ID W2KEY6_PHYPR Unreviewed; 487 AA.
AC W2KEY6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=L917_16439 {ECO:0000313|EMBL:ETL83627.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL83627.1};
RN [1] {ECO:0000313|EMBL:ETL83627.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL83627.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CHvinca01.";
RL Submitted (NOV-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|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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI681989; ETL83627.1; -; Genomic_DNA.
DR AlphaFoldDB; W2KEY6; -.
DR EnsemblProtists; ETL83627; ETL83627; L917_16439.
DR VEuPathDB; FungiDB:PPTG_16778; -.
DR Proteomes; UP000054423; 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 Transferase {ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 41..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 156..180
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 224..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 109..262
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 287..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 335..487
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 378..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..435
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 472..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 54262 MW; E67B746B4C172710 CRC64;
MRKNGWETPF HVLQLATWVV FPAVMALFFA FYTPILDKTP AIVLSVVYAA ACLVTVVSVA
VCTGTDPSDD CIMRPSVRAT QSRFSSDFRL TVMLFWPQTL PDARDSRPDN RVYCNVCTKY
VNDQSRHCRL CDKCVDVFDH HCKWLNNCVG KKNYRFFLGS VVGASVFLAV QIAVGIYLVV
ELYTNEDDTM GNSATSYGCS TEKDDLTGLC VDGQYSISLQ TLRIIHIVLL AFLSPWLFMI
GQLALFHFHL CMENITTYDY IVRQRKRKNA QERQNIVRVP WWKRCCGQKP NPDSAPNNSK
PSVNQTSDSR PSGESVRSEE EELAAIEAEV DDSLEVLSNQ SGEIRERDSS RRSSSSYRKR
RSNSGTKRGF GLHVDLAGQR SVQTNTGANG VVYTPRSESG DTSYLAAPYS PGTPASPLSP
RSDAGSAYFS NSQVDEIETR DGEATNQPLP AYKVSSNSSM VMYGRPPIDD TSSENHIVDF
DSGDKKH
//