UniProt: A0A059AT43

Database: UniProt
Entry: A0A059AT43_EUCGR

LinkDB:  A0A059AT43_EUCGR 
Original site:  A0A059AT43_EUCGR

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (3)   
   Pfam (2)   
   PROSITE (3)   
   SMART (1)   
All databases (13)   

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ID   A0A059AT43_EUCGR        Unreviewed;       492 AA.
AC   A0A059AT43;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=EUGRSUZ_I02519 {ECO:0000313|EMBL:KCW56856.1};
OS   Eucalyptus grandis (Flooded gum).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Myrtales; Myrtaceae; Myrtoideae; Eucalypteae; Eucalyptus.
OX   NCBI_TaxID=71139 {ECO:0000313|EMBL:KCW56856.1};
RN   [1] {ECO:0000313|EMBL:KCW56856.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW56856.1};
RA   Schmutz J., Hayes R., Myburg A., Tuskan G., Grattapaglia D., Rokhsar D.S.;
RT   "The genome of Eucalyptus grandis.";
RL   Submitted (JUL-2013) 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}.
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DR   EMBL; KK198761; KCW56856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A059AT43; -.
DR   EnsemblPlants; KCW56856; KCW56856; EUGRSUZ_I02519.
DR   Gramene; KCW56856; KCW56856; EUGRSUZ_I02519.
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; 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:SF101; PROTEIN S-ACYLTRANSFERASE 23-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF01529; DHHC; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 4.
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   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        274..297
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        309..330
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        414..434
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        454..479
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   REPEAT          62..94
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          95..127
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          162..194
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          195..227
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          368..435
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
SQ   SEQUENCE   492 AA;  53141 MW;  58B9CC71F2BFC935 CRC64;
     MASSEIEVTE PSVAAAAQDP PGEAAAAAAV VDVFSASAYG DLEQLRRFVE QGGASLSTPD
     ANGYYALQWA ALNNFADVVQ YIIENGGNVN ATDNLKQTAL HWAAVRGSVA VADVLLQNGA
     WVEAADINGY RAVHVAAQYG QTAFLNHIVG RYHADNDAPD NDGRSPLHWA AYKGYADTIR
     LLLFREASQG RQDKEGCTPL HWAALRGNVE ACTVLVHAGT KQELKVKDNA GVTPAQLASN
     KGHWAVANFL SNAERAMSNH WTDKIRSGKF GDSGYAPILL CIIIGCTILF INSVLAAPDL
     PKVTAAVGLW AWTAISLAVG SLIMFFRCWS KDPGYIKTPR ELGNHQDDED PLLSIDVNNS
     SQWTGKWSQL CPTCKIVRPV RSKHCPSCKH CVEQFDHHCP WISNCVGKKN KWDFFVLICM
     ATMTSFLGAA VAVQSKLLAG IWTATAAFPT GKSWIHYVMV QHPGIAVFLL LDGIVLIAVT
     TLTTAQASQV LV
//

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