ID S9V2S5_9TRYP Unreviewed; 819 AA.
AC S9V2S5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=STCU_08654 {ECO:0000313|EMBL:EPY21201.1};
OS Strigomonas culicis.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Strigomonadinae; Strigomonas.
OX NCBI_TaxID=28005 {ECO:0000313|EMBL:EPY21201.1, ECO:0000313|Proteomes:UP000015354};
RN [1] {ECO:0000313|EMBL:EPY21201.1, ECO:0000313|Proteomes:UP000015354}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23560078;
RA Motta M.C., Martins A.C., de Souza S.S., Catta-Preta C.M., Silva R.,
RA Klein C.C., de Almeida L.G., de Lima Cunha O., Ciapina L.P., Brocchi M.,
RA Colabardini A.C., de Araujo Lima B., Machado C.R., de Almeida Soares C.M.,
RA Probst C.M., de Menezes C.B., Thompson C.E., Bartholomeu D.C., Gradia D.F.,
RA Pavoni D.P., Grisard E.C., Fantinatti-Garboggini F., Marchini F.K.,
RA Rodrigues-Luiz G.F., Wagner G., Goldman G.H., Fietto J.L., Elias M.C.,
RA Goldman M.H., Sagot M.F., Pereira M., Stoco P.H., de Mendonca-Neto R.P.,
RA Teixeira S.M., Maciel T.E., de Oliveira Mendes T.A., Urmenyi T.P.,
RA de Souza W., Schenkman S., de Vasconcelos A.T.;
RT "Predicting the Proteins of Angomonas deanei, Strigomonas culicis and Their
RT Respective Endosymbionts Reveals New Aspects of the Trypanosomatidae
RT Family.";
RL PLoS ONE 8:E60209-E60209(2013).
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|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:EPY21201.1}.
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DR EMBL; ATMH01008654; EPY21201.1; -; Genomic_DNA.
DR AlphaFoldDB; S9V2S5; -.
DR EnsemblProtists; EPY21201; EPY21201; STCU_08654.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000015354; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.30.450.40; -; 2.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
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; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SUPFAM; SSF55781; GAF domain-like; 2.
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 cGMP {ECO:0000256|ARBA:ARBA00022535};
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000015354};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 645..819
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 725
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 729
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 765
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 766
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 766
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
SQ SEQUENCE 819 AA; 91351 MW; 4C32CFE7C60F894B CRC64;
MLYYPHFHFL FSILFLSVII VFLGINLYRY KKREHDQQKD KISRARTMAF TVQNKGPKYG
ETNHLCAAFA LCQSIVSRYK RTGTDFTPAE AKAIENLVKT LPISNASAAC APLSISTRST
DNLSFLDDAV GASSTDTDIT RILSIVKNCG DVTTDIKKVL EALNREIALA LGTSYVRTYI
LNKNDNVLLD ALTGIAASLN EGTALGKSAS MTSTYTIAKT LYIPLRVDSE FVGCIEAPQG
RRQNGTYFET LIRVAAITTK NITTSRNQLW ETQKAEAMLN MATRLARDAL DESVLIQSIM
NTAKVLTESD RCSMFIVKDN DTLEAHFEDG NVVSIPSGTG IAGYVARTGD VVNIPNAYED
ERFNRDVDKA TGYHTKTILC LPVRYEGTTV AVAQLINKQD LVTDTELHLP RVFGKRDEEL
FETFSMFAGA SLRNCHINDN LVIEKKKSDA ILDVVTLLSN TDIRDVNGIV RHVLHGAKKL
LSADRSSLFL LDKERNELYS RMADSVSGNE IRFPSGQGIA GTVAASGTGE NIPDAYRDPR
FNSSVDKQLG YRTQSILCEP IILNGEVLAV VQLVNKINSD GTIGRFTKKD QNTFKVFSLF
AGISINNSHL LEFAVNAGRE AMELNEYRNN VTVTKTGKTK LLSISKVERN AVLSIMFDEK
YDFTSTKFNL FDVREYCSSP LNAAAALIYK LLLSTGLPQK FGCRDATLLN FILQCRKKYR
FVPYHNFFHV VDVCQTLHTF LFTGNACEFL TDLECYVLLI TALVHDLDHM GVNNSFNVKT
DAPLVFVKCE RQQLRRWRCT TAPSRLRSSP TPTRMFLEV
//
