ID A0A139AY40_GONPJ Unreviewed; 345 AA.
AC A0A139AY40;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=M427DRAFT_150949 {ECO:0000313|EMBL:KXS21617.1};
OS Gonapodya prolifera (strain JEL478) (Monoblepharis prolifera).
OC Eukaryota; Fungi; Fungi incertae sedis; Chytridiomycota;
OC Chytridiomycota incertae sedis; Monoblepharidomycetes; Monoblepharidales;
OC Gonapodyaceae; Gonapodya.
OX NCBI_TaxID=1344416 {ECO:0000313|EMBL:KXS21617.1, ECO:0000313|Proteomes:UP000070544};
RN [1] {ECO:0000313|EMBL:KXS21617.1, ECO:0000313|Proteomes:UP000070544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JEL478 {ECO:0000313|EMBL:KXS21617.1,
RC ECO:0000313|Proteomes:UP000070544};
RX PubMed=25977457; DOI=10.1093/gbe/evv090;
RA Chang Y., Wang S., Sekimoto S., Aerts A.L., Choi C., Clum A., LaButti K.M.,
RA Lindquist E.A., Yee Ngan C., Ohm R.A., Salamov A.A., Grigoriev I.V.,
RA Spatafora J.W., Berbee M.L.;
RT "Phylogenomic Analyses Indicate that Early Fungi Evolved Digesting Cell
RT Walls of Algal Ancestors of Land Plants.";
RL Genome Biol. Evol. 7:1590-1601(2015).
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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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}.
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DR EMBL; KQ965732; KXS21617.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A139AY40; -.
DR STRING; 1344416.A0A139AY40; -.
DR OMA; MLPRRNI; -.
DR OrthoDB; 1365413at2759; -.
DR Proteomes; UP000070544; 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:SF203; PALMITOYLTRANSFERASE; 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:UP000070544};
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 100..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 233..260
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 280..310
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 187..324
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 345 AA; 38728 MW; 71BCAC73A3F6FE79 CRC64;
MNGQRSPSLA PSGFSNPSST FSSQIARLET SNSHHLPSPG SPTPTLTSHR TSFSVINEPL
PLAKQPLVYW SDRRFWATDI RRDIRADNSW RRESAWQRPF HISFLTILLM FIYSYCVFFS
TTSFFVEPLI GIPNLVGWIV FGLAGVSMAG MVLYVTLVEV EASEVRQAGK ARNLDFVKTV
GVHVIDNGVC GICCVSVPVR TRHCKSCNKC VADFDHHCPY LNTCIAGRNY QGFLVLLSTT
VWVSALSMLL SFRVFVALFT ERDLFIRTLS STWHTFGDEN SLWVLAGVLI CFEGVIALLV
FVMSTALAIF HAYLRVLGMT TFEYNTGVRS TSRLQFLDFR RRSSS
//
