PFA5_ASHGO
ID PFA5_ASHGO Reviewed; 359 AA.
AC Q75D19;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2013, sequence version 2.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Palmitoyltransferase PFA5;
DE EC=2.3.1.225;
DE AltName: Full=Protein fatty acyltransferase 5;
GN Name=PFA5; OrderedLocusNames=ABR203W;
OS Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056)
OS (Yeast) (Eremothecium gossypii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=284811;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=15001715; DOI=10.1126/science.1095781;
RA Dietrich F.S., Voegeli S., Brachat S., Lerch A., Gates K., Steiner S.,
RA Mohr C., Poehlmann R., Luedi P., Choi S., Wing R.A., Flavier A.,
RA Gaffney T.D., Philippsen P.;
RT "The Ashbya gossypii genome as a tool for mapping the ancient Saccharomyces
RT cerevisiae genome.";
RL Science 304:304-307(2004).
RN [2]
RP GENOME REANNOTATION, AND SEQUENCE REVISION TO 241.
RC STRAIN=ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056;
RX PubMed=23749448; DOI=10.1534/g3.112.002881;
RA Dietrich F.S., Voegeli S., Kuo S., Philippsen P.;
RT "Genomes of Ashbya fungi isolated from insects reveal four mating-type
RT loci, numerous translocations, lack of transposons, and distinct gene
RT duplications.";
RL G3 (Bethesda) 3:1225-1239(2013).
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;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- DOMAIN: The DHHC domain is required for palmitoyltransferase activity.
CC {ECO:0000250}.
CC -!- PTM: Autopalmitoylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the DHHC palmitoyltransferase family. PFA5
CC subfamily. {ECO:0000305}.
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DR EMBL; AE016815; AAS50976.2; -; Genomic_DNA.
DR RefSeq; NP_983152.2; NM_208505.2.
DR AlphaFoldDB; Q75D19; -.
DR STRING; 33169.AAS50976; -.
DR EnsemblFungi; AAS50976; AAS50976; AGOS_ABR203W.
DR GeneID; 4619262; -.
DR KEGG; ago:AGOS_ABR203W; -.
DR eggNOG; KOG1311; Eukaryota.
DR HOGENOM; CLU_064801_0_0_1; -.
DR InParanoid; Q75D19; -.
DR OMA; YCVWIGT; -.
DR Proteomes; UP000000591; Chromosome II.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IBA:GO_Central.
DR GO; GO:0018230; P:peptidyl-L-cysteine S-palmitoylation; IBA:GO_Central.
DR GO; GO:0006612; P:protein targeting to membrane; IBA:GO_Central.
DR InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR Pfam; PF01529; DHHC; 1.
DR PROSITE; PS50216; DHHC; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipoprotein; Membrane; Palmitate; Reference proteome;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..359
FT /note="Palmitoyltransferase PFA5"
FT /id="PRO_0000212973"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 47..67
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 206..226
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 120..170
FT /note="DHHC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00067"
SQ SEQUENCE 359 AA; 41610 MW; 959886B9706059CF CRC64;
MWQCKNKSRW WYSLVPILCI CIMCYGAIAY SYSFCYVEVW THLGMKAAAI GMTCLHLIIV
ILLWIIWAQI IMMGPGRQPR VAPFMILPEM ADAGERAKEG AATSVLPPDV YQCDTQGYPV
WCSVCQSLKG LRTHHSVHLG FCVPRLDHYC VWLGTVIGRR NYRLFNQFLM CFLMHALIIF
VSVVSLQRRI ASSARMRGER EDPNVLVVLS LSCLVLLMVG ALFISFLNYM ANNQTTIEKL
YTPKRQPRTM CFCVYNPADQ YRYVVKSLPH ENWNMWDKGS AYANYKDFLG SSIWRWFIPI
GSNIPEFQTS AWEDDYNAIL GPYKEELGSH YRDILMQRIE QGKYVTRLRV YGDKFREGL