ID G5BFE9_HETGA Unreviewed; 349 AA.
AC G5BFE9;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=Phosphotriesterase-related protein {ECO:0000256|ARBA:ARBA00020475};
DE AltName: Full=Parathion hydrolase-related protein {ECO:0000256|ARBA:ARBA00029607};
GN Name=PTER {ECO:0000313|EMBL:JAO00634.1};
GN ORFNames=GW7_20304 {ECO:0000313|EMBL:EHB08010.1};
OS Heterocephalus glaber (Naked mole rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC Heterocephalus.
OX NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB08010.1, ECO:0000313|Proteomes:UP000006813};
RN [1] {ECO:0000313|EMBL:EHB08010.1, ECO:0000313|Proteomes:UP000006813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21993625; DOI=10.1038/nature10533;
RA Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT "Genome sequencing reveals insights into physiology and longevity of the
RT naked mole rat.";
RL Nature 479:223-227(2011).
RN [2] {ECO:0000313|EMBL:JAO00634.1}
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Kidney {ECO:0000313|EMBL:JAO00634.1};
RA Bens M., Sahm A., Jahn N., Morhart M., Holtze S., Hildebrandt T.B.,
RA Platzer M., Szafranski K.;
RT "FRAMA: From RNA-seq data to annotated mRNA assemblies.";
RL Submitted (OCT-2015) 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; JH169933; EHB08010.1; -; Genomic_DNA.
DR EMBL; GEBF01002999; JAO00634.1; -; Transcribed_RNA.
DR RefSeq; XP_004860035.1; XM_004859978.2.
DR RefSeq; XP_004860036.1; XM_004859979.2.
DR RefSeq; XP_004860038.1; XM_004859981.2.
DR RefSeq; XP_012933312.1; XM_013077858.1.
DR AlphaFoldDB; G5BFE9; -.
DR STRING; 10181.G5BFE9; -.
DR GeneID; 101722260; -.
DR KEGG; hgl:101722260; -.
DR CTD; 9317; -.
DR eggNOG; ENOG502QQQR; Eukaryota.
DR InParanoid; G5BFE9; -.
DR OMA; MVKCGFI; -.
DR OrthoDB; 5387837at2759; -.
DR Proteomes; UP000006813; Unassembled WGS sequence.
DR Bgee; ENSHGLG00000008340; Expressed in adult mammalian kidney and 10 other cell types or tissues.
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 Metal-binding {ECO:0000256|PIRSR:PIRSR601559-52};
KW Reference proteome {ECO:0000313|Proteomes:UP000006813}.
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"
SQ SEQUENCE 349 AA; 39173 MW; 869574BE48282093 CRC64;
MSFLSGKVQT VLGLVDPSKL GRTLTHEHLT MTFDCNYYPP PPCHEVTSKE PILMKNLFWI
QQNPYSHKEN LQLHQETAAI KEELLYFKAK GGGAVVENTT TGICRDVQTL KWLAEQTGVH
VIAGAGFYVG ATHSSETRAM SVEQLTEVLT KEILHGADGT TIKCGVIGEI GCSWPLTESE
RKVLQATAHA QEQLGCPVIV HPGQSPSAPF QIIRALQEAG ADISKTVMSH LDRSILDKKE
LLEFAQLGCY LEYDLFGNKF LNYQFNPNID MPDDNKRIRR VRLLVEEGYG DRILMAHDIH
TKHRLMKYGG HGYSHILTNI VPKMLLRGIT EAALDKILIE NPKRWLTFK
//
