ID A0A1Q8S591_9PEZI Unreviewed; 813 AA.
AC A0A1Q8S591;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=CCHL11_00759 {ECO:0000313|EMBL:OLN96541.1};
OS Colletotrichum chlorophyti.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum.
OX NCBI_TaxID=708187 {ECO:0000313|EMBL:OLN96541.1, ECO:0000313|Proteomes:UP000186583};
RN [1] {ECO:0000313|EMBL:OLN96541.1, ECO:0000313|Proteomes:UP000186583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTL11 {ECO:0000313|EMBL:OLN96541.1,
RC ECO:0000313|Proteomes:UP000186583};
RA Gan P., Narusaka M., Tsushima A., Narusaka Y., Takano Y., Shirasu K.;
RT "Draft Genome Assembly of Colletotrichum chlorophyti a pathogen of
RT herbaceous plants.";
RL Submitted (NOV-2016) 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:OLN96541.1}.
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DR EMBL; MPGH01000017; OLN96541.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q8S591; -.
DR STRING; 708187.A0A1Q8S591; -.
DR OrthoDB; 5480099at2759; -.
DR Proteomes; UP000186583; 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:UP000186583};
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 379..403
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 409..430
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 524..549
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 569..591
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 480..605
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 1..345
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 670..794
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 290..337
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 671..700
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 813 AA; 88378 MW; 34448036190169BC CRC64;
MTSKDHPGGH NAPNGDDGFP KPQFPGRSDR PGPPSIISSR MTDIASDDGG EAAVQTLSNN
QRRRSGIASE TVSRPGTAKT GVSGPQEGRR RGPPPRMNYI TSLNEKRGSI GSGSIAGSIS
SRPPSSTSRS HVPSLTSSAF FRPMSSQKLQ AQRGGSSRPV TQNRQQQALA DADSTAEPSA
AAAAAVASGG PNARHSVISN PVSNPVARVQ RHLSGDGDMR PPPSRGTEYT DQGTYDRITA
NTSPTHGHHH AGSMSESVTP LQRNQRNSRN LSVNVDRRFG ERGGQPSPIK SPRSFRSSFL
LPGRSDQGQN KSNRSLPGGE KLSSTASTPQ LNPVDSSRPA DKHNLKKSKT NLGYVFQYFE
GNTVFCLGGR FQNTKHRPIN VATGLFIILP AVLFFVFSAS WLWHEISPAI PVTFGYLFYI
CISSFLHASV SDPGILPRNL HNFPPVEPTD DPLRLGPPTN DWVLIKSAES STAAMEVPVK
HCRTCNIWRP PRAHHCRLCD NCIETHDHHC VWLNNCVGRR NYRYFFAFVS SATFLALYLL
GASLTQILIH MNREGISFGQ AIDHFRVPFA MVIYGFVAFL YPAALMGYHI FLMARGETTR
EYINSHKFIK KERFRAFTQG SMLKNWIVVL CRPRPPTYYQ FKTKYQSGDQ RLGAFRDQPK
NDNQGVEMQN AEYEGERRGQ CETNDERASP FDDFFGGRFR TDTERMGGSY GTGGGGPGGS
GFGGQSAGFG RDGGFDAGNG GFSGAEGGMR SPGFGGNGGG DTGRGYGTGG SFPIPGDTRR
GGGRHDLGRI PQPLPASVYR RQRLWISRGS ATC
//
