ID A0A2T4C5A2_TRILO Unreviewed; 687 AA.
AC A0A2T4C5A2;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 08-NOV-2023, entry version 21.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=M440DRAFT_1331653 {ECO:0000313|EMBL:PTB76741.1};
OS Trichoderma longibrachiatum ATCC 18648.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=983965 {ECO:0000313|EMBL:PTB76741.1, ECO:0000313|Proteomes:UP000240760};
RN [1] {ECO:0000313|EMBL:PTB76741.1, ECO:0000313|Proteomes:UP000240760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18648 {ECO:0000313|EMBL:PTB76741.1,
RC ECO:0000313|Proteomes:UP000240760};
RG DOE Joint Genome Institute;
RA Aerts A., Atanasova L., Chenthamara K., Zhang J., Grujic M., Henrissat B.,
RA Kuo A., Salamov A., Lipzen A., Labutti K., Barry K., Miao Y., Rahimi M.J.,
RA Shen Q., Grigoriev I.V., Kubicek C.P., Druzhinina I.S.;
RT "Multiple horizontal gene transfer events from other fungi enriched the
RT ability of initially mycotrophic Trichoderma (Ascomycota) to feed on dead
RT plant biomass.";
RL Submitted (JUL-2016) 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|ARBA:ARBA00001870,
CC 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; KZ679131; PTB76741.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4C5A2; -.
DR STRING; 983965.A0A2T4C5A2; -.
DR Proteomes; UP000240760; 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:SF43; PALMITOYLTRANSFERASE APP; 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};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000240760};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 372..390
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 402..423
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 517..542
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 562..587
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 473..598
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 1..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..171
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 643..687
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..66
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..237
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 248..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..659
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 687 AA; 75770 MW; 9403700DC9B65E4A CRC64;
MASPIPDSPV SPRSGSNNQA YPPRTTASTP NDRRPDSVVS SHMTDIASED EADGNASTSA
PRTHHTRESG SAIRPETAKT GASSKAWGGA RKSLGVGKRG SGTSTTSSAL GLSSSSVTSR
SHVPSLTSNA FFHPMSSQKL QAQRAVAARP PATAQPPAAP QPQFGDLPDN ATDFDGSVIH
DFAPSPVAHH APPVQFQHVM YSEDQRQLPS RGTDFTEHDT FDQATETTTS PTGHYAGGSL
SESVRPLRKV SGPEKTPPHL DLSRGSHLRD LRSFPSPMLK TPRSFRSTFL PGASDQGQAQ
SSENRNAAGV EKLASTAASS PRLNPVDSQV RPKTESTAVK RKTRRRRNYE YFEGNTMFLF
GGRWQNTRQR PINVATGLFV VLPCVLFFVF EAPFLWHHIS PAVPIIFAYL AYICFSSFLH
ASISDPGILP RNLHQFPPLA PHEDPLRVDP PTNDWTLIKS AEPTAAAMEF PVKHCRTCNI
WRPPRAHHCR LCDNCIETHD HHCVWLNNCV GKRNYRYFFT FVSSATVLSL YLIGVSLAQL
IVYANQHNIS FGKSVNHFRV SLALVILGIF CFLYPAALMG YHIFLMARGE TTREFMNSHK
FTKSERYRPF DQASIWRNIL AVLCRPRTPS YYQFKKSYEN GDQRLGLHRH QRPAPDSRGH
EMSAVKPSSQ GGFQGPVALR GSSHGEA
//