ID A0A2G9HAW4_9LAMI Unreviewed; 643 AA.
AC A0A2G9HAW4;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=CDL12_12690 {ECO:0000313|EMBL:PIN14671.1};
OS Handroanthus impetiginosus.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC asterids; lamiids; Lamiales; Bignoniaceae; Crescentiina; Tabebuia alliance;
OC Handroanthus.
OX NCBI_TaxID=429701 {ECO:0000313|EMBL:PIN14671.1, ECO:0000313|Proteomes:UP000231279};
RN [1] {ECO:0000313|Proteomes:UP000231279}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. UFG-1 {ECO:0000313|Proteomes:UP000231279};
RX PubMed=29253216; DOI=10.1093/gigascience/gix125;
RA Silva-Junior O.B., Grattapaglia D., Novaes E., Collevatti R.G.;
RT "Genome assembly of the Pink Ipe (Handroanthus impetiginosus,
RT Bignoniaceae), a highly valued, ecologically keystone Neotropical timber
RT forest tree.";
RL Gigascience 7:1-16(2018).
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}.
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:PIN14671.1}.
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DR EMBL; NKXS01002238; PIN14671.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G9HAW4; -.
DR STRING; 429701.A0A2G9HAW4; -.
DR OrthoDB; 163401at2759; -.
DR Proteomes; UP000231279; Unassembled WGS sequence.
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:SF316; PROTEIN S-ACYLTRANSFERASE 21; 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:UP000231279};
KW Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:PIN14671.1};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 41..62
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 196..226
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 247..276
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 152..287
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 87..111
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 357..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..643
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 299..320
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 427..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..621
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..643
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 643 AA; 69614 MW; 01C1350170F39B45 CRC64;
MARRHGWQLP AHSFQVVAIT VFFLLSVAFY AFLAPFLGKD IYEYIATGIY SFLALCVFIL
YVRCTGIDPA DPGILIEADK TSAYGSHVES GLPGNLSATE EPTKLGSNNG GKSHRNDSGC
CSKVGCCLCG FLVTEDCRKD EDLAQEQNGE EDALFCTLCN AEVRKFSKHC RSCDKCVDGF
DHHCRWLNNC VGRKNYITFV SLMAASLVWL VFECAVGIAV LVRCFVDRKA TENEIISRLG
DGFSRPPFAT VVALCTAVSF LATVPLGELL FFHIILIRKG ITTYEYVVAM RTQSEPPGPS
IDAGEQQSLP SSPTSSAVTA ISGRSSVGRG LQYKGAWCTP PRIFMDHQDE IVPHLEPGRL
PSTVDPDAVS DKGKRVPQRP VRISAWKLAK LDSNEAIKAG AKARASSSVL RPVSSRSHHH
DADHLSSTTM SGKSSPTSTN QGYYAPAAIS TKSSYPPSRA SRDDTDTCAH SISNMSSPLA
TNLSQSPLGQ ESSSRDHFNP IYQSSTVQSP ISARDEAPLG DNQGRAPVRK NNQVIAENTK
SSSVYWDPEA GRFVSAATRS VGSSSQVSAT ELMYKGQSIF FGGPLVNEQV NRGARAGSSM
SSGQQRSSTS SYYQQGRSQR GGQLPVFVPS DAQQQNQFSS RLE
//
