ID   A0A1I7UC07_9PELO        Unreviewed;       371 AA.
AC   A0A1I7UC07;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=palmitoyl-protein hydrolase {ECO:0000256|ARBA:ARBA00012423};
DE            EC=3.1.2.22 {ECO:0000256|ARBA:ARBA00012423};
OS   Caenorhabditis tropicalis.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=1561998 {ECO:0000313|Proteomes:UP000095282, ECO:0000313|WBParaSite:Csp11.Scaffold629.g7803.t2};
RN   [1] {ECO:0000313|WBParaSite:Csp11.Scaffold629.g7803.t2}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (NOV-2016) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the AB hydrolase superfamily. AB hydrolase 2
CC       family. {ECO:0000256|ARBA:ARBA00006499}.
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DR   AlphaFoldDB; A0A1I7UC07; -.
DR   STRING; 1561998.A0A1I7UC07; -.
DR   WBParaSite; Csp11.Scaffold629.g7803.t2; Csp11.Scaffold629.g7803.t2; Csp11.Scaffold629.g7803.
DR   Proteomes; UP000095282; Unplaced.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003140; PLipase/COase/thioEstase.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR   PANTHER; PTHR10655; LYSOPHOSPHOLIPASE-RELATED; 1.
DR   PANTHER; PTHR10655:SF17; PALMITOYL-PROTEIN HYDROLASE; 1.
DR   Pfam; PF02230; Abhydrolase_2; 1.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
FT   DOMAIN          7..86
FT                   /note="Ribosomal protein eL8/eL30/eS12/Gadd45"
FT                   /evidence="ECO:0000259|Pfam:PF01248"
FT   DOMAIN          156..368
FT                   /note="Phospholipase/carboxylesterase/thioesterase"
FT                   /evidence="ECO:0000259|Pfam:PF02230"
FT   REGION          137..160
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..155
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   371 AA;  40072 MW;  D373F08FBC900886 CRC64;
     MFKNFQKRRV VCGAHEALSK VQRGKAQLVF YAKNLDENNR RAASNVHQLQ KQCPLEGIPL
     IEALTRKEMS RVMNKFPYVG VVAVTDFSGL FTRVLLSSAA VSTQSSSSTV LASKPSQQKF
     LASIIGSSLS SRLLCSLGGS SPSDEEETPM SISQGTPAVV KPRGEQKGTL IFLHGLGDQG
     HGWADSFSTE ARVDTVKVIC PHSSERSVSL NMGMRMPAWY DLFGLSLTSP EDNEGIQNAA
     AYVHSLIDAE VAAGVPASKV IVGGFSMGGA LAIYAGLTYP QKLGGIIGLS SFFLQRTKFP
     GAYTANNATN IFLGHGNVDQ LVPFQFGQMS ETLIKKFNPN VQLHAYRDMG HQSCAEEMRD
     VKAFISNNIG K
//