ID T0K3A9_COLGC Unreviewed; 414 AA.
AC T0K3A9;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=CGLO_10622 {ECO:0000313|EMBL:EQB49987.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB49987.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(2013).
CC -!- FUNCTION: Palmitoyltransferase that targets several endosomal SNAREs.
CC Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic
CC end of their transmembrane domain. May have a role in the cellular
CC quality control of transmembrane domain-containing proteins.
CC {ECO:0000256|ARBA:ARBA00043903}.
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: 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. SWF1
CC subfamily. {ECO:0000256|ARBA:ARBA00038463}.
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:EQB49987.1}.
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DR EMBL; AMYD01002174; EQB49987.1; -; Genomic_DNA.
DR AlphaFoldDB; T0K3A9; -.
DR STRING; 1237896.T0K3A9; -.
DR eggNOG; KOG1312; Eukaryota.
DR HOGENOM; CLU_042181_2_1_1; -.
DR OMA; HIYLIWA; -.
DR OrthoDB; 5480099at2759; -.
DR Proteomes; UP000015530; 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:SF286; PALMITOYLTRANSFERASE ZDHHC4; 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 Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000015530};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 80..100
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 200..223
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 261..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 156..298
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
SQ SEQUENCE 414 AA; 47572 MW; 432B8270085110CC CRC64;
MGLLRNAVLF VLAISFVVFV AFFGRLPALR HTPIATLHRI MRIHIPNGFL AIDRLLTGGR
FSSSMLRFGN FMMNDRHPTV VIFFLVLLSV SEYLFLPTAW PQISTFHKVA GSIAIFLPYL
FLYLSVMTDP GYITHENHAY YMSLYPYDWS IFFPGHECKT CGFLKPPRSK HCSICKRCIA
KLDHHCIFIN GCVGYKNHHY FLLLLATTAL LTSYGGFLGF SLLSKRIATE YPTWALWPPK
GMEIKDYLLI WNWALQDSVG MGAVTLLAAM ISPLVWGLFA YNVWLIYSGT TTNESLKWSD
WKAEMDDGCA FKRKLQPNRV KDRRYEPERT RWPLESQQVL ARTDDGMPPP SNVSTQSEWE
RVWKLADVEN LYDLGFWDNV ADVFIPDYNF NVKRDQPTVE AVGRQRHSAR GAPL
//
