ID A0A0M9WFU8_9EURO Unreviewed; 732 AA.
AC A0A0M9WFU8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=ACN38_g5831 {ECO:0000313|EMBL:KOS43262.1};
OS Penicillium nordicum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=229535 {ECO:0000313|EMBL:KOS43262.1, ECO:0000313|Proteomes:UP000037696};
RN [1] {ECO:0000313|EMBL:KOS43262.1, ECO:0000313|Proteomes:UP000037696}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DAOMC 185683 {ECO:0000313|EMBL:KOS43262.1,
RC ECO:0000313|Proteomes:UP000037696};
RA Nguyen H.D., Seifert K.A.;
RT "Genome sequencing of Penicillium nordicum.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Palmitoyltransferase specific for casein kinase 1.
CC {ECO:0000256|ARBA:ARBA00002100}.
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: Early endosome membrane
CC {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004520}. Endosome membrane
CC {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004337}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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 AKR/ZDHHC17 subfamily. {ECO:0000256|ARBA:ARBA00010104}.
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:KOS43262.1}.
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DR EMBL; LHQQ01000085; KOS43262.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M9WFU8; -.
DR STRING; 229535.A0A0M9WFU8; -.
DR OrthoDB; 33889at2759; -.
DR Proteomes; UP000037696; Unassembled WGS sequence.
DR GO; GO:0031901; C:early endosome 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; 1.
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; PF00023; Ank; 2.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF01529; DHHC; 1.
DR SMART; SM00248; ANK; 5.
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|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU079119};
KW ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW ProRule:PRU00023}; Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW Membrane {ECO:0000256|RuleBase:RU079119};
KW Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW Reference proteome {ECO:0000313|Proteomes:UP000037696};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
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 299..317
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 323..341
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 361..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 391..410
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 489..511
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 540..562
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT REPEAT 85..117
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 152..184
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 185..217
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT REPEAT 218..250
FT /note="ANK"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT DOMAIN 440..575
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..732
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 732 AA; 81468 MW; 999B7910CF128153 CRC64;
MSTKTSPESW DPSPGPTSGS TSASNGNGTP TPPNDVEMKS LRPDPPKGSI PLGEDIMQLA
RMGEIGTMQK LFTAKKFTAN HRDEEGITPL HWAAINNQYA MCRFLIDSGA DVNAKGGESV
ATPAMWAAQR CHYYIVNLLL QNGGDPLLTD VQGYNILHLA TIDGNAFLVV LLLHQEIPVD
VVDQQGHTGL MWAAYKGYPA CVDLFLRWGA NANAVDEGGL TPLHWALVKG SMPCVLKLLE
YGTDRFAKTR DGKSPATVAQ EMNTLRVWYR SLNERGFEPD GTQKVVPLGL ASFVRNKSIM
AKFFFLWPFL MILVTIWMLS NLAIFVAVPL VLVTLFGMQY VAQQFANKGP MEYRVLQKTP
YLAGVFAGTL FWVGFRYAFK VLPATYSSSP ILNILFAVFF CLTAYFYIFS MVQDPGYVPK
VSSRNQQREI VRELFEQWKF DEENFCIPCM TRKPLRSRHC RRCGRCVAKH DHHCPWIDNC
VGANNLRHFV LYIVSLEVGI ILFVQLTIAY INSLPAPTNA TCNVINDTLC DYASRDPFTL
ILNVWITLQL VWVTMLCAVQ LVQISRNQTT YENMRGHHFD RSYPSSQAFA SAMTAGTTSM
EAAGLSASGQ GPNPALGGPL PHRRKNGCIQ QWSSLLGIDA FWTTAKDGLR DGPQAARPRN
PFSRGVVTNC RDFWCDPAPL FGKRQTGAAM LGGEVINYHD MYETPMRMHT GNRSNEGPGY
RSVAGEDPER MV
//
