ID A0A2G2Z0S8_CAPAN Unreviewed; 583 AA.
AC A0A2G2Z0S8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=S-acyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
DE AltName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
GN ORFNames=T459_18997 {ECO:0000313|EMBL:PHT75475.1};
OS Capsicum annuum (Capsicum pepper).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Solanales; Solanaceae; Solanoideae; Capsiceae; Capsicum.
OX NCBI_TaxID=4072 {ECO:0000313|EMBL:PHT75475.1, ECO:0000313|Proteomes:UP000222542};
RN [1] {ECO:0000313|EMBL:PHT75475.1, ECO:0000313|Proteomes:UP000222542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CM334 {ECO:0000313|Proteomes:UP000222542};
RX PubMed=29089032; DOI=10.1186/s13059-017-1341-9;
RA Kim S., Park J., Yeom S.I., Kim Y.M., Seo E., Kim K.T., Kim M.S., Lee J.M.,
RA Cheong K., Shin H.S., Kim S.B., Han K., Lee J., Park M., Lee H.A.,
RA Lee H.Y., Lee Y., Oh S., Lee J.H., Choi E., Choi E., Lee S.E., Jeon J.,
RA Kim H., Choi G., Song H., Lee J., Lee S.C., Kwon J.K., Lee H.Y., Koo N.,
RA Hong Y., Kim R.W., Kang W.H., Huh J.H., Kang B.C., Yang T.J., Lee Y.H.,
RA Bennetzen J.L., Choi D.;
RT "New reference genome sequences of hot pepper reveal the massive evolution
RT of plant disease-resistance genes by retroduplication.";
RL Genome Biol. 18:R210.1-R210.11(2017).
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:PHT75475.1}.
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DR EMBL; AYRZ02000007; PHT75475.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G2Z0S8; -.
DR STRING; 4072.A0A2G2Z0S8; -.
DR EnsemblPlants; PHT75475; PHT75475; T459_18997.
DR Gramene; PHT75475; PHT75475; T459_18997.
DR OMA; DTYYRAI; -.
DR Proteomes; UP000222542; Chromosome 7.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016409; F:palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
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; PF12796; Ank_2; 3.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 6.
DR SUPFAM; SSF48403; Ankyrin repeat; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 3.
DR PROSITE; PS50088; ANK_REPEAT; 4.
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:UP000222542};
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 234..256
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 268..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 373..397
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 417..439
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 21..53
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 54..86
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 121..153
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 154..178
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 328..455
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 514..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 514..561
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 583 AA; 63878 MW; 477B04181CFFF371 CRC64;
MEKLQRLVES EGCSVSEPDG LGYYALQWAA LNNRTAAAQY IIEHGGDVNA ADHTGQTALH
WSAVRGAVQV AELLLQEGAR VNAADMYGYQ PTHVAAQYGQ TAFLYYVVTK WNADPDVPDS
DGRSPLHWAA YKGFADCIRL LLFLDAYRGR QDKEGCTPLH WSAIRGHLEA CTVLVQAGKK
EDLIVTDNTG LTPAQLASDK NHRQVAFFLG NARRLYDKRC DGTTQLGKLS KLGLAPILCC
TIFILLTTYI HAVIMASTLP KLTAAGALFA WSGVLLASAG LVTFYRCSRK DPGFIRRSPR
DSQNSKDDEP LLKMEMNHPA LLAGNWSQLC STCKIVRPLR AKHCSTCDRC VEQFDHHCPW
VSNCIGKKNK WDFFIFLVLE VLAMVLTGAV TLTRVLTDPA APSSFGAWLS HAGTHHIGAL
AFLFTDFFLL IGVAVLTGVQ ASQISHNITT NEMANMMRYS YLRGPGGRFR NPYDHGCKKN
CSDFLINGYN EDIERAEESV QSEGIGMMQI PHSSSMQNGA GHSHQINGNG HHVINISNSN
QNSHQSHVHS ANCSHNVKSK TDSVPVGLGV GLGRNSTRNV LPS
//
