ID A0A0R3R2Z0_9BILA Unreviewed; 447 AA.
AC A0A0R3R2Z0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
OS Brugia timori.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001438001-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:BTMF_0001438001-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (FEB-2017) to UniProtKB.
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}.
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DR STRING; 42155.A0A0R3R2Z0; -.
DR WBParaSite; BTMF_0001438001-mRNA-1; BTMF_0001438001-mRNA-1; BTMF_0001438001.
DR Proteomes; UP000050602; Unplaced.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR PANTHER; PTHR24161; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR24161:SF17; PALMITOYLTRANSFERASE HIP14; 1.
DR Pfam; PF00023; Ank; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 3.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 2.
DR PROSITE; PS50088; ANK_REPEAT; 2.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Membrane {ECO:0000256|RuleBase:RU079119};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 155..173
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 182..205
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 211..233
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 323..345
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 365..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 13..45
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 81..113
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 297..400
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
SQ SEQUENCE 447 AA; 50908 MW; 22CCBC777636209B CRC64;
LVPQIKALQL DVAGFTPLHV AVQFGRTSTA AYLIAAGQSP DERDETMMTP AMWAAYKVFS
RDPLQMLITM GADLSCTDTT YANTALHWAV IQGNHSAINV LIKYNAELVL RNRDNETPRD
IAIRRGDILI SRIMFFLPVC IMVAVGLILH VILSYMVKAL LLLLVGVFGR IVYRSLATDR
SFYIIPLGAA VASKIVLAVT WLLYLHAFAG WYWQISFFIL VTLAPVLFLW IIFSDPGXXX
XXXXXXXXKE SRQAVSFCST CLLKRPARSK HCSVCDRCVK RLFLFNYGPY GDQVKFCFNE
TRLFDHHCPW VLNCIGEKNH LHFVFYLGIV IASSLQFLVA TFHYWRDSCG EISQANITYC
NPWVTYVFVI ALYHFIWTSA MLTFQIYQIL CEMTTNERLN AYRYEHFHST GDHLRIKSPF
SKGMLQNLYN FCCGGAIASC EEENQLD
//
