ID A0A317XDQ6_9EURO Unreviewed; 456 AA.
AC A0A317XDQ6;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=BO94DRAFT_12377 {ECO:0000313|EMBL:PWY96465.1};
OS Aspergillus sclerotioniger CBS 115572.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=1450535 {ECO:0000313|EMBL:PWY96465.1, ECO:0000313|Proteomes:UP000246702};
RN [1] {ECO:0000313|EMBL:PWY96465.1, ECO:0000313|Proteomes:UP000246702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115572 {ECO:0000313|EMBL:PWY96465.1,
RC ECO:0000313|Proteomes:UP000246702};
RG DOE Joint Genome Institute;
RA Vesth T.C., Nybo J., Theobald S., Brandl J., Frisvad J.C., Nielsen K.F.,
RA Lyhne E.K., Kogle M.E., Kuo A., Riley R., Clum A., Nolan M., Lipzen A.,
RA Salamov A., Henrissat B., Wiebenga A., De Vries R.P., Grigoriev I.V.,
RA Mortensen U.H., Andersen M.R., Baker S.E.;
RT "The genomes of Aspergillus section Nigri reveals drivers in fungal
RT speciation.";
RL Submitted (DEC-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}.
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:PWY96465.1}.
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DR EMBL; MSFK01000001; PWY96465.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317XDQ6; -.
DR STRING; 1450535.A0A317XDQ6; -.
DR OrthoDB; 1387838at2759; -.
DR Proteomes; UP000246702; 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:SF405; PALMITOYLTRANSFERASE; 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:UP000246702};
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 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 53..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 211..234
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 165..303
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 90..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 422..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..439
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 440..456
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 456 AA; 51699 MW; 4E15968CBA2AAFE4 CRC64;
MARPDKRINV AVARAIPPFL LCVSVYASYI VTKPLCIDYL IRPLPKYHRS SRVGAGAAIL
AIFYILIIVV ITTYLRLLYN VVRNPGYLPR APPPIKGQDT EPSDPQHRKK KRHRNGRTPE
KPDKSEVDIE RGVDCNADGG PIPLDTTALE NFYTKDVFVC QEDGRPLYCS TCCHYKTDRA
HHCREVDRCV LKMDHFCPWV GGVVSETSFK FFIQFVFYTM LFCTFSLIVC ATFTAEMKRQ
TGGANVHLAI GIGLCVFRSH KSFWLFCLTI NRSSLFGLFT FGMTLSSLQL AMLNMSTIEN
LNRRSAVWTL AIRVPNKMLA KLNPESRWAP TFRTITYPLP PASLDPEAAR EYQPAGEKHV
FAILQTLPGE NPFDLGSPFR NLQQVLGYSI IDWLLPFKQS PCADRTTGGS FYELGPVVSR
LKKEAGLEPP REPQSTQTDT HKRHKRRHST HRQSQE
//
