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Database: UniProt
Entry: A0A1S2Z3A3_CICAR
LinkDB: A0A1S2Z3A3_CICAR
Original site: A0A1S2Z3A3_CICAR 
ID   A0A1S2Z3A3_CICAR        Unreviewed;       625 AA.
AC   A0A1S2Z3A3;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-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   Name=LOC101496942 {ECO:0000313|RefSeq:XP_004514247.1};
OS   Cicer arietinum (Chickpea) (Garbanzo).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; Hologalegina; IRL clade; Cicereae; Cicer.
OX   NCBI_TaxID=3827 {ECO:0000313|Proteomes:UP000087171, ECO:0000313|RefSeq:XP_004514247.1};
RN   [1] {ECO:0000313|RefSeq:XP_004514247.1}
RP   IDENTIFICATION.
RC   TISSUE=Etiolated seedlings {ECO:0000313|RefSeq:XP_004514247.1};
RG   RefSeq;
RL   Submitted (SEP-2023) 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|ARBA:ARBA00008574, ECO:0000256|RuleBase:RU079119}.
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DR   RefSeq; XP_004514247.1; XM_004514190.3.
DR   AlphaFoldDB; A0A1S2Z3A3; -.
DR   PaxDb; 3827-XP_004514247-1; -.
DR   GeneID; 101496942; -.
DR   KEGG; cam:101496942; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   OrthoDB; 163401at2759; -.
DR   Proteomes; UP000087171; Unplaced.
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; PTHR22883:SF285; S-ACYLTRANSFERASE; 1.
DR   PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW   ECO:0000256|RuleBase:RU079119}; Membrane {ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000087171};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        43..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        224..247
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        268..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          179..312
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          91..110
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          379..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          442..470
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          561..625
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..110
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..462
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        601..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   625 AA;  68827 MW;  44FA735A25DBD6C8 CRC64;
     MRKHGWQLPY HPLQVVAISV FLALGFAFYV FFAPFVGNKM YQYIVIALYT PLITVVFGLY
     IWCAAADPSD PGVFKSKKYL KIPDNKKVVG HKSSKLGEES TPSMHDANDS TVGGNSMDNE
     TFGTEGNMKN ASNSVEKANA SSSCLSCFLL VCSPCAYICR CSGSSEESSD KQTSEDGMFY
     CSLCEVEVFK YSKHCRVCDK CVNHFDHHCR WLNNCIGKKN YRQFFTLMIA AMLLFILQWS
     TGILVLIRCF VERKQFSMEI SSKLGSSFSL APFVIVVSAC TILAMIATLP VVQLFFFHIL
     LIKKGLSTYD YIVALRELEQ EQEQLGNGGQ QSPQMSTVSS FTGLSSASSF NALHRGAGAW
     CTPPRMFIED QFDVVPPETS SVSSLGKKSM REEPLKKKNP GAVKISPWTL ARLNAEDVAK
     AAAEAKKKSK ILLPVIRHDQ SSRLEPDSSF GSSGQRMVPA NENNKKQDNK RIYLPADLSM
     ESMMKVSANN TDRGFNGRSG FAPLQYEARS AFKTSQAMPS SAGIVLSSPE SSLDSPDIHP
     FRASGAEEAR HLAGLSAADA AALKENPLSR STSDGYEASG GEDSDQVPSR IVQRSADRSN
     FLFRADQDER SFRPTLSSSK SHSRH
//
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