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Database: UniProt
Entry: Q8IE90_PLAF7
LinkDB: Q8IE90_PLAF7
Original site: Q8IE90_PLAF7 
ID   Q8IE90_PLAF7            Unreviewed;       676 AA.
AC   Q8IE90;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 145.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=PF3D7_1322500 {ECO:0000313|EMBL:CAD52373.1};
OS   Plasmodium falciparum (isolate 3D7).
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX   NCBI_TaxID=36329 {ECO:0000313|EMBL:CAD52373.1, ECO:0000313|Proteomes:UP000001450};
RN   [1] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368864; DOI=10.1038/nature01097;
RA   Gardner M.J., Hall N., Fung E., White O., Berriman M., Hyman R.W.,
RA   Carlton J.M., Pain A., Nelson K.E., Bowman S., Paulsen I.T., James K.,
RA   Eisen J.A., Rutherford K., Salzberg S.L., Craig A., Kyes S., Chan M.S.,
RA   Nene V., Shallom S.J., Suh B., Peterson J., Angiuoli S., Pertea M.,
RA   Allen J., Selengut J., Haft D., Mather M.W., Vaidya A.B., Martin D.M.,
RA   Fairlamb A.H., Fraunholz M.J., Roos D.S., Ralph S.A., McFadden G.I.,
RA   Cummings L.M., Subramanian G.M., Mungall C., Venter J.C., Carucci D.J.,
RA   Hoffman S.L., Newbold C., Davis R.W., Fraser C.M., Barrell B.;
RT   "Genome sequence of the human malaria parasite Plasmodium falciparum.";
RL   Nature 419:498-511(2002).
RN   [2] {ECO:0000313|Proteomes:UP000001450}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Isolate 3D7 {ECO:0000313|Proteomes:UP000001450};
RX   PubMed=12368867; DOI=10.1038/nature01095;
RA   Hall N., Pain A., Berriman M., Churcher C., Harris B., Harris D.,
RA   Mungall K., Bowman S., Atkin R., Baker S., Barron A., Brooks K.,
RA   Buckee C.O., Burrows C., Cherevach I., Chillingworth C., Chillingworth T.,
RA   Christodoulou Z., Clark L., Clark R., Corto C., Cronin A., Davies R.,
RA   Davies P., Dear P., Dearden F., Doggett J., Feltwell T., Goble A.,
RA   Goodhead I., Gwilliam R., Hamlin N., Hance Z., Harper D., Hauser H.,
RA   Hornsby T., Holroyd S., Horrocks P., Humphray S., Jagels K., James D.,
RA   Johnson D., Kerhornou A., Knight A., Kontfortov B., Keyes S., Larke N.,
RA   Lawson D., Lennard N., Line A., Maddison M., McLean J., Mooney P.,
RA   Moule S., Murphy L., Oliver K., Ormond D., Price C., Quail M.A.,
RA   Rabbinowitsch E., Rajandream M-A., Rutter S., Rutherford K.M., Sanders M.,
RA   Simmonds M., Seeger K., Sharp S., Smith R., Squares R., Squares S.,
RA   Stevens K., Taylor K., Tivey A., Unwin L., Whitehead S., Woodward J.,
RA   Sulston J.E., Craig A., Newbold C., Barrell B.G.;
RT   "Sequence of Plasmodium falciparum chromosomes 1, 3-9 and 13.";
RL   Nature 419:527-531(2002).
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; Evidence={ECO:0000256|ARBA:ARBA00001870,
CC         ECO:0000256|RuleBase:RU079119};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family.
CC       {ECO:0000256|RuleBase:RU079119}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU079119}.
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DR   EMBL; AL844509; CAD52373.1; -; Genomic_DNA.
DR   RefSeq; XP_001349965.1; XM_001349929.1.
DR   AlphaFoldDB; Q8IE90; -.
DR   SMR; Q8IE90; -.
DR   STRING; 36329.Q8IE90; -.
DR   PaxDb; 5833-MAL13P1-126; -.
DR   EnsemblProtists; CAD52373; CAD52373; PF3D7_1322500.
DR   GeneID; 813676; -.
DR   KEGG; pfa:PF3D7_1322500; -.
DR   VEuPathDB; PlasmoDB:PF3D7_1322500; -.
DR   HOGENOM; CLU_407426_0_0_1; -.
DR   InParanoid; Q8IE90; -.
DR   OMA; DVPDCNG; -.
DR   OrthoDB; 246226at2759; -.
DR   PhylomeDB; Q8IE90; -.
DR   Proteomes; UP000001450; Chromosome 13.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; ISS:GeneDB.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; ISS:GeneDB.
DR   GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR22883:SF485; PALMITOYLTRANSFERASE; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   SMART; SM00248; ANK; 5.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119};
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Membrane {ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001450};
KW   Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:CAD52373.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        48..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        81..98
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        110..132
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        293..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        329..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        518..540
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        552..574
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   REPEAT          44..76
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          473..591
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          369..388
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   676 AA;  80837 MW;  C87687553D8A3075 CRC64;
     MNNSTSCVSI NVQDILFNLA KQKDERIFYF LEKDKTLINI QDGNGNSLLH WAVFLNNVYL
     VYYLLENNAE RDIKSHSKQT PLFWAICSNN ILMIYILNKY GSNLFQEDDK GYNCLIISIQ
     YNHILAFFYL LYLNIAITHK DYNNCTVIDW AAYNNNLFFL RFFSIFMNNL YSLNLNTPTS
     TLHKAIIGNS YEACVYLIMN KHQNVYDIGT DDKKTILQFV EDNKSKIDPR IYQFLNSKQV
     YRICQKKANR NIDRNRNFLY EANGTIGPYT IKKKKKLPIF LSIYTKYIEN KAILLYPLML
     LFLYVYLNIT YFLYARKYIN GQQLYLDLFH PFLFVIYYFV VTSNPGYLEN NKNNVPNINL
     EGKKKKDMNM KCRNGDNDKD TYNDVDTKDE EYKDKPLNDY DKKANNKERP KENITFQYII
     KNITDEINRY ERKYKLVEFA KRIKKENIFE LKNSMEINWD IPPIEFTEIN MNMLCPTCFL
     FKNIRTKHCS LCDKCVEIFD HHCDFTLNCM GIENARIFLL WILLNIFFSF SIIYIYGWFI
     FNSSLNYYNI KFYIILMAIV LSILIIYFMG AIFIRSIMNI LENITSNEKF KIYTYKTFFT
     YELTMDEKKQ PTVIRKFKNP FDQGMLFNFI NFLTKSKTKL IKKEKQFIII DKNIKSQKLT
     EFVDKLNKRL NEMNIE
//
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