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Database: UniProt
Entry: A0A0R3VVY6_TAEAS
LinkDB: A0A0R3VVY6_TAEAS
Original site: A0A0R3VVY6_TAEAS 
ID   A0A0R3VVY6_TAEAS        Unreviewed;       332 AA.
AC   A0A0R3VVY6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=TASK_LOCUS1576 {ECO:0000313|EMBL:VDK23285.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000157501-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000157501-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK23285.1, ECO:0000313|Proteomes:UP000282613}
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: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {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; UYRS01000451; VDK23285.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0R3VVY6; -.
DR   STRING; 60517.A0A0R3VVY6; -.
DR   WBParaSite; TASK_0000157501-mRNA-1; TASK_0000157501-mRNA-1; TASK_0000157501.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; 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:SF43; PALMITOYLTRANSFERASE APP; 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:UP000282613};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        32..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        57..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          14..57
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          204..240
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          255..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        211..240
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        265..280
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        283..299
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..320
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   332 AA;  37037 MW;  EE76314E7FE39854 CRC64;
     MLIIGFSFLF LFTERFDHHC PWVGNCVGAR NYRYFVIFLL AVSLLCFYVL CFSVVNVVLK
     ILFTIFLCLS ISGLAFYHVY LSCREISTHE DIRHFPKTLR QMGRENPFSK GNGIVNMLGV
     LCGPAPPSIV LDFFSSTTMM ADAQSNPDRQ LRLEMVTGTL KAWKLVDPEV VRSLNSPMLS
     SPHPRSVEDL AMYHKQSVAA RPLRFDSGTQ QGEVDWRNTT GGYPRQAPTN SVTSQNIGRS
     TLTRRLRDLI GEFLRRHGPL LKRDKKPQSQ SSTSSTKPPK KPRKVTLAGE LDEHGDRMPS
     TGFAGRSIVS MTTTLPHSAP PSHAASIGHP DG
//
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