ID A0A151L5X0_PLARE Unreviewed; 815 AA. AC A0A151L5X0; DT 08-JUN-2016, integrated into UniProtKB/TrEMBL. DT 08-JUN-2016, sequence version 1. DT 02-OCT-2024, entry version 27. DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067}; DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067}; GN ORFNames=PRSY57_1469700 {ECO:0000313|EMBL:KYN94355.1}; OS Plasmodium reichenowi. OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida; OC Plasmodiidae; Plasmodium; Plasmodium (Laverania). OX NCBI_TaxID=5854 {ECO:0000313|EMBL:KYN94355.1, ECO:0000313|Proteomes:UP000076359}; RN [1] {ECO:0000313|EMBL:KYN94355.1, ECO:0000313|Proteomes:UP000076359} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=SY57 {ECO:0000313|EMBL:KYN94355.1, RC ECO:0000313|Proteomes:UP000076359}; RX PubMed=27002652; DOI=10.1038/ncomms11078; RA Sundararaman S.A., Plenderleith L.J., Liu W., Loy D.E., Learn G.H., Li Y., RA Shaw K.S., Ayouba A., Peeters M., Speede S., Shaw G.M., Bushman F.D., RA Brisson D., Rayner J.C., Sharp P.M., Hahn B.H.; RT "Genomes of cryptic chimpanzee Plasmodium species reveal key evolutionary RT events leading to human malaria."; RL Nat. Commun. 7:11078-11078(2016). 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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi- CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. 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:KYN94355.1}. 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; LVLA01000015; KYN94355.1; -; Genomic_DNA. DR RefSeq; XP_019970030.1; XM_020115373.1. DR AlphaFoldDB; A0A151L5X0; -. DR EnsemblProtists; KYN94355; KYN94355; PRSY57_1469700. DR GeneID; 24533958; -. DR KEGG; prei:PRSY57_1469700; -. DR VEuPathDB; PlasmoDB:PRCDC_1469700; -. DR VEuPathDB; PlasmoDB:PRG01_1470400; -. DR OrthoDB; 5479253at2759; -. DR Proteomes; UP000076359; Chromosome 14. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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; 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:SF198; CAMP-SPECIFIC 3',5'-CAMP PHOSPHODIESTERASE 4; 1. DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1. DR Pfam; PF00233; PDEase_I; 1. DR PRINTS; PR00387; PDIESTERASE1. 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 Coiled coil {ECO:0000256|SAM:Coils}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067}; KW Membrane {ECO:0000256|SAM:Phobius}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, KW ECO:0000256|PIRSR:PIRSR623088-3}; Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 56..77 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 89..111 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 123..141 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 162..181 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 187..204 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT TRANSMEM 216..235 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 384..744 FT /note="PDEase" FT /evidence="ECO:0000259|PROSITE:PS51845" FT COILED 1..29 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 459 FT /note="Proton donor" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1" FT BINDING 463 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 499 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 500 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 500 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" FT BINDING 616 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3" SQ SEQUENCE 815 AA; 97114 MW; 566E0C2B95341676 CRC64; MNEYNNDNME QEKEKKKEEE KYKNIIKKEY FIFPRLYDKN KEIEYNKLRI HNIKEYICIH LTISLFIILI ECFVFSFNLN IKDTTYVEIC VVIFSILNCL MHIVVLIKMY FFTSESVYTK GVFIGYIVLN QVFQFLSLYF FTKRNEQNKN DIAHLKYYDN SFNLYVHFFV DSVFILCLPT LSFCLSVLFV MMFLCLNILL INMIKFNKIS YGGDIYYIGL LSVVLLMFFI LRYMMEERNR LLFFFLKDMM FDNYKKWYCD YIGAHYDKDK DSTTVNGENN RYEKEKCEDY KFLFFNKCIL FHDFTMNACY KDYYSMICFL NKLLKSCNIK GDMVSNTSVN INGDTYQNMN CHDNISSNIP KNYNSFYEEL EKNLNESDIL TIAYEVEVLK NIKKINCDEI GKNWDYSFID SEYGKSTLVI LEVGYHLISP YIENNENKKK KLQLFLLLIN SMYFPNPYHN ANHGATVCHL SKCLAHITDY DSYLNNTYMI CYLIASIAHD VGHPGKTNSY LSETNHILSI RYNDMSILEN YHCSITFSIL QLIGFDFLIN NEDTKLVEKN NYTNMRKFII ELIISTDMKL HFEYVDIFKK RKKSQNFDIS DTDAINLGTI NIKLADIGHT CLKWKDHAKW TMLVSEEFFS QKRVEELHKN KNIDPLNFSN FGREDNIDEG MIFNYENIYI NYINNINNIN TYDYSYIKLN FIHHHDFVKS IPSTQVYFFE IIVMPLIKEL QSMEKSKKEI TQKVLHNLNI NLQTWRLIEN NINLFYNTEK MTGTDYYKNL EKQKLLRGIR LLDIAEEDVI SLTKNFKEEI KHAKS //