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Database: UniProt
Entry: A0A0R3X018_HYDTA
LinkDB: A0A0R3X018_HYDTA
Original site: A0A0R3X018_HYDTA 
ID   A0A0R3X018_HYDTA        Unreviewed;       577 AA.
AC   A0A0R3X018;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=TTAC_LOCUS6424 {ECO:0000313|EMBL:VDM30633.1};
OS   Hydatigena taeniaeformis (Feline tapeworm) (Taenia taeniaeformis).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Hydatigera.
OX   NCBI_TaxID=6205 {ECO:0000313|Proteomes:UP000046396, ECO:0000313|WBParaSite:TTAC_0000643901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TTAC_0000643901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDM30633.1, ECO:0000313|Proteomes:UP000274429}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) 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; UYWX01020303; VDM30633.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3X018; -.
DR   STRING; 6205.A0A0R3X018; -.
DR   WBParaSite; TTAC_0000643901-mRNA-1; TTAC_0000643901-mRNA-1; TTAC_0000643901.
DR   Proteomes; UP000046396; Unplaced.
DR   Proteomes; UP000274429; 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; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR22883:SF433; PALMITOYLTRANSFERASE; 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:UP000274429};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        16..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        136..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        172..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          89..211
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          260..313
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..532
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          553..577
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..296
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        427..460
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        468..486
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   577 AA;  64333 MW;  F1C7E1939EC46096 CRC64;
     MGCHTFSCWE FSQTHGYIII ILQFILLFYV ISNFARATFM DPGYLPRGLP SGSPIIQIGV
     PGEKVMSNDK TSPPRPLMYK TVQINGVSTR LKWCVTCEIY RLPRCSHCSI CKHCIDTFDH
     HCPWVNNCIG RRNYRFFFLF LLSLTFHMIM TFTVSLLFVL ERQQNLMTTE GIIANVILIL
     VGLIFIPVVG LTGFHIYLVF NGLTTNEQVT SKYGDNHSPF DRGPCSNCVF MCCRPLGAIL
     IRKPVTGAAM QLSLQAKYRQ KMRRSNKNSR TKGVNGRVNT YSSGVRPNTS DPQPPILMSE
     LGNRLDGDTN ASPKDLLLRL NNEETSLAQV QSFSLTDKRD DSQYPSANYQ AGSVSFPDNL
     PVGFSYRAPD KPTGVNPGES TGRIFSCKHL AEDRPIQAGH QTSRSPMDYN ASVVYSMQPN
     APLVPPHLPS RSSSISKLRQ PTLVVPKTAN VPPSSSSRLK AIEEPSRHRL QQPQQQQPQN
     IPASAYTGGT VLPKYPVKQA PNATQSTNSR NPSRDKRLHH YTPRQPGYSA PVTSEGYFAS
     QQPQTLREYH FAQQPPRGNS AIISSEEAPD GTFEISV
//
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