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PTER_DROPS
ID   PTER_DROPS              Reviewed;         350 AA.
AC   Q29BL3;
DT   03-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Phosphotriesterase-related protein;
DE            EC=3.1.-.-;
DE   AltName: Full=Parathion hydrolase-related protein;
GN   ORFNames=GA14949;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
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; CM000070; EAL26984.1; -; Genomic_DNA.
DR   RefSeq; XP_001357849.1; XM_001357812.2.
DR   AlphaFoldDB; Q29BL3; -.
DR   SMR; Q29BL3; -.
DR   STRING; 7237.FBpp0282770; -.
DR   EnsemblMetazoa; FBtr0284332; FBpp0282770; FBgn0074975.
DR   GeneID; 4800604; -.
DR   KEGG; dpo:Dpse_GA14949; -.
DR   eggNOG; ENOG502QQQR; Eukaryota.
DR   HOGENOM; CLU_054760_0_1_1; -.
DR   InParanoid; Q29BL3; -.
DR   OMA; MVKCGFI; -.
DR   PhylomeDB; Q29BL3; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Bgee; FBgn0074975; Expressed in female reproductive system and 3 other 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   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_0000388678"
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;  39490 MW;  49359AA20CB21248 CRC64;
     MTAVETVLGS ITPNLLGRTL THEHVALDFE HFYRPPPADF ESELKAKISM STLGYVRLYP
     YSSKENVRFY DEEALEAAKK DVLLYKKHGG GSIVENSSYG LKRNLEFIVE LAKSTGVHFI
     AGTGHYIHAV QDASHASLTV EQMSDLYTKD ILTGIEIKGK MVKCGFIGEV ASVYPIHEFE
     KNSIKATGEI QEVLGCGVSF HPHRDAQAPF DIMRLYLEAG GRAQKCVMSH LDRTLFKIEE
     LVELSELGCY LQYDLFGTEC SYYQLNTNVD MISDGQRIEN LMKLIEEGLL DRLLMSHDIH
     TKHRLTSYGG HGYHHIHTNI LPRMFARGVT LEQVEQMTVT NPANWLSFDP
 
 
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