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PFA5_ASPFU
ID   PFA5_ASPFU              Reviewed;         443 AA.
AC   Q4WUK1;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Palmitoyltransferase pfa5;
DE            EC=2.3.1.225;
DE   AltName: Full=Protein fatty acyltransferase 5;
GN   Name=pfa5; ORFNames=AFUA_5G08740;
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Fumigati.
OX   NCBI_TaxID=330879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100;
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA   Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA   Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA   Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA   Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA   Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA   Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA   O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA   Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA   Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA   Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA   Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA   Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA   Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA   Barrell B.G., Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
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   -!- PTM: Autopalmitoylated. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA5
CC       subfamily. {ECO:0000305}.
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DR   EMBL; AAHF01000003; EAL91725.2; -; Genomic_DNA.
DR   RefSeq; XP_753763.2; XM_748670.2.
DR   AlphaFoldDB; Q4WUK1; -.
DR   STRING; 746128.CADAFUBP00005509; -.
DR   EnsemblFungi; EAL91725; EAL91725; AFUA_5G08740.
DR   GeneID; 3511558; -.
DR   KEGG; afm:AFUA_5G08740; -.
DR   VEuPathDB; FungiDB:Afu5g08740; -.
DR   eggNOG; KOG1315; Eukaryota.
DR   HOGENOM; CLU_034009_0_0_1; -.
DR   InParanoid; Q4WUK1; -.
DR   OMA; HYCPWAG; -.
DR   OrthoDB; 1491968at2759; -.
DR   Proteomes; UP000002530; Chromosome 5.
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: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.
FT   CHAIN           1..443
FT                   /note="Palmitoyltransferase pfa5"
FT                   /id="PRO_0000212974"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        57..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        220..240
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          175..225
FT                   /note="DHHC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
FT   REGION          96..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          410..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        106..122
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..137
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   443 AA;  49712 MW;  B262E2D1B31C338B CRC64;
     MARRAADKRV NLAVSRIIPP ILIGVFGYAS YAITKPLCVD YLIHPAHHYD RRSRSGAGAA
     ILAIYYVLLI PVLATYLRLL YNVVLSPGYL PRGTACTQNQ TGSDGSKHRH RRHRRRKSGH
     HLSKTTEKTD RSDGGDVERG LEYSARAKAY PLDAEGLESF YTKDVFVCQP DGRPVYCSTC
     CQFKTDRAHH CREVDRCVRK MDHFCPWVGG VVSETSFKFF IQFIVYTMIY CIFVLIVFAI
     YTAELRREAG RTNVHWIVCL ALSSLFGFFT FGVAISSVQL AANNLTTIEN LNRRSAVWTL
     AIRVPRHILS KRWAPTFRTI TYPLPPVPPA ESEVARESPG GEQHVFAILQ TLPGENPFDL
     GSPLKNIQQV MGFSLLEWLL PIKQSPCADH SSNESAFALG PVVTRLKKEA GLEVSTESES
     ADPVGAAETP QHEQRRGKHR RRN
 
 
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