmitoyltransferase 3;
DE   AltName: Full=Protein fatty acyltransferase 3;
GN   Name=ptr-3; Synonyms=pfa3; ORFNames=B13M13.170, NCU01267;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12655011; DOI=10.1093/nar/gkg293;
RA   Mannhaupt G., Montrone C., Haase D., Mewes H.-W., Aign V., Hoheisel J.D.,
RA   Fartmann B., Nyakatura G., Kempken F., Maier J., Schulte U.;
RT   "What's in the genome of a filamentous fungus? Analysis of the Neurospora
RT   genome sequence.";
RL   Nucleic Acids Res. 31:1944-1954(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   PubMed=12712197; DOI=10.1038/nature01554;
RA   Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA   Jaffe D.B., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA   Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA   Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA   DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA   Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA   Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M., Paulsen I.,
RA   Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT   "The genome sequence of the filamentous fungus Neurospora crassa.";
RL   Nature 422:859-868(2003).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAE76126.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; BX842618; CAE76126.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CM002240; EAA31509.3; -; Genomic_DNA.
DR   RefSeq; XP_960745.3; XM_955652.3.
DR   AlphaFoldDB; Q7S7C5; -.
DR   STRING; 5141.EFNCRP00000004011; -.
DR   EnsemblFungi; EAA31509; EAA31509; NCU01267.
DR   GeneID; 3876895; -.
DR   KEGG; ncr:NCU01267; -.
DR   VEuPathDB; FungiDB:NCU01267; -.
DR   HOGENOM; CLU_024136_0_1_1; -.
DR   InParanoid; Q7S7C5; -.
DR   Proteomes; UP000001805; Chromosome 2, Linkage Group V.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
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..622
FT                   /note="Palmitoyltransferase pfa3"
FT                   /id="PRO_0000212957"
FT   TOPO_DOM        1..38
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        39..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        60..76
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        77..97
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        98..175
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        176..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        197..217
FT                   /note="Vacuolar"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        218..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        239..622
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          132..182
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          298..334
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          533..622
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        312..334
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        419..433
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        462..489
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   622 AA;  69714 MW;  2DCBA9B1491C7D78 CRC64;
     MDATPYTTSS TSTALDSPSS LSATMARRWA RKLERYCCTC VTYFPLAFVY SMTSWAAYVD
     VSLSTTPSRV TWLGHSYGFI AVVLYLLANW CYTYAVFTSP GSTTNEYGYS TLPTQAPPTA
     TSFTVKSNGE FRFCKKCQAR KPDRAHHCST CRRCVLKMDH HCPWLATCVG LRNHKAFLLF
     LIYTSVFCWV SFAGSASWVW EEIMSNTTYV ETLMPVNYIM LSVISGIIGI VLSAFCGWHI
     YLASRGQTTI ECLEKTRYLS PLRESMQRTY VNQHTPGQGI ALPKYGQQLL DIHQNTIPGV
     TRPEEGEEMR RMTTPSGSSQ RNDLASQHNP ELQAGSRRFT YDEMEHIRAR KRYEDYLDEQ
     DSTKLPHAFD LGTPRNLLHL FGTNAWLWPF PVCTTIGDGW SWEPNPKWIE ARDRIARERE
     EQRQRERQAG WGPADDDDIT PVYTPTWTPP NQQHPQGGAG RHYLQPSSQP QTQRNSNSSS
     PSFTPSRRTP SKADRILGRD PNMYADDEPV IYGKHDVAMS RLSPAGRTLV VEDDVLNDDD
     DDDEDYFQDA GRKQEDAEQS ALNVVTNGRW GRPAGASGVG LLAHGRPGGA RSPISPISPP
     ARGFGGSAKN GEEGRSNDDG VD