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Database: UniProt
Entry: A0A1J1HF33_PLARL
LinkDB: A0A1J1HF33_PLARL
Original site: A0A1J1HF33_PLARL 
ID   A0A1J1HF33_PLARL        Unreviewed;       870 AA.
AC   A0A1J1HF33;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   Name=DHHC4 {ECO:0000313|EMBL:CRH02477.1};
GN   ORFNames=PRELSG_1420500 {ECO:0000313|EMBL:CRH02477.1};
OS   Plasmodium relictum.
OC   Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC   Plasmodiidae; Plasmodium; Plasmodium (Haemamoeba).
OX   NCBI_TaxID=85471 {ECO:0000313|EMBL:CRH02477.1, ECO:0000313|Proteomes:UP000220158};
RN   [1] {ECO:0000313|EMBL:CRH02477.1, ECO:0000313|Proteomes:UP000220158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SGS1 {ECO:0000313|EMBL:CRH02477.1,
RC   ECO:0000313|Proteomes:UP000220158};
RG   Pathogen Informatics;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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|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}.
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DR   EMBL; LN835309; CRH02477.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1J1HF33; -.
DR   VEuPathDB; PlasmoDB:PRELSG_1420500; -.
DR   OMA; ETKINCF; -.
DR   OrthoDB; 276762at2759; -.
DR   Proteomes; UP000220158; Chromosome 14.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR22883:SF438; PROTEIN S-ACYLTRANSFERASE 7-RELATED; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119}; Membrane {ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000220158};
KW   Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:CRH02477.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        34..58
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        70..90
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        182..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        236..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        847..865
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          134..269
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          331..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        331..356
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   870 AA;  103351 MW;  04E50BED5290765B CRC64;
     MKILKRSKSL ERQNFDKINN VQIYGENQIH CKGFFISGPA FLTVISSFLM IFIPVGIFHA
     FTSTWFFEKG IYFVTFLNLF FFVLTIYSFF KTSFMDPGII PRQKSVLNLY DVIIEQYRET
     QPPRQKEVLI NGHFYKLKYC YTCNIYRGLR TVHCSICDNC VEKFDHHCPW VGNCIGARNY
     KYFVFFVLNL YILICITLSA SIYKLVICIN KLSGDGYNTE KIFIHIWRVA ADSLILIIYT
     VLTLWFVIGL LCYHIYTILT NQTTYEQIKT FYQNDNPFNI GIVNNIKEVL FTKTRPSYIN
     FVNPQLQVVD KNCYHNIIVF NDKGVNIEED IREKSSSDNR KKDKKKMDSM EIRSINKKSS
     KKKKSSKDCI PPSHGSKIRI KSYNIKKKIN KEKISEEYDI TKISNISNKA IEKSAHLKFD
     KNKNIKYTKI KLPKIKNDDS EHLNEDVEEK NVSSHKRIIN LNNVGALFIK NNSSSSISTK
     NGNNKEMKKK RRDNYVDNEI DNEFYDYQEE LIDIEKRMLK KDDYIVIKNT NEKNGEYSNK
     MKKKQKKKIL YKTKESKQIR KKKIKYETKI NCFNSSIQVR KKRNFPILNK KRFSFIGNLK
     NKSEIYYIVS YCNEKKKKSS INSEKEFKKK ENIDEDKIFF KEYNRSTKKK EKMKLKENKR
     EEDIQKNVII DIYNNMPDER KTKINNEIIL EIPKKKEYES NTSLEEIEKR KKTNYIKYDR
     LYLVGKGCKL ENFSEIYEMK YAKMHNLKYK KINKKLKKNK LKLLSKSHIN IHLFYNNKEC
     TNVSNNINGN IDTLGKYESC NFNNIYFSKI KNINKIDNLK LLNYLVHKNK QNEIRSDMKK
     KSKVSKFFYF FTTFALIIKC IHIPSNNDND
//
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