ID A0A099ZGW6_TINGU Unreviewed; 349 AA.
AC A0A099ZGW6;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 22-FEB-2023, entry version 25.
DE RecName: Full=Phosphotriesterase-related protein {ECO:0000256|ARBA:ARBA00020475};
DE AltName: Full=Parathion hydrolase-related protein {ECO:0000256|ARBA:ARBA00029607};
DE Flags: Fragment;
GN ORFNames=N309_14794 {ECO:0000313|EMBL:KGL80045.1};
OS Tinamus guttatus (White-throated tinamou).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Palaeognathae; Tinamiformes; Tinamidae; Tinamus.
OX NCBI_TaxID=94827 {ECO:0000313|EMBL:KGL80045.1, ECO:0000313|Proteomes:UP000053641};
RN [1] {ECO:0000313|EMBL:KGL80045.1, ECO:0000313|Proteomes:UP000053641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N309 {ECO:0000313|EMBL:KGL80045.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|PIRSR:PIRSR601559-52};
CC Note=Binds 2 divalent metal cations per subunit.
CC {ECO:0000256|PIRSR:PIRSR601559-52};
CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC Phosphotriesterase family. {ECO:0000256|PROSITE-ProRule:PRU00679}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00679}.
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DR EMBL; KL892764; KGL80045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A099ZGW6; -.
DR STRING; 94827.A0A099ZGW6; -.
DR Proteomes; UP000053641; 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 PIRSF; PIRSF016839; PhP; 2.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR601559-52};
KW Reference proteome {ECO:0000313|Proteomes:UP000053641}.
FT BINDING 26
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 28
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 169
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 201
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 230
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT BINDING 298
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR601559-52"
FT NON_TER 349
FT /evidence="ECO:0000313|EMBL:KGL80045.1"
SQ SEQUENCE 349 AA; 38776 MW; 51F882242C23A845 CRC64;
MPSLGGKVQT VLGLVEPDQL GYTLTHEHLS MNYTCCYFPP APGQEPLSEG PIEMKNLFWI
KQHPYSHKEN LLLYQETAAV KEELLLFKAA GGGTIVENTT TGIDRDMNAL KKLAEETGVH
IVAGAGFYVD STHSSHTQAM TVEQLTGVLV DEILRGADGT GIRCGVVGEL GCSWPLTPSE
QRVLQAAAHA QAQLGCPVIV HPGRSSDAPF QIIRILQEAG ADVSKTVMCH LDRTIFDTKK
LLEFAELGCY LEYDLFGVEF LHYQFQPSVD MPSDNERIAR IRTLIGEGYE DRILIAHDVH
TKHRLMKYGG HGYSHILKNI VPKMLVRGIS QSQIDKILLE NPKRWLTFK
//
