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Database: UniProt
Entry: J9J5N8_9SPIT
LinkDB: J9J5N8_9SPIT
Original site: J9J5N8_9SPIT 
ID   J9J5N8_9SPIT            Unreviewed;       703 AA.
AC   J9J5N8;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119};
DE            EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119};
GN   ORFNames=OXYTRI_00023 {ECO:0000313|EMBL:EJY88759.1};
OS   Oxytricha trifallax.
OC   Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; Spirotrichea;
OC   Stichotrichia; Sporadotrichida; Oxytrichidae; Oxytrichinae; Oxytricha.
OX   NCBI_TaxID=1172189 {ECO:0000313|EMBL:EJY88759.1};
RN   [1] {ECO:0000313|EMBL:EJY88759.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JRB310 {ECO:0000313|EMBL:EJY88759.1};
RX   PubMed=23382650; DOI=10.1371/journal.pbio.1001473;
RA   Swart E.C., Bracht J.R., Magrini V., Minx P., Chen X., Zhou Y.,
RA   Khurana J.S., Goldman A.D., Nowacki M., Schotanus K., Jung S., Fulton R.S.,
RA   Ly A., McGrath S., Haub K., Wiggins J.L., Storton D., Matese J.C.,
RA   Parsons L., Chang W.J., Bowen M.S., Stover N.A., Jones T.A., Eddy S.R.,
RA   Herrick G.A., Doak T.G., Wilson R.K., Mardis E.R., Landweber L.F.;
RT   "The Oxytricha trifallax Macronuclear Genome: A Complex Eukaryotic Genome
RT   with 16,000 Tiny Chromosomes.";
RL   PLoS Biol. 11:E1001473-E1001473(2013).
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       {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:EJY88759.1}.
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DR   EMBL; AMCR01000022; EJY88759.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9J5N8; -.
DR   EnsemblProtists; EJY88759; EJY88759; OXYTRI_00023.
DR   OrthoDB; 5475903at2759; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001594; Palmitoyltrfase_DHHC.
DR   PANTHER; PTHR24161; ANK_REP_REGION DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   PANTHER; PTHR24161:SF85; LD20463P-RELATED; 1.
DR   Pfam; PF12796; Ank_2; 1.
DR   Pfam; PF01529; DHHC; 1.
DR   SMART; SM00248; ANK; 4.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
DR   PROSITE; PS50216; DHHC; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU079119};
KW   ANK repeat {ECO:0000256|ARBA:ARBA00023043, ECO:0000256|PROSITE-
KW   ProRule:PRU00023}; Membrane {ECO:0000256|RuleBase:RU079119};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane {ECO:0000256|RuleBase:RU079119};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU079119}.
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        477..504
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   TRANSMEM        510..538
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU079119"
FT   REPEAT          334..363
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          458..545
FT                   /note="Palmitoyltransferase DHHC"
FT                   /evidence="ECO:0000259|Pfam:PF01529"
FT   REGION          549..569
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          589..620
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   703 AA;  80635 MW;  A8FE6F588D24B2E7 CRC64;
     MANPDSKASL NNNLEKRQGS QGYNQLLVSS FTDDYTKQTL LQKQNKLTFM NDKYSALESH
     YRQSLIDSVI ARSPQEISNN ITAMMVGGIS GGGGTGGMNL NSQIMTSSQV IEKSWGSGNK
     RSESKIINSD IVPQRLSDFA KNNYLKETTD IVLQNAQTMA SKDKDERFTN QLLIDQSQLM
     DSGVDMEIRQ IQIYIKDNNL RAILNYNMSK QELIDLKLCS QLNILQAICF YNAETILLWL
     ADALKEDEQA KRELAAYQEP FGGNQALHFA VINGNRKLIE IVLNEFQANP LGKTLQGLNV
     LHCAAQSDRG VLSLYYFIEI YHIDIESLDN FYCTPLHFAI LNKQFKAVEA LLGLGANPNS
     QIREGQSCLH LAVTKFIEET EDYEEPKRII KELLFNGASR DTKNTQSNCL CFMTHRPLEK
     VQKSRKFMIL ILAFNLINFA IFLAYYLRFV FTTNTDERFD HHCAYINNCL GHRNHKYFII
     FLFCIFIYFI SSTTVCLASI AMYGDPPHNA WAVIVWIIRI YTIAINCLQF VPLGYQIYEQ
     TKKLFKKEQF GDDESSRHQS RATSNMRSQI QGNAQSVLTY QSNLRKNESN NQENLLESQS
     KPNLSRKNSP RKQLLKKSTL QQSMTSQLSL INLERGRCYN FRQLFCYQPA TQEQLKAFLF
     SSSERFSTFI IRQQNEEKKK GQFNLSKVDK NITSDKYDET SIL
//
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