ID B8NTQ0_ASPFN Unreviewed; 736 AA.
AC B8NTQ0;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 24-JAN-2024, entry version 69.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=AFLA_099810 {ECO:0000313|EMBL:EED46317.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED46317.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED46317.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
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; EQ963484; EED46317.1; -; Genomic_DNA.
DR RefSeq; XP_002383853.1; XM_002383812.1.
DR AlphaFoldDB; B8NTQ0; -.
DR STRING; 332952.B8NTQ0; -.
DR EnsemblFungi; EED46317; EED46317; AFLA_099810.
DR VEuPathDB; FungiDB:AFLA_010221; -.
DR VEuPathDB; FungiDB:AFLA_010224; -.
DR eggNOG; KOG1315; Eukaryota.
DR HOGENOM; CLU_376815_0_0_1; -.
DR Proteomes; UP000001875; 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; PTHR42081; -; 1.
DR PANTHER; PTHR42081:SF1; -; 1.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
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 52..75
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 174..237
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 97..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 278..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 342..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 684..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 364..421
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..466
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 610..624
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..703
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 736 AA; 84603 MW; 276FE94EC75FD70C CRC64;
MARPDRRVSL AVARIIPLVL LCTVIYASYA ITKPLCIDYL ITPLPKYNRS SRVGAGIAII
VVYYVLLTPM VITYLRLLYN VICNPGFIPR GSSYLPDQQD AEAPNAHRRN RKRRRKSHRK
PGTAEKSDTS DEVDLERGVD HHAGGKAFPL NAEGLENFYT KDVFICQPDG RPIYCSTCCQ
YKTDRAHHCR EVDRCVRKMD HFCPWVGGVV SETSFKFFIQ FVFYTFVFCT FTLIVYGRGQ
SSLGCWYRIF WVTLYLTGCF PSSKAHVVIM SPIVHSGYRE HDPSRRSRYP PTGGLRKGED
IDDYDAYSYT NPREQFEKDS AARLRHDRGS YWRERPLSLT GIDDPQLVSR SGPRSPKPPP
STRGFDRLEW DPRVRRPMQG SADSDVDVAR AHRRAGRRNP VHLHQEADEG YSSYRSDYED
AHRRRHRHRR HDNNRSGRHP YDDGASRGSI TNEPASQGTT TGLGTAVLGG VHNDYESQRA
ERHRSHEHDT RERHSRLQRS SRRQVDSDSD AYTSDEDLRK HRREASARPK ASRSDDSASG
SERPRRRRSH SRPRPQDSST TKEMIQIDRQ EDKRTESTVS KDSETPPKGI LKTPTDKFPE
EPNPVREGVA PLKDAHKKGI PPGARWTKID RRLVNPAALE AGRERFEERS DYVIVLRVLS
KEEIQAYAVR TQEIRDARYR EYVQERRRRR EEDKRRGRAV DDFSSDDEED DDDSPGGVED
KPAEQHKMAE PVKSAG
//
