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Database: UniProt
Entry: A0A165N9Q1_EXIGL
LinkDB: A0A165N9Q1_EXIGL
Original site: A0A165N9Q1_EXIGL 
ID   A0A165N9Q1_EXIGL        Unreviewed;       388 AA.
AC   A0A165N9Q1;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=EXIGLDRAFT_667476 {ECO:0000313|EMBL:KZW00426.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW00426.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW00426.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW00426.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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; KV425901; KZW00426.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165N9Q1; -.
DR   STRING; 1314781.A0A165N9Q1; -.
DR   InParanoid; A0A165N9Q1; -.
DR   OrthoDB; 6683at2759; -.
DR   Proteomes; UP000077266; 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:SF23; PALMITOYLTRANSFERASE ZDHHC6; 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:UP000077266};
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        17..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        50..75
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        161..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        199..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          113..236
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
SQ   SEQUENCE   388 AA;  43676 MW;  39A1F5F0AC42E080 CRC64;
     MSNDDGASQG GRRWYHFIPL CFAVLIILSP HPSLIVLLTS FQLQTLNSPL LFVTHILVIY
     SLTFMAYSSL IVCVVRDPGP VGPPPAADED SEETTLTDAL RSIKAADDDY DKPGRWCRRC
     WAPKPERAHH CSICDRCVLK MDHHCPWMGG RCIGHRTYPS FVHFIFTTTM LSVYVAGVAI
     SALYYIIKHP YELGETVPLH VLLLVVLGGA FTLMMGSFAG YHAYLISTNQ TTIEHLSPFL
     LLRFLPEPLP PPSRTANNQT LTAEQQDSPY YFPSPVEPRP PWVPQEHELS YKQRRMVQRA
     HEKLRMYDLG FKRNWAAIFG VPELSGKRNH ARWKLWAARI LWGGGAALGD GRTFPANPRA
     DSQLAELAMK LYGEDDQRPR DSSASSDA
//
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