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Database: UniProt
Entry: A0A3N2QAB5_9PEZI
LinkDB: A0A3N2QAB5_9PEZI
Original site: A0A3N2QAB5_9PEZI 
ID   A0A3N2QAB5_9PEZI        Unreviewed;       621 AA.
AC   A0A3N2QAB5;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=SODALDRAFT_336925 {ECO:0000313|EMBL:ROT43692.1};
OS   Sodiomyces alkalinus F11.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX   NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT43692.1, ECO:0000313|Proteomes:UP000272025};
RN   [1] {ECO:0000313|EMBL:ROT43692.1, ECO:0000313|Proteomes:UP000272025}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F11 {ECO:0000313|EMBL:ROT43692.1,
RC   ECO:0000313|Proteomes:UP000272025};
RX   PubMed=30368956; DOI=10.1111/mec.14912;
RA   Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA   Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA   Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA   Grigoriev I.V., Debets A.J.M.;
RT   "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT   shifted to a protein diet.";
RL   Mol. Ecol. 27:4808-4819(2018).
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; ML119051; ROT43692.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3N2QAB5; -.
DR   STRING; 1314773.A0A3N2QAB5; -.
DR   OrthoDB; 6683at2759; -.
DR   Proteomes; UP000272025; 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; PTHR12246; PALMITOYLTRANSFERASE ZDHHC16; 1.
DR   PANTHER; PTHR12246:SF19; S-ACYLTRANSFERASE; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {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:UP000272025};
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        12..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        46..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        153..177
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        189..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          104..231
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          275..298
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          408..560
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          597..621
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        418..461
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        510..531
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        532..549
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   621 AA;  68808 MW;  FC68C384174F2F2B CRC64;
     MARRWARRVE RGCCLFATYL PLTLVYGLTT WALWVDVSIG SLPTKMPWIG TGTSIGAVII
     YALLNWSYTT AVFTDPGSTT NKYGYSELPT EAPPVATSFT VKSNGEMRFC KKCQARKPDR
     AHHCSSCRRC VLKMDHHCPW LATCVGLRNH KAFLLFLIYT TLLCFYSFAL AGAWTYVEII
     DNNTTYVDAL LPINLIILSV VAGIIGVVIG AFTGWHVMLA GRGQTTIECL EKTRYLSPLR
     KTMESRTIRG MPLPGYGRQL IDMHANALPG ITRPEEGEEM RRDPAGRDGQ RRPMAMSYEE
     LERQRARKRY EEYLDEQDSK NLPSAFDLGF KRNLLHLFGP SPLLWFVPVC NTTGDGWSWE
     PSPKWLAARE RIAAEREAQR AREVTAGWGA EAPPQFYAPS VPLSLSLPLP SPSPSPSPSQ
     FGAGRHYLQP QKTQAQRSSS SSAASPSAAS PSATPSRSSP LPSPFGRKMP SKADRVLGRD
     PNLYADGPQE AVSMQRLNRK GRALEDELGL TDENYEDDDE EEEDDDDDEK YRDDDVGNKW
     GDDGENSRLV RKGGGTAVTK TGRKDEVAAV VEHRTLNLVT NGNNWRRGGA SGLLRTASHS
     PVATRAAVSS KDPLEDDDTV D
//
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