ID A0BY96_PARTE Unreviewed; 975 AA.
AC A0BY96;
DT 28-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=GSPATT00033366001 {ECO:0000313|EMBL:CAK63513.1};
OS Paramecium tetraurelia.
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Peniculida; Parameciidae; Paramecium.
OX NCBI_TaxID=5888 {ECO:0000313|EMBL:CAK63513.1, ECO:0000313|Proteomes:UP000000600};
RN [1] {ECO:0000313|EMBL:CAK63513.1, ECO:0000313|Proteomes:UP000000600}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Stock d4-2 {ECO:0000313|EMBL:CAK63513.1,
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; CT868026; CAK63513.1; -; Genomic_DNA.
DR RefSeq; XP_001430911.1; XM_001430874.1.
DR AlphaFoldDB; A0BY96; -.
DR EnsemblProtists; CAK63513; CAK63513; GSPATT00033366001.
DR GeneID; 5016695; -.
DR KEGG; ptm:GSPATT00033366001; -.
DR eggNOG; KOG3688; Eukaryota.
DR HOGENOM; CLU_006752_0_0_1; -.
DR InParanoid; A0BY96; -.
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 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 650..975
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 724
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 728
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 767
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 768
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 768
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 878
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
SQ SEQUENCE 975 AA; 115271 MW; 9C7933442A667AF7 CRC64;
MLSNPHLSNY IRFFQIISDM EQECLITQKE KHQLKVNLTL KDMQLVNMIA LNTDADDEEF
KYSIINYLRK QNQSPRQRQG QKIRCKSTGI EMSPIRLMRR NSVSKESKIT EEQLMQQIDD
LNDSLVMILS NENKCILTHP VTEKLKSILE VIQKTTISSP STTNTKTLQV DETENCKIVD
KFTQLYSDMK KHYTDYLNCH LLLMDNNLSY ETLVQSVRVF VKRLIDSDQI TYLHIREDQS
QQTYYSVEDQ YIITNDKQIY NETQLIQPNK VLLLDECNFY PALSEQFKIK LYKRNYLIKL
NNQDVFVCFH LSDQTSIISE FLALADEFDI FEDLNQLCTF LIETIKQAKI QIFTPLQLSH
MIQGIGIAFI RSSKYLFIKK CIHILQSKYQ VDIHINTGDA MSIISSPSFF YGTQKQVDFE
FKDELNVSIT INGMDLNRKA DLMVYKQLTQ SFNKYLKFIR QCYDRTTFYK FFVKSQDTLI
FEFDKLGRLI FLSRPIPLEI KKEFNIDFDP KKTKMTYQQL FQNEELLKYI ENFLQEQNIL
RDSDQQYQVF MKMEERSFKG FFIIFQQGWF KYDQKKFDLN DPSLQKELQK QIIQQETIRF
IDKLEQNNPQ ILNSVVQMFK PRSTQRQTVH YRNSILQFEP AKLGVQHKCS LRLEDLSTQC
TVPNINNFNF NILSVDEMVQ KQLVVVEILK HHNLIKEYDV PLDTLCSFLS EIEYKYNKKK
NVFHNYDHGV SVMQNIHAIL FQLHQTNNAS ILSTFNQFAL LLSGLCHDVS HTGRTNTFEI
NSLSNLAIRY HDRSVLEQHH AAKSLKLLCV PHTNILQSLK GEEFRKFRRM FISNILFTDI
TEHFNLIKNF ETKVLEQNFG SQDEDIKLLS GMIIHTSDFT GGAKQFELSK QWSFKVNKEF
EQQYELEGQL GYPQLPYMKD LQKLPVMAKQ EAGFFKFIVR PLWQSMSKYL DNRLQEQVDY
LDETIQKWEE IANSE
//
