ID A0A026W013_OOCBI Unreviewed; 662 AA.
AC A0A026W013;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN ORFNames=X777_12644 {ECO:0000313|EMBL:EZA49041.1};
OS Ooceraea biroi (Clonal raider ant) (Cerapachys biroi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Dorylinae; Ooceraea.
OX NCBI_TaxID=2015173 {ECO:0000313|EMBL:EZA49041.1, ECO:0000313|Proteomes:UP000053097};
RN [1] {ECO:0000313|EMBL:EZA49041.1, ECO:0000313|Proteomes:UP000053097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=24508170; DOI=10.1016/j.cub.2014.01.018;
RA Oxley P.R., Ji L., Fetter-Pruneda I., McKenzie S.K., Li C., Hu H.,
RA Zhang G., Kronauer D.J.;
RT "The genome of the clonal raider ant Cerapachys biroi.";
RL Curr. Biol. 24:451-458(2014).
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; KK107549; EZA49041.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A026W013; -.
DR STRING; 2015173.A0A026W013; -.
DR EnsemblMetazoa; XM_011348884.3; XP_011347186.1; LOC105284987.
DR OMA; CLRNCCY; -.
DR Proteomes; UP000053097; 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:UP000053097};
KW Transferase {ECO:0000256|RuleBase:RU079119, ECO:0000313|EMBL:EZA49041.1};
KW Transmembrane {ECO:0000256|RuleBase:RU079119};
KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 42..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 145..169
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT TRANSMEM 181..203
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU079119"
FT DOMAIN 99..219
FT /note="Palmitoyltransferase DHHC"
FT /evidence="ECO:0000259|Pfam:PF01529"
FT REGION 282..406
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 420..439
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 516..563
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 589..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 631..662
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 307..338
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 593..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 631..651
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 662 AA; 73214 MW; B11080F1D00ACF92 CRC64;
MPKCDVKTRY LPATLAWLML LVTTALFFIF PCSNYYVSRW GLWVPALEGV VTFFVVVNFS
LATFMDPGVI PKAPPDEDRE DDFRAPLYKS VEINGITVRM KWCVTCKFYR PPRCSHCSVC
NHCIETFDHH CPWVNNCIGR RNYRYFFFFL VSLSIHMICI FGLCLYYVLQ HKEKLSEATS
IISLVLMGLA MLLVIPIFGL TGFHMVLVSR GRTTNEQVTG KFNGGYNPFS RGCLRNCCYT
QFGPQYPSLL KPDKYSGKRR GACASEISTI GSENQVKTYM DSSNGVRNAS SNAYNKLSPG
RDGSDTDMEP TASQSADCEP TPPLQRHGSK SNFFLPPVEN NESPRHPPSS QHRHPIHYPR
GSPHPRPRGM NGSRSHTPDP LSPETSGSAA TVPQRGPGQG GASPTMQQRI KAIGVPTPLA
ISSPIRRSNP GTPTQVRRPD FIGVNEAPTY YDVQQGNSAV VGVTGSVVTG YSPQRRFLSE
SELVRQGTDH PYSRTNNTVD NIRELAGSPQ RGVYMWKDNS PGSYPGPPAG TVVSGAPHQS
PSQRPHPPYD YYRSNPTSPT QQSYAANAPR AAYHPAIRGG VPVFPPQPLQ SPQVKRKAAT
MATPTTPTSG DARRRPMSFV RALEMTDSME MVSAPNDSRS QRPTTPTPDR ASVYDMNYEI
SV
//
