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Entry: A0A1A6ABG5_9TREE
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ID   A0A1A6ABG5_9TREE        Unreviewed;       316 AA.
AC   A0A1A6ABG5;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=I303_01596 {ECO:0000313|EMBL:OBR87394.1};
OS   Kwoniella dejecticola CBS 10117.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Tremellales; Cryptococcaceae; Kwoniella.
OX   NCBI_TaxID=1296121 {ECO:0000313|EMBL:OBR87394.1, ECO:0000313|Proteomes:UP000078595};
RN   [1] {ECO:0000313|EMBL:OBR87394.1, ECO:0000313|Proteomes:UP000078595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 10117 {ECO:0000313|EMBL:OBR87394.1,
RC   ECO:0000313|Proteomes:UP000078595};
RG   The Broad Institute Genome Sequencing Platform;
RA   Cuomo C., Litvintseva A., Chen Y., Heitman J., Sun S., Springer D.,
RA   Dromer F., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A.,
RA   Alvarado L., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Cryptococcus dejecticola CBS10117.";
RL   Submitted (JUL-2013) 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|ARBA:ARBA00001870,
CC         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; KI894028; OBR87394.1; -; Genomic_DNA.
DR   RefSeq; XP_018265236.1; XM_018404955.1.
DR   AlphaFoldDB; A0A1A6ABG5; -.
DR   STRING; 1296121.A0A1A6ABG5; -.
DR   GeneID; 28965295; -.
DR   VEuPathDB; FungiDB:I303_01596; -.
DR   OrthoDB; 1387838at2759; -.
DR   Proteomes; UP000078595; 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:SF488; 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};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|RuleBase:RU079119};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078595};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        144..165
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        177..196
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          100..212
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          1..45
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..44
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   316 AA;  36074 MW;  CD438E50E4FCEC67 CRC64;
     MVVTGPGIAT THVPKSAHPE PTDFRMENFG ISNLSSSQGS DPAEAPQISE LAPIGNLIHD
     TLVTHRPSSD FGTEAPLKGS KVKDWRTVER PLPPLPPPVR WCQYCEIVKP PRTHHCRHCG
     VCILQFDHHC LWIGQCVGWG NHKFFIIFTF WGAIFCIYTF VFLVVSSTKS SNTDGQVVAM
     IVLSALFGLF TLSMYLSHIH LIVTGRTTVE SFASRDQHDA ESRVLQQEYG YFFHNSERRK
     VQKKWKEEWG NTPVDARWIF GTKMEMWEQE MGKSRLGWIL PIGRPLGDGI HYESNRRFGP
     NGEWLKKKDW PKDLQI
//
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