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Database: UniProt
Entry: H1V396_COLHI
LinkDB: H1V396_COLHI
Original site: H1V396_COLHI 
ID   H1V396_COLHI            Unreviewed;       411 AA.
AC   H1V396;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=CH063_06635 {ECO:0000313|EMBL:CCF34698.1}, CH63R_14118
GN   {ECO:0000313|EMBL:OBR02892.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF34698.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|EMBL:CCF34698.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:CCF34698.1};
RA   Ma L.-J., O'Connell R., van Themaat E.V.L., Stueber K., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Gearin G., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Heiman D., Howarth C., Larimer J., Lui A.,
RA   MacDonald P.J.P., McCowen C., Montmayeur A., Murphy C., Neiman D.,
RA   Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Stolte C.,
RA   Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The genome sequence of Colletotrichum higginsianum IMI 34906.";
RL   Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
RN   [3] {ECO:0000313|EMBL:OBR02892.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|EMBL:OBR02892.1};
RA   O'Connell R., Zambounis A., Thon M., Dallery J.-F.;
RT   "Resequencing and annotation of the Colletotrichum higginsianum genome.";
RL   Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|Proteomes:UP000092177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000092177};
RX   PubMed=28851275; DOI=10.1186/s12864-017-4083-x;
RA   Dallery J.-F., Lapalu N., Zampounis A., Pigne S., Luyten I., Amselem J.,
RA   Wittenberg A.H.J., Zhou S., de Queiroz M.V., Robin G.P., Auger A.,
RA   Hainaut M., Henrissat B., Kim K.-T., Lee Y.-H., Lespinet O., Schwartz D.C.,
RA   Thon M.R., O'Connell R.J.;
RT   "Gapless genome assembly of Colletotrichum higginsianum reveals chromosome
RT   structure and association of transposable elements with secondary
RT   metabolite gene clusters.";
RL   BMC Genomics 18:667-667(2017).
CC   -!- FUNCTION: Palmitoyltransferase that targets several endosomal SNAREs.
CC       Palmitoylates the SNAREs at cysteine residues close to the cytoplasmic
CC       end of their transmembrane domain. May have a role in the cellular
CC       quality control of transmembrane domain-containing proteins.
CC       {ECO:0000256|ARBA:ARBA00043903}.
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. SWF1
CC       subfamily. {ECO:0000256|ARBA:ARBA00038463}.
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DR   EMBL; CACQ02001239; CCF34698.1; -; Genomic_DNA.
DR   EMBL; LTAN01000010; OBR02892.1; -; Genomic_DNA.
DR   RefSeq; XP_018151410.1; XM_018309092.1.
DR   STRING; 759273.H1V396; -.
DR   EnsemblFungi; CCF34698; CCF34698; CH063_06635.
DR   GeneID; 28873199; -.
DR   KEGG; chig:CH63R_14118; -.
DR   VEuPathDB; FungiDB:CH63R_14118; -.
DR   eggNOG; KOG1312; Eukaryota.
DR   HOGENOM; CLU_042181_2_1_1; -.
DR   OrthoDB; 5480099at2759; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   Proteomes; UP000092177; Chromosome 10.
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:SF286; PALMITOYLTRANSFERASE ZDHHC4; 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   Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW   Lipoprotein {ECO:0000256|ARBA:ARBA00023288};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU079119};
KW   Palmitate {ECO:0000256|ARBA:ARBA00023139};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        40..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        78..96
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        108..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        200..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        259..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          154..298
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
SQ   SEQUENCE   411 AA;  47085 MW;  CDEBE884BEBF465A CRC64;
     MGTLRNVALL VLGISFTVFV AFFGRLPALR HTPIATLHRL MWIHIPNAFL AVDKLLTGGR
     FSTSMMRFGN YMMHDRHPTV VIFFLLILSV SEYLYLPGAW PQLPLFHKIT GSVAIFLPYL
     FLYLSVMADP GYITSENHAY YMSLYPYDYS IFFPGQICST CNLIKPPRSK HCSICKRCVA
     KLDHHCIFIN GCVGYRNQHY FVLLLLSTAL LTSYGALLGF SLLSGKVGSQ YPAWSIWPPK
     GMEVKEYLLV WSWALQDNVG MGAVTLLAAM TSPLVWGLLS YTVWLIYCGT TTNESLKWSD
     WKAEMDDGCA FKRNMPTNRI KDTRFEPERT RWPLDAQQVL ARTDDGMPPP DHGPGEGEWE
     RVWNLKDVEN LYDLGLWDNM ADIFVSDYDF NVRRDQPSVE DPWRQRHTSK S
//
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