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Database: UniProt
Entry: A0A066XD91_COLSU
LinkDB: A0A066XD91_COLSU
Original site: A0A066XD91_COLSU 
ID   A0A066XD91_COLSU        Unreviewed;       690 AA.
AC   A0A066XD91;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=CSUB01_04064 {ECO:0000313|EMBL:KDN67143.1};
OS   Colletotrichum sublineola (Sorghum anthracnose fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum graminicola species complex.
OX   NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN67143.1, ECO:0000313|Proteomes:UP000027238};
RN   [1] {ECO:0000313|Proteomes:UP000027238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX   PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA   Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT   "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT   of cultivated sorghum.";
RL   Genome Announc. 2:E0054014-E0054014(2014).
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:KDN67143.1}.
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DR   EMBL; JMSE01000840; KDN67143.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A066XD91; -.
DR   STRING; 1173701.A0A066XD91; -.
DR   eggNOG; KOG1311; Eukaryota.
DR   HOGENOM; CLU_021757_0_0_1; -.
DR   OMA; VPVKYCK; -.
DR   OrthoDB; 5480099at2759; -.
DR   Proteomes; UP000027238; 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:UP000027238};
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        377..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        407..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        522..547
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        567..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          478..603
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          1..342
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        53..79
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        96..156
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        188..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        229..342
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   690 AA;  76059 MW;  E8F37A1C8DD900DE CRC64;
     MTSKDQAGGA NAPTGDDTFA KPRFPGRSDR PGPPSIISSR MTDIASDDEG EAAAQTPSEN
     NPRSRSAMDS VSRPGTAKTG TTGAWEGRRR GPPSRMNYIT SLQDKRRSTG AGSTAGSIAS
     RPPSSTGRSH VPSLTSSAFF HPMSSQKLQA QRGGSRPVTR QPKLDDAEPE PSQSDAAAAA
     VASGGPNARH SVISNPISNP VARIQRQLSE DGEMRPPPSR GTEYTEPGTY DRITANTSPT
     HGHYAAGSMS ESVTPLHRNQ RNSRNSRNLS VNVERGFKER GSQSSAGKSP RSFRSSFLLS
     GRSDQGQNKS NRSLPGGEKL SSTPSTPQLN PTDPSRPAKG DNLNKSKSNL GYVFQYFQGN
     TVFCMGGRFQ NTKHRPVNVA TGMFIVLPAV LFFIFSAPWL WRNISPAIPL TFAYLFYICF
     SSFLHASVSD PGILPRNLHA FPPVEPTEDP LRLGPPTNDW VLIKSAESST AAMEVPVKHC
     RTCNIWRPPR AHHCRLCDNC IETHDHHCVW LNNCVGRRNY RYFFAFVSSA TFLSLYLFGA
     SLGQIIAHQN RSGISFSQSI DDFRVPFAMV IYGLIAFLYP AALMGYHIFL MARGETTREY
     INSHKFIKKE RFRAFTQGSM LKNWIVVLCR PRPPTYYQFK KRYSAGDQRL GAFRDRPKQD
     AQSMEMQSVR PFTGFQGPVS LRNEANTSTT
//
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