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Database: UniProt
Entry: A0A3M9YDQ6_9PEZI
LinkDB: A0A3M9YDQ6_9PEZI
Original site: A0A3M9YDQ6_9PEZI 
ID   A0A3M9YDQ6_9PEZI        Unreviewed;       673 AA.
AC   A0A3M9YDQ6;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   Name=ERF2 {ECO:0000313|EMBL:RNJ58693.1};
GN   ORFNames=D7B24_004328 {ECO:0000313|EMBL:RNJ58693.1};
OS   Verticillium nonalfalfae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=1051616 {ECO:0000313|EMBL:RNJ58693.1, ECO:0000313|Proteomes:UP000267145};
RN   [1] {ECO:0000313|EMBL:RNJ58693.1, ECO:0000313|Proteomes:UP000267145}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VnAa140 {ECO:0000313|EMBL:RNJ58693.1,
RC   ECO:0000313|Proteomes:UP000267145};
RA   Stajich J.E., Kasson M.T.;
RT   "Genome sequence of Verticillium nonalfalfae VnAa140.";
RL   Submitted (OCT-2018) 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: Endoplasmic reticulum membrane
CC       {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004477}. 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       {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:RNJ58693.1}.
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DR   EMBL; RBVV01000024; RNJ58693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M9YDQ6; -.
DR   STRING; 1051616.A0A3M9YDQ6; -.
DR   OrthoDB; 5480099at2759; -.
DR   Proteomes; UP000267145; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        358..382
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        388..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        503..528
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        548..570
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          459..584
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          1..323
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          644..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        60..78
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        103..196
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        205..228
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  74313 MW;  90E7ABEFC8AF83CD CRC64;
     MASRDHTGRA TSPSAHDDFP TPQFPGRSEG QGPPSIISSR MTDIASDDGG EAETQHHPAG
     VQRKGTTDTA SRPGTAKTGL SGSRDGWRHP QPLRKSHVSG LAAKRGSTGS GSVASNRPPS
     STSRSHVPSL TSHAFFHPLS SQKLQAQRGG PSRPQTVNQQ QPTLDENAQE SGDGTRQSII
     SNPMVRIQNQ TSDDGELRAP PSRGTEFTEQ ETLDRITANT SPTHGHYPAG SLTDSVRPLQ
     RKPFEPRNLN INVDKSYKER GNLPSPIKSP RSFRSSFLMP GRSQERVNTP NRVPPPGAEK
     LSSAASSPRL NGEGSGRPAE VSELPIPAAK PGFVFEHFEG NMVFCFGGRF QNSRQRPINI
     ATGLMVVIPG VLFFAFSAPW LWNNISPAIP ITFAYVFYIC LSSFFHASVS DPGILPRNQH
     VFPPSQADND PLRQQPPTND WTLIKSAESA TAAMEVPVKH CRTCNIWRPP RAHHCRLCDN
     CIETHDHHCV WLNNCVGRRN YRYFFTFVTS ATFIAAYLLG ASLAQILVYM SREDVSFGSA
     IDKFRVPFAM VIYGGLAFCY PAALMGYHIF LMARGETTRE YINSHKFIKQ ERFRAFTQGS
     MLKNWFVVLC RPRPPTYYSF KARYQPGDQR LGDLRDRKSI KDRDAQGMEL RDVPPATGFQ
     GPAALRQEAN AAA
//
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