ID Q107X5_LEIDO Unreviewed; 287 AA. AC Q107X5; DT 22-AUG-2006, integrated into UniProtKB/TrEMBL. DT 22-AUG-2006, sequence version 1. DT 09-DEC-2015, entry version 29. 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; Euglenozoa; Kinetoplastida; Trypanosomatidae; OC 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: Palmitoyl-CoA + [protein]-L-cysteine = CC [protein]-S-palmitoyl-L-cysteine + CoA. CC {ECO:0000256|RuleBase:RU079119}. CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase CC activity. {ECO:0000256|RuleBase:RU079119}. CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. CC {ECO:0000256|RuleBase:RU079119}. CC -!- SIMILARITY: Contains 1 DHHC-type zinc finger. CC {ECO:0000256|RuleBase:RU079119}. CC -!- SIMILARITY: Contains DHHC-type zinc finger. CC {ECO:0000256|SAAS:SAAS00117289}. 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; COG5273; LUCA. DR eggNOG; KOG1311; Eukaryota. 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 GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR001594; Znf_DHHC_palmitoyltrfase. DR Pfam; PF01529; zf-DHHC; 1. DR PROSITE; PS50216; ZF_DHHC; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000256|RuleBase:RU079119}; KW Membrane {ECO:0000256|RuleBase:RU079119}; KW Metal-binding {ECO:0000256|RuleBase:RU079119, KW ECO:0000256|SAAS:SAAS00117307}; KW Transferase {ECO:0000256|RuleBase:RU079119, KW ECO:0000256|SAAS:SAAS00117292}; KW Transmembrane {ECO:0000256|RuleBase:RU079119}; KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}; KW Zinc {ECO:0000256|RuleBase:RU079119, ECO:0000256|SAAS:SAAS00117282}; KW Zinc-finger {ECO:0000256|RuleBase:RU079119, KW ECO:0000256|SAAS:SAAS00117305}. FT TRANSMEM 29 47 Helical. {ECO:0000256|RuleBase:RU079119}. FT TRANSMEM 53 74 Helical. {ECO:0000256|RuleBase:RU079119}. FT TRANSMEM 162 185 Helical. {ECO:0000256|RuleBase:RU079119}. FT TRANSMEM 217 236 Helical. {ECO:0000256|RuleBase:RU079119}. FT DOMAIN 117 167 DHHC-type. {ECO:0000259|PROSITE:PS50216}. FT NON_TER 287 287 {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 //