(data stored in ACNUC16935 zone)

SWISSPROT: PFA4_EMENI

ID   PFA4_EMENI              Reviewed;         435 AA.
AC   Q5BD15; C8VN05;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 1.
DT   05-JUL-2017, entry version 77.
DE   RecName: Full=Palmitoyltransferase pfa4 {ECO:0000255|HAMAP-Rule:MF_03199};
DE            EC=2.3.1.225 {ECO:0000255|HAMAP-Rule:MF_03199};
DE   AltName: Full=Protein S-acyltransferase {ECO:0000255|HAMAP-Rule:MF_03199};
DE            Short=PAT {ECO:0000255|HAMAP-Rule:MF_03199};
DE   AltName: Full=Protein fatty acyltransferase 4 {ECO:0000255|HAMAP-Rule:MF_03199};
GN   Name=pfa4 {ECO:0000255|HAMAP-Rule:MF_03199}; ORFNames=AN1565;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL
OS   194 / M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R.,
RA   Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J.,
RA   Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J.,
RA   Purcell S., Harris S., Braus G.H., Draht O., Busch S., D'Enfert C.,
RA   Bouchier C., Goldman G.H., Bell-Pedersen D., Griffiths-Jones S.,
RA   Doonan J.H., Yu J., Vienken K., Pain A., Freitag M., Selker E.U.,
RA   Archer D.B., Penalva M.A., Oakley B.R., Momany M., Tanaka T.,
RA   Kumagai T., Asai K., Machida M., Nierman W.C., Denning D.W.,
RA   Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P.,
RA   von Dohren H., Doonan J., Driessen A.J., Durek P., Espeso E.,
RA   Fekete E., Flipphi M., Estrada C.G., Geysens S., Goldman G.,
RA   de Groot P.W., Hansen K., Harris S.D., Heinekamp T., Helmstaedt K.,
RA   Henrissat B., Hofmann G., Homan T., Horio T., Horiuchi H., James S.,
RA   Jones M., Karaffa L., Karanyi Z., Kato M., Keller N., Kelly D.E.,
RA   Kiel J.A., Kim J.M., van der Klei I.J., Klis F.M., Kovalchuk A.,
RA   Krasevec N., Kubicek C.P., Liu B., Maccabe A., Meyer V., Mirabito P.,
RA   Miskei M., Mos M., Mullins J., Nelson D.R., Nielsen J., Oakley B.R.,
RA   Osmani S.A., Pakula T., Paszewski A., Paulsen I., Pilsyk S., Pocsi I.,
RA   Punt P.J., Ram A.F., Ren Q., Robellet X., Robson G., Seiboth B.,
RA   van Solingen P., Specht T., Sun J., Taheri-Talesh N., Takeshita N.,
RA   Ussery D., vanKuyk P.A., Visser H., van de Vondervoort P.J.,
RA   de Vries R.P., Walton J., Xiang X., Xiong Y., Zeng A.P., Brandt B.W.,
RA   Cornell M.J., van den Hondel C.A., Visser J., Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a
RT   community effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
CC   -!- FUNCTION: Mediates the reversible addition of palmitate to target
CC       proteins, thereby regulating their membrane association and
CC       biological function. {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- CATALYTIC ACTIVITY: Palmitoyl-CoA + [protein]-L-cysteine =
CC       [protein]-S-palmitoyl-L-cysteine + CoA. {ECO:0000255|HAMAP-
CC       Rule:MF_03199}.
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC       {ECO:0000255|HAMAP-Rule:MF_03199}; Multi-pass membrane protein
CC       {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase
CC       activity. {ECO:0000255|HAMAP-Rule:MF_03199}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA4
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03199}.
DR   EMBL; AACD01000025; EAA64272.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85122.1; -; Genomic_DNA.
DR   RefSeq; XP_659169.1; XM_654077.1.
DR   STRING; 162425.CADANIAP00008195; -.
DR   EnsemblFungi; CADANIAT00008195; CADANIAP00008195; CADANIAG00008195.
DR   EnsemblFungi; EAA64272; EAA64272; AN1565.2.
DR   GeneID; 2875674; -.
DR   KEGG; ani:AN1565.2; -.
DR   HOGENOM; HOG000158571; -.
DR   InParanoid; Q5BD15; -.
DR   KO; K18932; -.
DR   OMA; WEENGFN; -.
DR   OrthoDB; EOG092C2B8O; -.
DR   Proteomes; UP000000560; Chromosome VII.
DR   Proteomes; UP000005890; Partially assembled WGS sequence.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
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   HAMAP; MF_03199; DHHC_PAT_PFA4; 1.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   InterPro; IPR033682; PFA4.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q5BD15.
DR   SWISS-2DPAGE; Q5BD15.
KW   Acyltransferase; Complete proteome; Endoplasmic reticulum;
KW   Lipoprotein; Membrane; Palmitate; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN         1    435       Palmitoyltransferase pfa4.
FT                                /FTId=PRO_0000212966.
FT   TOPO_DOM      1     10       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TRANSMEM     11     31       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TOPO_DOM     32     48       Lumenal. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TRANSMEM     49     69       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TOPO_DOM     70    129       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TRANSMEM    130    150       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TOPO_DOM    151    179       Lumenal. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TRANSMEM    180    200       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   TOPO_DOM    201    435       Cytoplasmic. {ECO:0000255|HAMAP-
FT                                Rule:MF_03199}.
FT   DOMAIN       91    141       DHHC. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00067}.
FT   ACT_SITE    121    121       S-palmitoyl cysteine intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_03199}.
SQ   SEQUENCE   435 AA;  50007 MW;  567AB44B60D3CCA6 CRC64;
     MLCSSFSVSR LAIPAVCILI AFLAYTSQIF FLYFEDAPLK EDEVWRINIL AICIWICYYR
     ACTVDPGHVP KGWMPSDRER LKADRASGRQ RWCRRCEAYK PPRAHHCKTC ERCVPKMDHH
     CPWTSNCVSH FTFPHFARFL FYAVVGIAYL ETRLWQRVSK VWGSRHLPSY LGPSMGQIGH
     LFVLFVTNSL TLFALSLLLL RTLWSLGSNT TTIESWEIER HETLLRRARR LGGSLPGPGG
     ISVHITKQEF PYDIGIWSNI RAGMGGSANV LSWFWPLART PDRSTGLEFE ENGFEDPTVS
     WPPPDPDRIP LPPMDQRDSF MYDITDTSGT SGQIDIEAFN RRKEADLRRR RAPTEIERRK
     PFHVRLEEYS NGSSDAEADT GSDDDSDHGE EGWKNSEGER LRDFGVDEEA EFYDEEDIPL
     ALLIQQRAKR QHLSQ
//

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