ID A0A0V1I5E8_9BILA Unreviewed; 387 AA.
AC A0A0V1I5E8;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
DE Flags: Fragment;
GN Name=ZDHHC16 {ECO:0000313|EMBL:KRZ18093.1};
GN ORFNames=T11_6449 {ECO:0000313|EMBL:KRZ18093.1};
OS Trichinella zimbabwensis.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC Trichinellida; Trichinellidae; Trichinella.
OX NCBI_TaxID=268475 {ECO:0000313|EMBL:KRZ18093.1, ECO:0000313|Proteomes:UP000055024};
RN [1] {ECO:0000313|EMBL:KRZ18093.1, ECO:0000313|Proteomes:UP000055024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ISS1029 {ECO:0000313|EMBL:KRZ18093.1};
RA Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT "Evolution of Trichinella species and genotypes.";
RL Submitted (JAN-2015) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KRZ18093.1}.
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DR EMBL; JYDP01000004; KRZ18093.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V1I5E8; -.
DR STRING; 268475.A0A0V1I5E8; -.
DR Proteomes; UP000055024; 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; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR PANTHER; PTHR12246:SF13; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW Membrane {ECO:0000256|RuleBase:RU079119};
KW Reference proteome {ECO:0000313|Proteomes:UP000055024};
KW Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:KRZ18093.1};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 67..88
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 174..193
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 253..274
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 131..290
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KRZ18093.1"
SQ SEQUENCE 387 AA; 46179 MW; 03AEA2B52DDD3378 CRC64;
LSSFRGYYSF IMHLSWIRIT KEKYNKARMI FLWLFYNAQC DYDYAIDTLF EPMYNFVDNY
IQQFGKIFVG FLSFMIFLMV TIAYLIVVPY EWPKRNFFQI CVYFVIGKWL LINLIFNFYM
GCRTEPVAVG VCKHCIQPKP PRTHHCSVCN RCILKMDHHC PWLNQCVGHY NHRYFYLTLI
FMWLSCIYVV YGMRDCFVDH YRIEGTIVPW CMAMENKLCY AKWLCHYATN ISTKCEMEQE
TCRELVSGKM VQYLILVEFF VALAIVVGLL WLIYSHGKII SNGETSIEYY VNLATAKKFA
TRQKVYMNPY DFGWRKNWKS FLGIDDFRED FFRKIIIPSI YQPYGDGLSW PFAFSLDELL
PHVQGQTSRS CQWLKKCPNN LLLLKIN
//