ID A0A1G4MFS0_LACFM Unreviewed; 365 AA.
AC A0A1G4MFS0;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=LAFE_0F13762G {ECO:0000313|EMBL:SCW02764.1};
OS Lachancea fermentati (Zygosaccharomyces fermentati).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4955 {ECO:0000313|EMBL:SCW02764.1, ECO:0000313|Proteomes:UP000190831};
RN [1] {ECO:0000313|Proteomes:UP000190831}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Devillers H.;
RL Submitted (MAR-2016) 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. PFA5
CC subfamily. {ECO:0000256|ARBA:ARBA00038298}.
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DR EMBL; LT598490; SCW02764.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G4MFS0; -.
DR STRING; 4955.A0A1G4MFS0; -.
DR OMA; YCKWCCK; -.
DR OrthoDB; 1387838at2759; -.
DR Proteomes; UP000190831; Chromosome f.
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:SF396; PALMITOYLTRANSFERASE PFA5; 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|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000190831};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 51..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 172..195
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 125..243
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
SQ SEQUENCE 365 AA; 42762 MW; D7CC59A1C1239F6C CRC64;
MRFNRPKITY FRLNRFCVPV IVFALIIYAT WAYCHKFCYD QVYVALNHKS IAIGLIVAEI
ILALLVFGIW LQLVLIGPGK QPRVPPFRIV QDLGEEISSI DDEKPLSSII PPDVYQCDPQ
GYPIWCSTCQ SLKMERTHHS STLGYCISRF DHYCVWIGTV VGRKNYRLFI QFNLYCDMLF
CLIIISICCY LPRIVHQHKR LPQVNPNILI TLGLDCVGFL MVTPLLLSHI YYMMTNRTSI
EILATKRHAK ATQTWFCYYN AVDGYRYVVE FLPREMQDFW NKHKILINIK EFLGQNAFMW
LIPIGSNIED HDAITTNFDD ILGPYRETIS QRFREIIEHK IEKGEYVKSM RVYGDRCRDT
LDHSV
//
