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Database: UniProt
Entry: A0A067BHX6_SAPPC
LinkDB: A0A067BHX6_SAPPC
Original site: A0A067BHX6_SAPPC 
ID   A0A067BHX6_SAPPC        Unreviewed;       460 AA.
AC   A0A067BHX6;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=SPRG_21755 {ECO:0000313|EMBL:KDO17743.1};
OS   Saprolegnia parasitica (strain CBS 223.65).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC   Saprolegnia.
OX   NCBI_TaxID=695850 {ECO:0000313|EMBL:KDO17743.1, ECO:0000313|Proteomes:UP000030745};
RN   [1] {ECO:0000313|EMBL:KDO17743.1, ECO:0000313|Proteomes:UP000030745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 223.65 {ECO:0000313|EMBL:KDO17743.1,
RC   ECO:0000313|Proteomes:UP000030745};
RX   PubMed=23785293;
RA   Jiang R.H., de Bruijn I., Haas B.J., Belmonte R., Lobach L., Christie J.,
RA   van den Ackerveken G., Bottin A., Bulone V., Diaz-Moreno S.M., Dumas B.,
RA   Fan L., Gaulin E., Govers F., Grenville-Briggs L.J., Horner N.R.,
RA   Levin J.Z., Mammella M., Meijer H.J., Morris P., Nusbaum C., Oome S.,
RA   Phillips A.J., van Rooyen D., Rzeszutek E., Saraiva M., Secombes C.J.,
RA   Seidl M.F., Snel B., Stassen J.H., Sykes S., Tripathy S., van den Berg H.,
RA   Vega-Arreguin J.C., Wawra S., Young S.K., Zeng Q., Dieguez-Uribeondo J.,
RA   Russ C., Tyler B.M., van West P.;
RT   "Distinctive expansion of potential virulence genes in the genome of the
RT   oomycete fish pathogen Saprolegnia parasitica.";
RL   PLoS Genet. 9:E1003272-E1003272(2013).
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; KK583577; KDO17743.1; -; Genomic_DNA.
DR   RefSeq; XP_012211550.1; XM_012356160.1.
DR   AlphaFoldDB; A0A067BHX6; -.
DR   STRING; 695850.A0A067BHX6; -.
DR   EnsemblProtists; KDO17743; KDO17743; SPRG_21755.
DR   GeneID; 24142327; -.
DR   KEGG; spar:SPRG_21755; -.
DR   VEuPathDB; FungiDB:SPRG_21755; -.
DR   OrthoDB; 71141at2759; -.
DR   Proteomes; UP000030745; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR039309; BT1.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR31585; FOLATE-BIOPTERIN TRANSPORTER 1, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR31585:SF5; RIBOSOMAL_L9 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF03092; BT1; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030745};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU079119}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT   TRANSMEM        60..77
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        98..117
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        129..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        244..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        290..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          212..324
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          346..404
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..460
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   460 AA;  50546 MW;  FE397FB87767ECD1 CRC64;
     MATTQKELGQ MDLQERVSYI QSATKDKDVD GDYADAKTPG ELDDGALVAG GALSLVSREA
     LALFSQYFAI GILYGMLPGM QYSVFQNYLK MEGYQVSAYG VLVVLGWSFK VFFGMLSDCV
     PIMGYRRKPW MLLGWTIATV CLCIMTFSSF PDPYCDARKI PCPKKVPTGV NMTAELRKWY
     NFDAPDQGGK ARNPAAAMAT RKWCVPVPAK PIRYCSACAK NSPGLDHHCT WLNTCIGEAN
     YEPFYLLILS GTCATLYQAV VGIVLATYWL DDVLVWHPAA HRDGLLVAIW LHNIICLVLG
     VAYGALTGFH TYLLYLRMGT YDFILKYGMQ NRCIRMLKCQ CLSPSRPLKT NVPSKTPKSP
     PTPAKKGDSV TPDSAADWKQ SRKLGPTAGN ATMAATKVSE GRRSTKISVV DELTDVPHAR
     RSGSIKSFEH LSVHEVQMAP APVSAAANND DPSMESDPLE
//
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