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Database: UniProt
Entry: A0A316U7D9_9BASI
LinkDB: A0A316U7D9_9BASI
Original site: A0A316U7D9_9BASI 
ID   A0A316U7D9_9BASI        Unreviewed;       626 AA.
AC   A0A316U7D9;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=BCV69DRAFT_282647 {ECO:0000313|EMBL:PWN21149.1};
OS   Pseudomicrostroma glucosiphilum.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC   Pseudomicrostroma.
OX   NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN21149.1, ECO:0000313|Proteomes:UP000245942};
RN   [1] {ECO:0000313|EMBL:PWN21149.1, ECO:0000313|Proteomes:UP000245942}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN21149.1,
RC   ECO:0000313|Proteomes:UP000245942};
RX   PubMed=29771364; DOI=10.1093/molbev/msy072;
RA   Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA   Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA   Spatafora J.W., Aime M.C.;
RT   "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT   clade Ustilaginomycotina.";
RL   Mol. Biol. Evol. 0:0-0(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; KZ819326; PWN21149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A316U7D9; -.
DR   STRING; 1684307.A0A316U7D9; -.
DR   OrthoDB; 6683at2759; -.
DR   Proteomes; UP000245942; 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:SF13; PALMITOYLTRANSFERASE ZDHHC16; 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:UP000245942};
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        35..56
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        68..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        368..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          292..405
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          223..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          420..448
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          487..511
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          551..626
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        237..259
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        487..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..568
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        599..614
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   626 AA;  69824 MW;  80F8C2F8846D6668 CRC64;
     MPSLSLLPLL ANCVNRSFRK VEKAADWLVG KAGPFFIAIC IGLVSIGAWT FFTLLLPSVL
     TPASESAFSL PTIASACLAL YCFNLIYSIA WYYYAACTIP PGGVSSFVSA AADLAYDQAS
     RQETDQDDAQ ASLRTGYLSN LDSHWTSYAD RARLASRWVS DAHDPSIEAY LDHERNVRGK
     TEEEIEEEDL WPRVKMCQKC EKVPLWWALA CLPEELRDVE KQRRSRNGDF DAGIEQDSKQ
     QPLQDDRPSP KSSSSTSITL SPWERTAVQP LRQSILAWLP ASTADTLVPP PKPERAHHCS
     VCKTCIIKFD HHCPWLNQCV GLYNERYFVG FLVYMVLGTS IVLVVGWPKA WEALRLWERW
     PYKTAPRLFV LLTYILCLAM GVALLVMLAS HLDMISRNLT SVESSDRQFY IGRAQMRQKE
     REVQRKAASK ATGRGSADAE TPEEKKRLKD AQALELERAW GNVYDLGTRT RNLAIFFNVG
     EGSSLASSSY PSSSSSLPEP TAPPARLTRR PRPRPVYYSL LPVRYPPHSD GWHWPKRRGT
     GGRAMLGVGL EEEVEFSGGE EEQEEQETPR EETSTKGGKG KKKKKGKGAA AGAASGSASE
     EQRRDEEREV LAGRTFDGSE AGLDMQ
//
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