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Database: UniProt
Entry: A0A0G4H5Q0_VITBC
LinkDB: A0A0G4H5Q0_VITBC
Original site: A0A0G4H5Q0_VITBC 
ID   A0A0G4H5Q0_VITBC        Unreviewed;       520 AA.
AC   A0A0G4H5Q0;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, 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=Vbra_10638 {ECO:0000313|EMBL:CEM38994.1};
OS   Vitrella brassicaformis (strain CCMP3155).
OC   Eukaryota; Sar; Alveolata; Colpodellida; Vitrellaceae; Vitrella.
OX   NCBI_TaxID=1169540 {ECO:0000313|EMBL:CEM38994.1, ECO:0000313|Proteomes:UP000041254};
RN   [1] {ECO:0000313|EMBL:CEM38994.1, ECO:0000313|Proteomes:UP000041254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Zhu J., Qi W., Song R.;
RL   Submitted (NOV-2014) 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; CDMY01001019; CEM38994.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4H5Q0; -.
DR   STRING; 1169540.A0A0G4H5Q0; -.
DR   VEuPathDB; CryptoDB:Vbra_10638; -.
DR   InParanoid; A0A0G4H5Q0; -.
DR   OrthoDB; 5491547at2759; -.
DR   Proteomes; UP000041254; 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:SF203; 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:UP000041254};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        42..63
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        69..87
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        155..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        200..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          110..244
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          314..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          421..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..348
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..385
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        435..454
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        485..499
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   520 AA;  57697 MW;  DA0AC3ABB6CDC74D CRC64;
     MRVASRGSPR VNKRAEESRK GDGAAAAGRK QEQKHTWITE EIASWAIFGL DVALYYVFCI
     PLLELPAKVG LGLVFGVTSI VVFYTAYMCT VIDPADMNIY ALPECVNMNE DDHVCGTCSS
     YVNKKSKHCR LCNKCVLNFD HHCKWLNNCI GKANYWYFLV LVVAVVVLTG LEVATAASLL
     GQHLLTDKVE DEWIEAYGEF SAVAFYILLI LVCVFNLPLL VLVLQLVLLH IWLIWHDLTT
     YEYIVLKSRQ MQEKMNRMEA LRAAGGYADT SPLDPKRLRQ QLQRCCGGLR AEGRTDETLP
     STCLDWIVFN KRRARRREPK GGSTQPEGHP HQPPHPPQGE PPLPRFPSRG PGQRAVPSGP
     FLELQIHTPP PAQSPVRTQN GAPPIPGDNT LEPYDDRLPT DLPVTRVGRN ESLAGHFAHD
     VNQSLALQPP EPLVASRDEA DRIREDDRSG GGRRAVHLDI PTPGVRPESS ATDAIEAPSM
     ALHDRQGLRQ TQSHTEQRSA PAEGRVPVAA HEGAGREQGR
//
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