ID A0A2G8JAQ1_STIJA Unreviewed; 185 AA.
AC A0A2G8JAQ1;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 12.
DE SubName: Full=Putative serum paraoxonase/arylesterase 2-like {ECO:0000313|EMBL:PIK32845.1};
DE Flags: Fragment;
GN ORFNames=BSL78_30343 {ECO:0000313|EMBL:PIK32845.1};
OS Stichopus japonicus (Sea cucumber).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Holothuroidea;
OC Aspidochirotacea; Aspidochirotida; Stichopodidae; Apostichopus.
OX NCBI_TaxID=307972 {ECO:0000313|EMBL:PIK32845.1, ECO:0000313|Proteomes:UP000230750};
RN [1] {ECO:0000313|EMBL:PIK32845.1, ECO:0000313|Proteomes:UP000230750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Shaxun {ECO:0000313|EMBL:PIK32845.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:PIK32845.1};
RX PubMed=29023486;
RA Zhang X., Sun L., Yuan J., Sun Y., Gao Y., Zhang L., Li S., Dai H.,
RA Hamel J.F., Liu C., Yu Y., Liu S., Lin W., Guo K., Jin S., Xu P.,
RA Storey K.B., Huan P., Zhang T., Zhou Y., Zhang J., Lin C., Li X., Xing L.,
RA Huo D., Sun M., Wang L., Mercier A., Li F., Yang H., Xiang J.;
RT "The sea cucumber genome provides insights into morphological evolution and
RT visceral regeneration.";
RL PLoS Biol. 15:E2003790-E2003790(2017).
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|PIRSR:PIRSR602640-2};
CC Note=Binds 2 calcium ions per subunit. {ECO:0000256|PIRSR:PIRSR602640-
CC 2};
CC -!- SIMILARITY: Belongs to the paraoxonase family.
CC {ECO:0000256|ARBA:ARBA00008595}.
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:PIK32845.1}.
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DR EMBL; MRZV01003172; PIK32845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G8JAQ1; -.
DR STRING; 307972.A0A2G8JAQ1; -.
DR Proteomes; UP000230750; Unassembled WGS sequence.
DR GO; GO:0004064; F:arylesterase activity; IEA:InterPro.
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; PARAOXONASE; 1.
DR PANTHER; PTHR11799:SF12; PARAOXONASE-RELATED; 1.
DR Pfam; PF01731; Arylesterase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR602640-2};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR602640-2};
KW Reference proteome {ECO:0000313|Proteomes:UP000230750}.
FT REGION 166..185
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 29
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR602640-1"
FT BINDING 31
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 80
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 81
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 136
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 NON_TER 1
FT /evidence="ECO:0000313|EMBL:PIK32845.1"
SQ SEQUENCE 185 AA; 20666 MW; C6CD69781259B097 CRC64;
QSFLFDFNKP DGDAKELELI GDVRLASPHG ISLWEDKEGI QIFLVDHRLT EDTIEIFRFE
PPLSLRHTRT IYNPLFANLN DVIATGDSSF YVTNAASVRD GPLLTISFLL QLSTGSVVYY
DGVTARQVAG NGKILNGITS SSDGRFIFVS YMVDEAIVVF RREGDGSFDE SPNHQFVSYP
RQPIL
//