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Database: UniProt
Entry: A0A0N5CZC8_THECL
LinkDB: A0A0N5CZC8_THECL
Original site: A0A0N5CZC8_THECL 
ID   A0A0N5CZC8_THECL        Unreviewed;       361 AA.
AC   A0A0N5CZC8;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Paraoxonase {ECO:0000256|RuleBase:RU368025};
DE            EC=3.1.1.2 {ECO:0000256|RuleBase:RU368025};
GN   ORFNames=TCLT_LOCUS5828 {ECO:0000313|EMBL:VDN03118.1};
OS   Thelazia callipaeda (Oriental eyeworm) (Parasitic nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Thelazioidea; Thelaziidae; Thelazia.
OX   NCBI_TaxID=103827 {ECO:0000313|Proteomes:UP000046394, ECO:0000313|WBParaSite:TCLT_0000583901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TCLT_0000583901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDN03118.1, ECO:0000313|Proteomes:UP000276776}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a phenyl acetate + H2O = a phenol + acetate + H(+);
CC         Xref=Rhea:RHEA:17309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:33853, ChEBI:CHEBI:140310; EC=3.1.1.2;
CC         Evidence={ECO:0000256|RuleBase:RU368025};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602640-2,
CC         ECO:0000256|RuleBase:RU368025};
CC       Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC       2, ECO:0000256|RuleBase:RU368025};
CC   -!- SIMILARITY: Belongs to the paraoxonase family.
CC       {ECO:0000256|ARBA:ARBA00008595, ECO:0000256|RuleBase:RU368025}.
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DR   EMBL; UYYF01004367; VDN03118.1; -; Genomic_DNA.
DR   STRING; 103827.A0A0N5CZC8; -.
DR   WBParaSite; TCLT_0000583901-mRNA-1; TCLT_0000583901-mRNA-1; TCLT_0000583901.
DR   OMA; NAMYLLV; -.
DR   Proteomes; UP000046394; Unplaced.
DR   Proteomes; UP000276776; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004064; F:arylesterase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR   InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR   InterPro; IPR002640; Arylesterase.
DR   PANTHER; PTHR11799:SF28; MECHANOSENSORY ABNORMALITY PROTEIN 6; 1.
DR   PANTHER; PTHR11799; PARAOXONASE; 1.
DR   Pfam; PF01731; Arylesterase; 1.
DR   PRINTS; PR01785; PARAOXONASE.
DR   SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|PIRSR:PIRSR602640-2, ECO:0000256|RuleBase:RU368025};
KW   Disulfide bond {ECO:0000256|RuleBase:RU368025};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180,
KW   ECO:0000256|RuleBase:RU368025};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368025};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2,
KW   ECO:0000256|RuleBase:RU368025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000276776};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   BINDING         112
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         163
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
FT   BINDING         218
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602640-2"
SQ   SEQUENCE   361 AA;  40615 MW;  88D4872049EFC4B2 CRC64;
     MSTSIITLLF VGLGCSIFVR LLLLLDVNKR VYNHTPGPCR LVWTPAVNGS GGITLISELD
     IALITSGYAK SRGVTSVVGA IYLYNFTDNR NYKANKLNIK GFDLRKFIPY GIDTYVSRGR
     VTVYVTNSLP NNDTVEVFQL DLNNLALIHR KTISSSKFLN LADIVVVGAD RFVVTNYLYF
     RQRWMQMLEL AMQAFSGSVV YYDGHEGSYL LKYFPAPNGI ALNKQKNQLY VASTISEFIR
     VYNLRQDMSL LFETEISLLS SPNKLFVEEA TGDIWIALHP VLYKAHEHIQ DPANMNLKSP
     SQILRIRLQD DGKSWVITEP YANDGATIWG SSAVLFHKNI MLIGSFFGRT LHCDIDSSQI
     V
//
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