ID Q107X5_LEIDO Unreviewed; 287 AA. AC Q107X5; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 17-JUN-2020, entry version 42. DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119}; DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119}; DE Flags: Fragment; GN Name=ZFD {ECO:0000313|EMBL:AAY96326.1}; OS Leishmania donovani. OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina; OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania. OX NCBI_TaxID=5661 {ECO:0000313|EMBL:AAY96326.1}; RN [1] {ECO:0000313|EMBL:AAY96326.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Dd8 {ECO:0000313|EMBL:AAY96326.1}; RA Ray S., Naik S.; RT "LdZFD: a Leishmania donovani DHHC containing zinc finger protein."; RL Submitted (MAY-2005) 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 -!- 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; DQ086112; AAY96326.1; -; Genomic_DNA. DR eggNOG; KOG1311; Eukaryota. DR eggNOG; COG5273; LUCA. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC. DR InterPro; IPR001594; Palmitoyltrfase_DHHC. DR Pfam; PF01529; DHHC; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|RuleBase:RU079119}; KW 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 29..47 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU079119" FT TRANSMEM 53..74 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU079119" FT TRANSMEM 162..185 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU079119" FT TRANSMEM 217..236 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU079119" FT DOMAIN 116..252 FT /note="DHHC" FT /evidence="ECO:0000259|Pfam:PF01529" FT NON_TER 287 FT /evidence="ECO:0000313|EMBL:AAY96326.1" SQ SEQUENCE 287 AA; 32253 MW; 58F56D46F1A9088D CRC64; MPLTAPPRRN GNIKVFLNGR IFVGPDWRIM TLSVVLISVC SLVFVFFTNE IMAARVIVGV TALISVAALL LCGLSDPGVK PRQPPPPPDA PPHESLWRER EYVDQNGYVH QARLEMKWWY SCNIYRPYRG VHCRYCDQCV ARRDHHCPWT GTCIGAKNYR SYFALVWVLS VMLFTALCGG IQSFVQRIVR HSKATPVIED GPSAFTSALI DTYGLELILI VLSFIFGLLV WSLAVYHTYL ISRNLTSGDA AKDLEENVFT HGSVLANVWA ALTGWREEEM TCGDART //