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Database: UniProt
Entry: Q4RQ45_TETNG
LinkDB: Q4RQ45_TETNG
Original site: Q4RQ45_TETNG 
ID   Q4RQ45_TETNG            Unreviewed;       754 AA.
AC   Q4RQ45;
DT   19-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   19-JUL-2005, sequence version 1.
DT   22-FEB-2023, entry version 72.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
DE   Flags: Fragment;
GN   ORFNames=GSTENG00030776001 {ECO:0000313|EMBL:CAG09487.1};
OS   Tetraodon nigroviridis (Spotted green pufferfish) (Chelonodon
OS   nigroviridis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Eupercaria; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Tetraodon.
OX   NCBI_TaxID=99883 {ECO:0000313|EMBL:CAG09487.1};
RN   [1] {ECO:0000313|EMBL:CAG09487.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15496914; DOI=10.1038/nature03025;
RA   Jaillon O., Aury J.-M., Brunet F., Petit J.-L., Stange-Thomann N.,
RA   Mauceli E., Bouneau L., Fischer C., Ozouf-Costaz C., Bernot A., Nicaud S.,
RA   Jaffe D., Fisher S., Lutfalla G., Dossat C., Segurens B., Dasilva C.,
RA   Salanoubat M., Levy M., Boudet N., Castellano S., Anthouard V., Jubin C.,
RA   Castelli V., Katinka M., Vacherie B., Biemont C., Skalli Z., Cattolico L.,
RA   Poulain J., De Berardinis V., Cruaud C., Duprat S., Brottier P.,
RA   Coutanceau J.-P., Gouzy J., Parra G., Lardier G., Chapple C.,
RA   McKernan K.J., McEwan P., Bosak S., Kellis M., Volff J.-N., Guigo R.,
RA   Zody M.C., Mesirov J., Lindblad-Toh K., Birren B., Nusbaum C., Kahn D.,
RA   Robinson-Rechavi M., Laudet V., Schachter V., Quetier F., Saurin W.,
RA   Scarpelli C., Wincker P., Lander E.S., Weissenbach J., Roest Crollius H.;
RT   "Genome duplication in the teleost fish Tetraodon nigroviridis reveals the
RT   early vertebrate proto-karyotype.";
RL   Nature 431:946-957(2004).
RN   [2] {ECO:0000313|EMBL:CAG09487.1}
RP   NUCLEOTIDE SEQUENCE.
RG   Genoscope;
RG   Whitehead Institute Centre for Genome Research;
RL   Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|RuleBase:RU363067};
CC       Note=Binds 2 divalent metal cations per subunit. Site 1 may
CC       preferentially bind zinc ions, while site 2 has a preference for
CC       magnesium and/or manganese ions. {ECO:0000256|RuleBase:RU363067};
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       {ECO:0000256|RuleBase:RU363067}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CAG09487.1}.
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DR   EMBL; CAAE01015006; CAG09487.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4RQ45; -.
DR   KEGG; tng:GSTEN00030776G001; -.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347:SF111; CAMP AND CAMP-INHIBITED CGMP 3',5'-CYCLIC PHOSPHODIESTERASE 10A; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF01590; GAF; 2.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS00126; PDEASE_I_1; 1.
DR   PROSITE; PS51845; PDEASE_I_2; 1.
PE   3: Inferred from homology;
KW   cGMP {ECO:0000256|ARBA:ARBA00022535};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR623088-3}.
FT   DOMAIN          436..753
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   ACT_SITE        509
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT   BINDING         509..513
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         513
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         547
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         548
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         548
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         548
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         658
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   BINDING         658
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         710
FT                   /ligand="AMP"
FT                   /ligand_id="ChEBI:CHEBI:456215"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAG09487.1"
FT   NON_TER         754
FT                   /evidence="ECO:0000313|EMBL:CAG09487.1"
SQ   SEQUENCE   754 AA;  85195 MW;  C52A532632B75260 CRC64;
     FNSAGLTDEK VKAYLSLHPQ MLDDFVLESV STETLDRWLK KKTSGSPADD ASVKEVSRQY
     QDTNMQGVVY ELNSYMEQRL DTGGDNKLLL YELCNIIKTA TKADGFALYF LGESNNSLCL
     FTPTGAKDGP PSLIPSGPIA CGTTIAAHVA KTRRTLLVED ITGDERFPDG TGQDSGIHVH
     SVLCLPILTA SGDIIAVLEL HRHRGKEPFN LSHQEVATAN LAWASVAIHQ VQVCRGLAKQ
     TELNDFLLDV SKTYFDNIVA IDSLLEHIMI YAKNLVNADR CALFQVDHNN KELYSDLFDI
     GEEKEGRPVF KKTKEIRFSI EKGIAGQVAQ TGEVLNIPDA YADPRFNREV DLKTGYTTRN
     ILCMPIVSRG TVIGVVQMVN KLSGSAFTKT DENNFKMFAV FCALALHCAN MYHRIRQSEC
     IYRVTMEKLS YHSICTSEEW KTLTQLNLPA PIYKEIEMFH FDINPFEEIW PAVFIYMVHN
     SCGKSSFELE KLCRFTMSVR KNYRRVPYHN WKHAVTVAHC MYAILQKTSG IFTEMEKKGL
     LIACLCHDLD HRGYSNSYLQ KFDHPLAALY STSTMEQHHF SQTVSILQLE GHNIFSNLNS
     SEYEQVLEII RKAIIATDLA LYFNNHQQLT ELLSSEALDL NNYSHRDRVI GLMMTACDLC
     SVTKKWQITR LTANDIYAEF WAEGDEMKKI GLQPIPMMDR DKKDEVPQGQ VGFYNSVAIP
     CYTTLAKLFP PSNPLLKACK ENLSMWEKIA CGEV
//
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