ID F9W751_TRYCI Unreviewed; 681 AA.
AC F9W751;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=TCIL3000_0_03910 {ECO:0000313|EMBL:CCD13013.1};
OS Trypanosoma congolense (strain IL3000).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Nannomonas.
OX NCBI_TaxID=1068625 {ECO:0000313|EMBL:CCD13013.1, ECO:0000313|Proteomes:UP000000702};
RN [1] {ECO:0000313|Proteomes:UP000000702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL3000 {ECO:0000313|Proteomes:UP000000702};
RA Jackson A.P., Berry A., Allison H.C., Burton P., Anderson J., Aslett M.,
RA Brown R., Corton N., Harris D., Hauser H., Gamble J., Gilderthorp R.,
RA McQuillan J., Quail M.A., Sanders M., Van Tonder A., Ginger M.L.,
RA Donelson J.E., Field M.C., Barry J.D., Berriman M., Hertz-Fowler C.;
RT "Divergent evolution of antigenic variation in African trypanosomes.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CCD13013.1, ECO:0000313|Proteomes:UP000000702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IL3000 {ECO:0000313|EMBL:CCD13013.1,
RC ECO:0000313|Proteomes:UP000000702};
RX PubMed=22331916; DOI=10.1073/pnas.1117313109;
RA Jackson A.P., Berry A., Aslett M., Allison H.C., Burton P.,
RA Vavrova-Anderson J., Brown R., Browne H., Corton N., Hauser H., Gamble J.,
RA Gilderthorp R., Marcello L., McQuillan J., Otto T.D., Quail M.A.,
RA Sanders M.J., van Tonder A., Ginger M.L., Field M.C., Barry J.D.,
RA Hertz-Fowler C., Berriman M.;
RT "Antigenic diversity is generated by distinct evolutionary mechanisms in
RT African trypanosome species.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:3416-3421(2012).
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:CCD13013.1}.
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DR EMBL; CAEQ01000986; CCD13013.1; -; Genomic_DNA.
DR AlphaFoldDB; F9W751; -.
DR VEuPathDB; TriTrypDB:TcIL3000_0_03910; -.
DR OMA; IHCILAT; -.
DR OrthoDB; 5479253at2759; -.
DR Proteomes; UP000000702; Unassembled WGS sequence.
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 SMART; SM00471; HDc; 1.
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 Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000000702}.
FT DOMAIN 348..676
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 427
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 427..431
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 431
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 468
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 468
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 580
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 580
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 632
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 681 AA; 76182 MW; 94652EC287590636 CRC64;
MNTVKSLTES ARCSLFLVKD DMLEAHFEDG NVVTMPRGAG IAGYVAQTGE TVNIPDAYAD
DRFNREVDKA TGYRTKTILC MPVMYEGAIV AVAQLINKLD LTTESGLRLP RVFGKRDEEL
FQTFSMFAGA SLRNCRINDR LLREKKKSDV ILDVVTMLSN TDIRDVDAIV RHALHGAKRL
LNADRSTLFL LDKERNELCS RMADSVAGKE IRFPCGQGIA GTVAASGIGE NIQDAYQDPR
FNREVDKQLG YRTQAILCEP IILNGEILAV VQLVNKLDAS GEVTVFTEDD RETFRVFSLF
AGISINNSHL FEFAVKAGRE VMELNEHRAA LFNRAAPSRS IKRIIAITDA ERDAIVQVEL
PNVDITDIDF DLFRVRDNSD RPMDAAASIA YRLLLGSGLP QKFGCSEEVL LNFILQCRKK
YRNVPYHNFY HVVDVCQTVY TFLYRGGVYQ KLTELECFVL LITALVHDLD HMGLNNSFYL
KTESPLGILS SASGNSSVLE VHHCNLAVEI LSDPESDVFG SLEGADRTLA FRSMIDCVLA
TDMAKHGSAL ESFLSFAADP SADSASFHRM TMEILLKAGD ISNVTKPFDI SRLWAMAVTE
EFYRQGDMEK ERGVEVLPMF DRSKNTELAK GQIGFIDFVA GPFFQKIVDA CLDGMMWTVE
RVRSNRAQWE RVLEKKPSFS Q
//
