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
//