ID E3LN48_CAERE Unreviewed; 621 AA.
AC E3LN48;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=Cre-pde-1 {ECO:0000313|EMBL:EFP03175.1};
GN ORFNames=CRE_28571 {ECO:0000313|EMBL:EFP03175.1};
OS Caenorhabditis remanei (Caenorhabditis vulgaris).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN [1] {ECO:0000313|Proteomes:UP000008281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG Caenorhabditis remanei Sequencing Consortium;
RA Wilson R.K.;
RT "PCAP assembly of the Caenorhabditis remanei genome.";
RL Submitted (JUL-2007) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; DS268411; EFP03175.1; -; Genomic_DNA.
DR RefSeq; XP_003115040.1; XM_003114992.1.
DR AlphaFoldDB; E3LN48; -.
DR STRING; 31234.E3LN48; -.
DR EnsemblMetazoa; CRE28571.1; CRE28571.1; WBGene00056049.
DR eggNOG; KOG3688; Eukaryota.
DR HOGENOM; CLU_005940_1_3_1; -.
DR InParanoid; E3LN48; -.
DR OMA; NLHERWT; -.
DR OrthoDB; 240889at2759; -.
DR Proteomes; UP000008281; Unassembled WGS sequence.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:EnsemblMetazoa.
DR GO; GO:0047555; F:3',5'-cyclic-GMP phosphodiesterase activity; IEA:EnsemblMetazoa.
DR GO; GO:0005516; F:calmodulin binding; IEA:EnsemblMetazoa.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007635; P:chemosensory behavior; IEA:EnsemblMetazoa.
DR GO; GO:0006935; P:chemotaxis; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:0032528; P:microvillus organization; IEA:EnsemblMetazoa.
DR GO; GO:0010754; P:negative regulation of cGMP-mediated signaling; IEA:EnsemblMetazoa.
DR GO; GO:0090038; P:negative regulation of protein kinase C signaling; IEA:EnsemblMetazoa.
DR GO; GO:0007602; P:phototransduction; IEA:EnsemblMetazoa.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:EnsemblMetazoa.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IEA:EnsemblMetazoa.
DR GO; GO:0010446; P:response to alkaline pH; IEA:EnsemblMetazoa.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEA:EnsemblMetazoa.
DR GO; GO:0070482; P:response to oxygen levels; IEA:EnsemblMetazoa.
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 InterPro; IPR013706; PDEase_N.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF226; DUAL SPECIFICITY CALCIUM_CALMODULIN-DEPENDENT 3',5'-CYCLIC NUCLEOTIDE PHOSPHODIESTERASE 1; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR Pfam; PF08499; PDEase_I_N; 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:UP000008281}.
FT DOMAIN 198..591
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 520..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 585..621
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..557
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 585..611
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 275..279
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 315
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 316
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 316
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 422
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 422
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 473
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 621 AA; 70312 MW; 039C3E72280A4149 CRC64;
MRESVDKKTR QLRDKYPPPQ MFVFSAMTLP PSTSTATSAE NGFRRVDGLQ RPVSLLRKQK
EANADGNDPD GATSPSSSRK KSYDNAPALE SLEKLRYILH QLNSGQLPLE DLKRNIEYAA
LVLETAYMDE TRRICDEDDD LAEVTPETVP DEVREWLAAT FTRQNAGKKR DKPKFKSVAN
AIRTGIFFEK LFRKQQVVQC PIPPEIAELM KEVCTWSFSP FQLNEVSEGH ALKYVGFELF
NRYGFMDRFK VPLSALENYL SALEVGYSKH NNPYHNVVHA ADVTQSSHFM LSQTGLANSL
GDLELLAVLF GALIHDYEHT GHTNNFHIQS QSQFAMLYND RSVLENHHVS SCFRLMKEDD
KNILTHLTRD EYKELRNMVI EIVLATDMST HFMQIKTMKS MLSLPEGIDK NKALCLIVHA
CDISHPAKPW NLHERWTEGV LEEFFRQGDL EASMGLPYSP LCDRHTVHVA DSQIGFIDFI
VEPTMVVCGE LLVKMVSGHL DRQKHRHILQ VEPLVSLPPT DSLFPPSVDG GDDKSPSNAL
SPLPDLRNSS TSPSSIRKIP LNYAGKLDIP TPWMKFLHEN KAHWKERAAK EEEERKVKEA
AEAEAAAKQA EENKENGVTV N
//
