ID A0A059CXY6_EUCGR Unreviewed; 674 AA.
AC A0A059CXY6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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_C043982 {ECO:0000313|EMBL:KCW83016.1};
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:KCW83016.1};
RN [1] {ECO:0000313|EMBL:KCW83016.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Leaf extractions {ECO:0000313|EMBL:KCW83016.1};
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; KK198755; KCW83016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A059CXY6; -.
DR EnsemblPlants; KCW83016; KCW83016; EUGRSUZ_C043982.
DR Gramene; KCW83016; KCW83016; EUGRSUZ_C043982.
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:SF17; PALMITOYLTRANSFERASE HIP14; 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; 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 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 346..364
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 376..399
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 487..510
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 530..553
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 135..167
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 168..200
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 235..267
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 268..300
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 442..569
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 654..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 674 AA; 73482 MW; 104813A7C6E8383C CRC64;
MSQITREIPS LTNHNLARSR KKAKSTLDQT VLPTHPSLPS LSSFSLSSLL LDRIRPPFPA
AMSSEIEVVD EARPADRDAA VAGGAVAAGA AAAAAAAPEE SLRDDVYTAA AYGDMEKLRR
LVESEGCSVS EPDGLGYCAL QWAALNNRTA AAQYIIEHGG DVHAADHTGQ TALHWSAVRG
AIQVAELLLR EGARVNAADS YGYQTTHVAA QYGQTSFLYH IVSKWNADPD VPDKDGRSPL
HWAAYKGFAD CIRLLLFLDA YRGRQDKEGC TPLHWAAIRG NLEACTVLVQ AGKKEDLMVT
DNTGLTPAQL ASEKSHRQVA FFLGNARSLL DKRCDGNSRL GKLSKLGLAP VLWFLIIVLL
LIYINSVIRA PTLPKLTAGF GLLAWSGVFL ASAGLVLFYR CSRKDPGYIR MNVHDPQNMK
DDEPLLKIEI NNPALLAGNW SQLCATCKIV RPLRAKHCST CDRCVEQFDH HCPWVSNCIG
KKNKWDFFVF LVLEVTAMLI TGAVALIRVS KDPLAPSSFG SWLSHVGTQH IGALSFFLAD
FSLFFGVAVL TAVQASQISH NITTNEMANA MRYSYLKGPG GRFRNPYDHG FKKNCSDFLI
NGYNEDVEYV EDSSHAEGIG MMHMGRTSNL QNGDVHSHQP AENGHIAINV GSTSSNSHHG
HVHSSHCSHN HVVL
//
