ID A0A093H7J2_STRCA Unreviewed; 607 AA.
AC A0A093H7J2;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, 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 ORFNames=N308_02086 {ECO:0000313|EMBL:KFV78578.1};
OS Struthio camelus australis.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Struthioniformes; Struthionidae;
OC Struthio.
OX NCBI_TaxID=441894 {ECO:0000313|EMBL:KFV78578.1, ECO:0000313|Proteomes:UP000053584};
RN [1] {ECO:0000313|EMBL:KFV78578.1, ECO:0000313|Proteomes:UP000053584}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N308 {ECO:0000313|EMBL:KFV78578.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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: Cytoplasmic vesicle membrane
CC {ECO:0000256|ARBA:ARBA00004439}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004439}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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 EMBL; KL206071; KFV78578.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A093H7J2; -.
DR STRING; 441894.ENSSCUP00000012485; -.
DR Proteomes; UP000053584; Unassembled WGS sequence.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi 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:SF18; PALMITOYLTRANSFERASE ZDHHC17; 1.
DR Pfam; PF12796; Ank_2; 2.
DR Pfam; PF01529; DHHC; 1.
DR PRINTS; PR01415; ANKYRIN.
DR SMART; SM00248; ANK; 5.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 4.
DR PROSITE; PS50088; ANK_REPEAT; 5.
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 Reference proteome {ECO:0000313|Proteomes:UP000053584};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:KFV78578.1};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 274..290
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 296..314
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 326..348
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 360..378
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 460..481
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 514..536
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 58..90
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 92..124
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 125..157
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 158..191
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 193..225
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 413..544
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFV78578.1"
FT NON_TER 607
FT /evidence="ECO:0000313|EMBL:KFV78578.1"
SQ SEQUENCE 607 AA; 69964 MW; 484661D992220A33 CRC64;
ELKPQSHYNH GYSESLGRKS HIDDYSTWDI VKATQYGIYE RCRELVEAGY DVRQPDKENV
TLLHWAAINN RIDLVKYYIS KGAIVDQLGG DLNSTPLHWA TRQGHLSMVV QLMKYGADPS
LIDGEGCSCI HLAAQFGHTS IVAYLIAKGQ DVDMMDQNGM TPLMWAAYRT HSVDPTRLLL
TFNVSVNLGD KYHKNTALHW AVLAGNTTVI SLLLEAGANV DAQNIKGESP LDLAKQRKNV
WMINHLQEAR QAKGYDSPSF LRKLKADKEF RQKVMLGTPF LVIWLIGFIA DLDIDSWLIK
GLMYGGVWAM VQFLSKSFFD HSMHSALPLG IYLATKFWMY VTWFFWFWND ILFLSHLNFF
FIHLPFLANS VALFYNFGKS WKSDPGIIKA TEEQKKKTIV ELAETGSLDL SIFCSTCLIR
KPVRSKHCGV CNRCIAKFDH HCPWVGNCVG AGNHRYFMGY LFFLLFMICW MIYGCISYWG
FHCETSYAKD GFWTYITQIA TCSPWMFWMF LNSVFHFMWV AVLLMCQMYQ ISCLGITTNE
RMNARRYKHF KVTTTSIESP FNHGCIRNII DFFEFRCCGL FRPVIVDWTR QYTIEYDQTS
GSGYQLV
//
