ID A0DIM1_PARTE Unreviewed; 779 AA.
AC A0DIM1;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=GSPATT00017245001 {ECO:0000313|EMBL:CAK82888.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK82888.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK82888.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK82888.1,
RC ECO:0000313|Proteomes:UP000000600};
RX PubMed=17086204; DOI=10.1038/nature05230;
RG Genoscope;
RA Aury J.-M., Jaillon O., Duret L., Noel B., Jubin C., Porcel B.M.,
RA Segurens B., Daubin V., Anthouard V., Aiach N., Arnaiz O., Billaut A.,
RA Beisson J., Blanc I., Bouhouche K., Camara F., Duharcourt S., Guigo R.,
RA Gogendeau D., Katinka M., Keller A.-M., Kissmehl R., Klotz C., Koll F.,
RA Le Moue A., Lepere C., Malinsky S., Nowacki M., Nowak J.K., Plattner H.,
RA Poulain J., Ruiz F., Serrano V., Zagulski M., Dessen P., Betermier M.,
RA Weissenbach J., Scarpelli C., Schachter V., Sperling L., Meyer E.,
RA Cohen J., Wincker P.;
RT "Global trends of whole-genome duplications revealed by the ciliate
RT Paramecium tetraurelia.";
RL Nature 444:171-178(2006).
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}.
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DR EMBL; CT868452; CAK82888.1; -; Genomic_DNA.
DR RefSeq; XP_001450285.1; XM_001450248.1.
DR AlphaFoldDB; A0DIM1; -.
DR STRING; 5888.A0DIM1; -.
DR EnsemblProtists; CAK82888; CAK82888; GSPATT00017245001.
DR GeneID; 5036070; -.
DR KEGG; ptm:GSPATT00017245001; -.
DR eggNOG; KOG3688; Eukaryota.
DR HOGENOM; CLU_020154_0_0_1; -.
DR InParanoid; A0DIM1; -.
DR Proteomes; UP000000600; Partially assembled WGS sequence.
DR GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
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 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:UP000000600}.
FT DOMAIN 446..779
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 528
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 532
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 569
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 682
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
SQ SEQUENCE 779 AA; 91662 MW; BA3F171D32EF10CD CRC64;
MQLMSENCLE FLQQIADLIL GSPAFTVIYE INKKVNGMST HIKEFENAYQ KLLKFKESTN
VNGSELDNLF GTNELYVYKN KYSYLIYDVK DVPFKAFPDY RLILDQFISL AYDFQKEIYD
KENLVSIIRG IKSRFIKNST RICQEIIRSQ VTEVLSSQCW IEMPDQIQYM NDLIIDQHGY
VVLPVKLDKK IKYYIKIESP NIDMITFSDY IQQLWQRLTY QLKDLKNEEF LKQMLEVNSP
NKLYIQLDGD RNIRYQSCCI PDSWYFMLIK GGSLEDLQLE QVNKQSLIQK MQELKSSVKG
AVSVCQICFS DKAVDVDLFA KRNEEDEITD YYIVFNAPKK KFEDDHRISA QMSSESKLQE
LSKAALINIK MEKLSKACIV MREYLKVNLS DEEIIDLLKE KDILKEVYNQ QSITDDIRSS
YVMEYYKAES IKDIKNPVQR SQQYIIETEL TNIKKFDLYT LDANDISNLS DYSFDITVVQ
DKHEQLRYTW ALFHLCNFID LYQINKEVFY QFTVIVQEKY SYRQNPFHNY DHGFTVAHAC
YYIIKSKSMN QYFDKFIQFT ALLSALCHDI DHTGRNNHFE SQKLSKLALR YNDESVLENH
HASVMFKILQ KEKYNILSSL SQDQCQIFRK YAIANILGTD MKKHFEIVKL LELKLSKLPD
EPFIQKEEDK KFLSSAIVHT CDLTMQSKTF KMAQKWSNRI ATEFSDQVAE EKQLSLPITQ
HFLPLGTPNF NQLLAKQEIS FIKFIVKPAY DLTAQVLQTG LEVPLKNLED NLKEWENQK
//
