ID G0MZC0_CAEBE Unreviewed; 570 AA.
AC G0MZC0;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=CAEBREN_03825 {ECO:0000313|EMBL:EGT48181.1};
OS Caenorhabditis brenneri (Nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=135651 {ECO:0000313|Proteomes:UP000008068};
RN [1] {ECO:0000313|Proteomes:UP000008068}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB2801 {ECO:0000313|Proteomes:UP000008068};
RG Caenorhabditis brenneri Sequencing and Analysis Consortium;
RA Wilson R.K.;
RL Submitted (JUL-2011) 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|ARBA:ARBA00007648, ECO:0000256|RuleBase:RU363067}.
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DR EMBL; GL379822; EGT48181.1; -; Genomic_DNA.
DR AlphaFoldDB; G0MZC0; -.
DR STRING; 135651.G0MZC0; -.
DR EnsemblMetazoa; CBN03825.1; CBN03825.1; WBGene00142550.
DR eggNOG; KOG3688; Eukaryota.
DR HOGENOM; CLU_005940_9_1_1; -.
DR InParanoid; G0MZC0; -.
DR OMA; YYLTCHP; -.
DR Proteomes; UP000008068; Unassembled WGS sequence.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-EC.
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; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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:SF179; 3',5'-CYCLIC PHOSPHODIESTERASE PDE-3-RELATED; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000008068}.
FT DOMAIN 167..522
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 115..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 526..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 248
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 248..252
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 311
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 312
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 312
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 421
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 421
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 472
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 570 AA; 64146 MW; C6CDDA445BD55041 CRC64;
MLPSRRSESH SPASRCKSAG HPLTTNGFHS IPSSASSSTH SMNRQGSVDN LIFKLLTRQK
YVAKCLGFVP ARSSVAIQTT PVVERDIVGC LNEASKPRIS NITFSTVTSA TGLPTVPAEP
NKARSSSYWK TEATPSNNNE HETPADLLRK ISVSRKESGT HVDTVVTTID GQRYDTKELD
NDPDFSETAE WAFPIFQISR KYPKTILSRL TYNIFQQAEL FRIFKVSPIK FFNFFHALEK
GYWEIPYHNR IHAADVLHGC YYLSVHPVRP QFGVVKSPDS LLPAPLPLAA SIMSQMSTLE
LMALFTAAAM HDYDHPGRTN AFLVTVEDKK AILYNDRSVL ENHHAAESWK LLNRPENHFI
ENLDPAEMKR FRYLVLEYIL ATDLKQHFEI IMTFNDRLAD MDLQVESDRL LVGKLLIKMA
DINSPTKPYG LHRQWTDRIC EEFYEQGDDE RKRGLAITPY MDRGDAQVAK LQDSFIAHVV
SPLAQAMHES GLLPILPGLE TSELMINMQH NHRKWKEEIE VETANYEPTT CNGGGVNGVI
EEESASTSDS PDPRRDSPSL DSELSQVGAD
//
