ID Q22CX0_TETTS Unreviewed; 718 AA. AC Q22CX0; DT 18-APR-2006, integrated into UniProtKB/TrEMBL. DT 16-APR-2014, sequence version 3. DT 27-MAR-2024, entry version 119. DE RecName: Full=Palmitoyltransferase {ECO:0000256|RuleBase:RU079119}; DE EC=2.3.1.225 {ECO:0000256|RuleBase:RU079119}; GN ORFNames=TTHERM_01014660 {ECO:0000313|EMBL:EAR83149.3}; OS Tetrahymena thermophila (strain SB210). OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata; OC Oligohymenophorea; Hymenostomatida; Tetrahymenina; Tetrahymenidae; OC Tetrahymena. OX NCBI_TaxID=312017 {ECO:0000313|EMBL:EAR83149.3, ECO:0000313|Proteomes:UP000009168}; RN [1] {ECO:0000313|Proteomes:UP000009168} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SB210 {ECO:0000313|Proteomes:UP000009168}; RX PubMed=16933976; DOI=10.1371/journal.pbio.0040286; RA Eisen J.A., Coyne R.S., Wu M., Wu D., Thiagarajan M., Wortman J.R., RA Badger J.H., Ren Q., Amedeo P., Jones K.M., Tallon L.J., Delcher A.L., RA Salzberg S.L., Silva J.C., Haas B.J., Majoros W.H., Farzad M., RA Carlton J.M., Smith R.K. Jr., Garg J., Pearlman R.E., Karrer K.M., Sun L., RA Manning G., Elde N.C., Turkewitz A.P., Asai D.J., Wilkes D.E., Wang Y., RA Cai H., Collins K., Stewart B.A., Lee S.R., Wilamowska K., Weinberg Z., RA Ruzzo W.L., Wloga D., Gaertig J., Frankel J., Tsao C.-C., Gorovsky M.A., RA Keeling P.J., Waller R.F., Patron N.J., Cherry J.M., Stover N.A., RA Krieger C.J., del Toro C., Ryder H.F., Williamson S.C., Barbeau R.A., RA Hamilton E.P., Orias E.; RT "Macronuclear genome sequence of the ciliate Tetrahymena thermophila, a RT model eukaryote."; RL PLoS Biol. 4:1620-1642(2006). 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; GG662521; EAR83149.3; -; Genomic_DNA. DR RefSeq; XP_001030812.3; XM_001030812.3. DR AlphaFoldDB; Q22CX0; -. DR EnsemblProtists; EAR83149; EAR83149; TTHERM_01014660. DR GeneID; 7830086; -. DR KEGG; tet:TTHERM_01014660; -. DR eggNOG; KOG0509; Eukaryota. DR eggNOG; KOG0726; Eukaryota. DR HOGENOM; CLU_267706_0_0_1; -. DR InParanoid; Q22CX0; -. DR OrthoDB; 5318579at2759; -. DR Proteomes; UP000009168; Unassembled WGS sequence. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW. DR GO; GO:0019706; F:protein-cysteine S-palmitoyltransferase activity; IEA:UniProtKB-EC. DR Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1. DR InterPro; IPR002110; Ankyrin_rpt. DR InterPro; IPR036770; Ankyrin_rpt-contain_sf. DR InterPro; IPR001594; Palmitoyltrfase_DHHC. DR PANTHER; PTHR22883; ZINC FINGER DHHC DOMAIN CONTAINING PROTEIN; 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|ARBA:ARBA00023315, KW ECO:0000256|RuleBase:RU079119}; KW ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023}; KW Membrane {ECO:0000256|RuleBase:RU079119}; KW Proteasome {ECO:0000313|EMBL:EAR83149.3}; KW Reference proteome {ECO:0000313|Proteomes:UP000009168}; KW Transferase {ECO:0000256|RuleBase:RU079119}; KW Transmembrane {ECO:0000256|RuleBase:RU079119}; KW Transmembrane helix {ECO:0000256|RuleBase:RU079119}. FT TRANSMEM 326..343 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU079119" FT TRANSMEM 349..371 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU079119" FT TRANSMEM 461..484 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU079119" FT TRANSMEM 511..536 FT /note="Helical" FT /evidence="ECO:0000256|RuleBase:RU079119" FT REPEAT 219..251 FT /note="ANK" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00023" FT DOMAIN 413..551 FT /note="Palmitoyltransferase DHHC" FT /evidence="ECO:0000259|Pfam:PF01529" FT REGION 559..626 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 585..601 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 608..623 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 718 AA; 84166 MW; 47AA0EBB3E536A85 CRC64; MIPEKNIKNS VECFSGMQLP KNYSEAIKFL KSLSNQQNVK LDYIVEILKV YKGINLNKFP KFNLLVQAVK DNNEFAFNLF LDYLQQADIP QEDKIEYINS NKALNCEEGY NALQYAVYYE FQDMALKLIE KGARYDTHIN EIGDKIIHSA ARGGSLKVIM KLQQLGVDIF EKTQSKGLNL STFEIACFEG NLHIMKYLLK MDEFENQKRI DINEQHPVSK ETPLHLGIRS KDYSVVKFLL IQGANKQLKN NENQTPLQFA IWRKEKIQKK LKEKRETVDQ YQIMEWESKI NHLDSLISLL GDIKFFNRLK LQTRVGPTKG MNKYSYILRI INILGFIGFI FILPYTDLFI GFIVFFYSIY LCSFYCLFCS YKSDPGYIKQ LGYESYQLDL NNNQPASQKD TFVNNFWLLL CKKEFEELCL ECCIIKPVRS KHCDFCNRCV AVMDHHCPFI KNCVGAKNHR YFFFMLVTQA LSQISILIAC IFALKELQQD DIEDEHSHQF IDSCPQLFNP IIAYISISIL IIQFIITCFP LFFIIIHQRT ILVNGLTSLE MRYKGKFDKQ KKEEIDENQP VTEVPNRTKS KQHPETRSNS TSQSTARLSH SNINDDQEDE QPEITEDQLE STDDQDTGSL YTALSAQQRD IFQNRNTNPS NKKWYENIKC MLFKNRKNKF YFADEELHRR IFQNQDQRFS LSCSQQFSEK DCLSKTESRN QLLMQYIK //