PTER_DROVI
ID PTER_DROVI Reviewed; 350 AA.
AC B4LW09;
DT 03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Phosphotriesterase-related protein;
DE EC=3.1.-.-;
DE AltName: Full=Parathion hydrolase-related protein;
GN ORFNames=GJ23635;
OS Drosophila virilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7244;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15010-1051.87;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH940650; EDW66514.1; -; Genomic_DNA.
DR RefSeq; XP_002052994.1; XM_002052958.2.
DR AlphaFoldDB; B4LW09; -.
DR SMR; B4LW09; -.
DR STRING; 7244.FBpp0238052; -.
DR EnsemblMetazoa; FBtr0239560; FBpp0238052; FBgn0210732.
DR GeneID; 6629587; -.
DR KEGG; dvi:6629587; -.
DR eggNOG; ENOG502QQQR; Eukaryota.
DR HOGENOM; CLU_054760_0_1_1; -.
DR InParanoid; B4LW09; -.
DR OMA; MVKCGFI; -.
DR OrthoDB; 972282at2759; -.
DR PhylomeDB; B4LW09; -.
DR Proteomes; UP000008792; 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 InterPro; IPR017947; AryldialkylPase_Zn-BS.
DR InterPro; IPR032466; Metal_Hydrolase.
DR InterPro; IPR001559; Phosphotriesterase.
DR PANTHER; PTHR10819; PTHR10819; 1.
DR Pfam; PF02126; PTE; 1.
DR SUPFAM; SSF51556; SSF51556; 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_0000388680"
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; 39691 MW; 584608B26AD3ACD2 CRC64;
MTRIQTVLGS ITPNLLGRTL THEHVALDFE HFYKPPPADF ENELQQKISM ATLGYVRLYP
YSSRENVRFY DEEALEASRK DVLLYKKHGG GAIVENSSYG LKRNLEFIVD LAKTTGVHFI
AGTGHYIHAT QDATHTNLTV EQMTDLYTRD ILTGIDVKGR TVKCGFIGEV ASVYPVQEFE
RHALLAAGEI QEVLGCGVSL HPHRVSKAPF EIMRLYLEAG GHANKCVMSH LDRTIFDMDE
LLEFAKLGCY LQYDLFGTEC SYYQLNSTVD MISDGQRIEN LIKLINEGLV DRLLMSHDIH
TKHRLTSYGG HGYHHIHMNI LPRMFQRGVT LEQVEQMTVT NPANWLSFNA
