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Database: UniProt
Entry: A0A094GTG3_9PEZI
LinkDB: A0A094GTG3_9PEZI
Original site: A0A094GTG3_9PEZI 
ID   A0A094GTG3_9PEZI        Unreviewed;       610 AA.
AC   A0A094GTG3;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
DE   Flags: Fragment;
GN   ORFNames=V501_07655 {ECO:0000313|EMBL:KFZ06157.1};
OS   Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ06157.1, ECO:0000313|Proteomes:UP000029315};
RN   [1] {ECO:0000313|EMBL:KFZ06157.1, ECO:0000313|Proteomes:UP000029315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFZ06157.1}.
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DR   EMBL; JPKD01002206; KFZ06157.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A094GTG3; -.
DR   STRING; 1420914.A0A094GTG3; -.
DR   HOGENOM; CLU_021757_0_0_1; -.
DR   Proteomes; UP000029315; 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:UP000029315};
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        354..378
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        384..405
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        499..522
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        542..566
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          455..579
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          1..181
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          238..322
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..83
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        97..142
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..254
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        270..290
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   NON_TER         610
FT                   /evidence="ECO:0000313|EMBL:KFZ06157.1"
SQ   SEQUENCE   610 AA;  64895 MW;  51CA76C6B65B7B5F CRC64;
     MSSSSPPRDP PPSQGGPPSI ISSRMTDIAS DDGHDLDTTS HATPAHRTST NRQSIQSSRP
     GTGSAAMSTR SPWSASPPSR RGPKSGGTPS ILGGVSGARP PSSTSRTHVP SLTSHAFFRP
     MSSQRLQAQR GGPRTPVAGQ NQRGSGDFGD APAVPSIASG YTGNPIQNRD ESGPPPPSRG
     TEISVQEYVQ TTTANTSPTH GHYQTTSLSS SVQPLQVNNA STNPNGLTVN TGLTTFRNAG
     LPAPSKSPHS FRSSFLLPSR GGDMAPHSPN RSNHGHSKLS SGATSPARPS DVTPLPSPLT
     PATGTLGEKH GPGGNGGGGA GGGGKGGVKN YVHFPGNTRF FLGGRFQNAR DRPVNIATGI
     LVVVPAVLFF VFQASWLWHR VSPAVPVVFA YLSFICFSSF IHASVSDPGI LPRDLHKFPP
     PPATEDPLTL APPTTAWLIV KSHLPASTAM EVPVKYCKTC HIWRPPRGHH CRICDNCIET
     HDHHCVWLNN CVGRRNYRYF FTFVAAGTGM AIFCIVTSVV QLSTVGRDNN SDFGSAIPRE
     RGVFALLIYA ALALPYPAAL LFYHIFLSGR GETTRELLNG RKFKRGERHR PFTLGSVIKN
     WIAVLGRPRG
//
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