ID   PTER_SALSA              Reviewed;         349 AA.
AC   B5X4Y9;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Phosphotriesterase-related protein;
DE            EC=3.1.-.-;
DE   AltName: Full=Parathion hydrolase-related protein;
GN   Name=pter;
OS   Salmo salar (Atlantic salmon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Protacanthopterygii; Salmoniformes;
OC   Salmonidae; Salmoninae; Salmo.
OX   NCBI_TaxID=8030;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
RX   PubMed=20433749; DOI=10.1186/1471-2164-11-279;
RA   Leong J.S., Jantzen S.G., von Schalburg K.R., Cooper G.A., Messmer A.M.,
RA   Liao N.Y., Munro S., Moore R., Holt R.A., Jones S.J., Davidson W.S.,
RA   Koop B.F.;
RT   "Salmo salar and Esox lucius full-length cDNA sequences reveal changes in
RT   evolutionary pressures on a post-tetraploidization genome.";
RL   BMC Genomics 11:279-279(2010).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily.
CC       Phosphotriesterase family. {ECO:0000255|PROSITE-ProRule:PRU00679}.
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DR   EMBL; BT046108; ACI34370.1; -; mRNA.
DR   RefSeq; NP_001135294.1; NM_001141822.1.
DR   AlphaFoldDB; B5X4Y9; -.
DR   SMR; B5X4Y9; -.
DR   GeneID; 100196800; -.
DR   KEGG; sasa:100196800; -.
DR   CTD; 9317; -.
DR   OMA; MVKCGFI; -.
DR   OrthoDB; 972282at2759; -.
DR   Proteomes; UP000087266; Chromosome ssa03.
DR   Bgee; ENSSSAG00000041406; Expressed in mesonephros and 15 other tissues.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR032466; Metal_Hydrolase.
DR   InterPro; IPR001559; Phosphotriesterase.
DR   PANTHER; PTHR10819; PTHR10819; 1.
DR   Pfam; PF02126; PTE; 1.
DR   PIRSF; PIRSF016839; PhP; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
DR   PROSITE; PS51347; PHOSPHOTRIESTERASE_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Metal-binding; Reference proteome.
FT   CHAIN           1..349
FT                   /note="Phosphotriesterase-related protein"
FT                   /id="PRO_0000388668"
FT   BINDING         26
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P45548"
FT   BINDING         28
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   349 AA;  38743 MW;  5FE63E23158A1081 CRC64;
     MSALSGKVQT VLGPIEPDQL GRTMTHEHLT MTFECCYFSP APGDETVAQA PIQMKNLFWL
     KQNPYSSHEN LLLLQETNAV REELHEYRKA GGGTIVENTT QGIARDLPCL KQLAKESGVH
     IIGGAGYYVD ATHSEATRKM TVEKLTDIII SEVLHGADGT EIRCGVIGEI GCSWPITDSE
     KKVLQATAHA QTELGCPVII HPGRNPGAPA EIVRLLQEAG GDISKTVMSH LDRTIFDNGE
     LLEFAKMGSY LEYDLFGMET LNYAYNLEVD MPSDSQRVKA LAFLVQEGYE DNIVIAHDIH
     TKNRLTKYGG HGYSHILKNI VPKMLKRGIN QTQVDKILID NPKRWLTFK