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Database: UniProt
Entry: PTER_DROWI
LinkDB: PTER_DROWI
Original site: PTER_DROWI 
ID   PTER_DROWI              Reviewed;         350 AA.
AC   B4NAJ1;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   23-SEP-2008, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Phosphotriesterase-related protein;
DE            EC=3.1.-.-;
DE   AltName: Full=Parathion hydrolase-related protein;
GN   ORFNames=GK11368;
OS   Drosophila willistoni (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=7260;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tucson 14030-0811.24;
RX   PubMed=17994087; DOI=10.1038/nature06341;
RG   Drosophila 12 genomes consortium;
RT   "Evolution of genes and genomes on the Drosophila phylogeny.";
RL   Nature 450:203-218(2007).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250|UniProtKB:P45548};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000250|UniProtKB:P45548};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR   EMBL; CH964232; EDW80805.1; -; Genomic_DNA.
DR   RefSeq; XP_002069819.1; XM_002069783.2.
DR   AlphaFoldDB; B4NAJ1; -.
DR   SMR; B4NAJ1; -.
DR   STRING; 7260.B4NAJ1; -.
DR   EnsemblMetazoa; FBtr0242019; FBpp0240511; FBgn0213379.
DR   GeneID; 6647896; -.
DR   KEGG; dwi:6647896; -.
DR   eggNOG; ENOG502QQQR; Eukaryota.
DR   HOGENOM; CLU_054760_0_1_1; -.
DR   OMA; MVKCGFI; -.
DR   OrthoDB; 5387837at2759; -.
DR   PhylomeDB; B4NAJ1; -.
DR   Proteomes; UP000007798; Unassembled WGS sequence.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0009056; P:catabolic process; IEA:InterPro.
DR   CDD; cd00530; PTE; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001559; Phosphotriesterase.
DR   PANTHER; PTHR10819; PHOSPHOTRIESTERASE-RELATED; 1.
DR   PANTHER; PTHR10819:SF3; PHOSPHOTRIESTERASE-RELATED PROTEIN; 1.
DR   Pfam; PF02126; PTE; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
DR   PROSITE; PS01322; PHOSPHOTRIESTERASE_1; 1.
DR   PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..350
FT                   /note="Phosphotriesterase-related protein"
FT                   /id="PRO_0000388681"
FT   BINDING         22
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         24
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         169
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         169
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         201
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         230
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         298
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
SQ   SEQUENCE   350 AA;  39402 MW;  C2E9A252E3BE81A9 CRC64;
     MSTVQTVLGA ITPNLLGRTL THEHVALDFE HFFRPPPADF ERELQAKISM STLGYVRMYP
     YSSKENVRFY DEEALEAAKK DVLLYKKHGG GSIVENSSYG LKRNLEFIVD LAKSTGVHFI
     AGTGHYIHAV QDASHASLTV EQMSDLYSKD IITGIQVNGE TVKCGFIGEV ASVYPVHEFE
     KHSLQAAGEI QEVLGCGVSL HPHRVTNAPF EIMRLYMEAG GRANKCVMSH LDRTIFDIDE
     LLEFAKLGCY MQYDLFGTEC SYYQLNSTIN MLSDGQRIDN LMKLIEEGLV DRLLMSHDIH
     TKHRLTSYGG HGYHHIHMNI LPRMFAKGVT IEQVEQMTVT NPANWLAFNP
//
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