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Database: UniProt
Entry: A0A195EEP9_9HYME
LinkDB: A0A195EEP9_9HYME
Original site: A0A195EEP9_9HYME 
ID   A0A195EEP9_9HYME        Unreviewed;       666 AA.
AC   A0A195EEP9;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=ALC57_03796 {ECO:0000313|EMBL:KYN26755.1};
OS   Trachymyrmex cornetzi.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC   Formicidae; Myrmicinae; Trachymyrmex.
OX   NCBI_TaxID=471704 {ECO:0000313|EMBL:KYN26755.1, ECO:0000313|Proteomes:UP000078492};
RN   [1] {ECO:0000313|EMBL:KYN26755.1, ECO:0000313|Proteomes:UP000078492}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tcor2-1 {ECO:0000313|EMBL:KYN26755.1};
RC   TISSUE=Whole body {ECO:0000313|EMBL:KYN26755.1};
RA   Nygaard S., Hu H., Boomsma J., Zhang G.;
RT   "Trachymyrmex cornetzi WGS genome.";
RL   Submitted (SEP-2015) 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|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       ERF2/ZDHHC9 subfamily. {ECO:0000256|ARBA:ARBA00023463}.
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DR   EMBL; KQ978983; KYN26755.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A195EEP9; -.
DR   STRING; 471704.A0A195EEP9; -.
DR   Proteomes; UP000078492; Unassembled WGS sequence.
DR   GO; GO:0043229; C:intracellular organelle; IEA:UniProt.
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; PTHR12349; ANKYRIN REPEAT AND LEM DOMAIN-CONTAINING PROTEIN 2; 1.
DR   PANTHER; PTHR12349:SF2; PALMITOYLTRANSFERASE ZDHHC8; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW   Membrane {ECO:0000256|RuleBase:RU079119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078492};
KW   Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:KYN26755.1};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        12..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        42..64
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        152..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        188..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   DOMAIN          106..226
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          289..410
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          424..443
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          515..570
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..617
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          630..658
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        289..306
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        314..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        382..410
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        556..570
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        596..616
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        637..655
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   666 AA;  74275 MW;  DB2953781A4AD9DB CRC64;
     MPKCDVKTRP LPATFAWIVL LISTALFFIF PCWNYYVSRW GLWVPILQGV ITFFVVINFS
     LATFMDPGVI PKAIWFFIKA PPDEDREDDF RAPLYKSVEI NGITVRMKWC VTCKFYRPPR
     CSHCSVCNHC IETFDHHCPW VNNCIGRRNY RYFFFFLLSL SFHMLSIFGL CLYYLLEHKE
     QLSEVNTIVA LILMGVVMLL FIPIFGLTGF HVVLVSRGRT TNEQVTGKFN GGYNPFSRGC
     LRNCCHTQFG PQYPSLLKPD KYSGKRRGAC ASEISTIGSE NQVKTYMDSS NGVRNASSNA
     YNKLSPGRDG SDTDMEPTAS QSADCEPTPP LQRHGSKSNF FLPPVENNES PRHPPPSQLR
     HPIHYPRGSP HPRPRGMNGS RSHTPDPLSP ETSGSPATVP QRQGGASPTM QQRIKAIGVP
     TPLAISSPIR RSNPGTPTQV RRPDFIGVNE APTYYDVQQG NTGVGVPGSV ITGYSPQRRF
     LSESELVRQG TDHPYSRTNN TVDNIRELAG SPQRGVYMWK DNSPGSYPGP PPGGAVSSTA
     HQSPSHRPPP YDYYRSNPTS PTQQSQYTTN APRAAYHPAL RGGVPVFPPH QPHQSPQVKR
     KATTMATPTT PTSGDARRRP MSFVRALEMT DSMEMVSAPN DPRSQRPTTP TPDRASVYDM
     NYEISV
//
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