ID A0A0W0FME4_9AGAR Unreviewed; 500 AA.
AC A0A0W0FME4;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=WG66_9941 {ECO:0000313|EMBL:KTB37457.1};
OS Moniliophthora roreri.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB37457.1, ECO:0000313|Proteomes:UP000054988};
RN [1] {ECO:0000313|EMBL:KTB37457.1, ECO:0000313|Proteomes:UP000054988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB37457.1,
RC ECO:0000313|Proteomes:UP000054988};
RA Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT pod rot of cacao.";
RL Submitted (DEC-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KTB37457.1}.
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DR EMBL; LATX01001846; KTB37457.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0W0FME4; -.
DR eggNOG; ENOG502QQMK; Eukaryota.
DR Proteomes; UP000054988; 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 Gene3D; 3.30.470.10; -; 1.
DR Gene3D; 3.20.10.10; D-amino Acid Aminotransferase, subunit A, domain 2; 1.
DR InterPro; IPR001544; Aminotrans_IV.
DR InterPro; IPR036038; Aminotransferase-like.
DR InterPro; IPR043132; BCAT-like_C.
DR InterPro; IPR043131; BCAT-like_N.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR Pfam; PF01063; Aminotran_4; 1.
DR Pfam; PF01529; DHHC; 1.
DR SUPFAM; SSF56752; D-aminoacid aminotransferase-like PLP-dependent enzymes; 1.
PE 3: Inferred from homology;
KW Acyltransferase {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:UP000054988};
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 241..261
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 267..288
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 338..357
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 377..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 326..416
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
SQ SEQUENCE 500 AA; 56569 MW; E7E4F6483D8A1C1D CRC64;
MSYQLLSSTR YDALLLSLRW NNDGTENDIV PSCFLLLKYH YHRLRDAAEE HGWAIAAGSI
SYEGLKEECV RAVEEAGTGT SYRIRITLSE TGLVAVIASP VPPLTADPSS ASLVHSSTVH
PSLSLTLDTK LTSSSIFTRT KTTQREHYDN ARQRAGLISY VDPADVLLFN EKNEITETSI
ANVAFWRDGG WVTPDASTGC LTGVFRRWLL EKGRVREGIV RKDEVKDEEV VLVFNGAAGP
YFVGFAVVLL STGLICFFDV IMPNLPYSLV TTPICILIAL NLFMHYYYVV TIPPGFVEDP
PREAGSSFLW ASPRIKKTHR SLTEGINQCV GLHNERHFVM FMGYLCLAAL TFCILGYEEF
FHALGLFQDE WQYHVPVLAF ILIFILAGVL FFAVGVMFAF HIHSVMKGET SVEHHDNEHY
RKVALSRAET FVNSYNLGRR KNLELFFNVG ENGYPLYTLF FPFRILPYTD GRSWARRPGF
DRHHGVRQGE ELTDDDEEWD
//
