ID Q49UB9_TRYCR Unreviewed; 918 AA.
AC Q49UB9;
DT 13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 13-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=C3747_204g30 {ECO:0000313|EMBL:PWV00883.1};
OS Trypanosoma cruzi.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma; Schizotrypanum.
OX NCBI_TaxID=5693 {ECO:0000313|EMBL:AAM28249.1};
RN [1] {ECO:0000313|EMBL:AAM28249.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Brener {ECO:0000313|EMBL:AAM28249.1};
RX PubMed=16776650; DOI=10.1042/BJ20060757;
RA Diaz-Benjumea R., Laxman S., Hinds T.R., Beavo J.A., Rascon A.;
RT "Characterization of a novel cAMP-binding, cAMP-specific cyclic nucleotide
RT phosphodiesterase (TcrPDEB1) from Trypanosoma cruzi.";
RL Biochem. J. 399:305-314(2006).
RN [2] {ECO:0000313|EMBL:PWV00883.1, ECO:0000313|Proteomes:UP000246078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCC {ECO:0000313|EMBL:PWV00883.1,
RC ECO:0000313|Proteomes:UP000246078};
RX PubMed=29708484;
RA Berna L., Rodriguez M., Chiribao M.L., Parodi-Talice A., Pita S., Rijo G.,
RA Alvarez-Valin F., Robello C.;
RT "Expanding an expanded genome: long-read sequencing of Trypanosoma cruzi.";
RL Microb. Genom. 0:0-0(2018).
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 ---------------------------------------------------------------------------
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; AY099403; AAM28249.1; -; Genomic_DNA.
DR EMBL; PRFC01000204; PWV00883.1; -; Genomic_DNA.
DR AlphaFoldDB; Q49UB9; -.
DR SMR; Q49UB9; -.
DR VEuPathDB; TriTrypDB:BCY84_02099; -.
DR VEuPathDB; TriTrypDB:C3747_204g30; -.
DR VEuPathDB; TriTrypDB:C4B63_26g201; -.
DR VEuPathDB; TriTrypDB:ECC02_004700; -.
DR VEuPathDB; TriTrypDB:Tc_MARK_5774; -.
DR VEuPathDB; TriTrypDB:TcBrA4_0119400; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM04784; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM04786; -.
DR VEuPathDB; TriTrypDB:TcCL_ESM04787; -.
DR VEuPathDB; TriTrypDB:TcCLB.508277.100; -.
DR VEuPathDB; TriTrypDB:TcCLB.509943.20; -.
DR VEuPathDB; TriTrypDB:TCDM_05304; -.
DR VEuPathDB; TriTrypDB:TcG_04573; -.
DR VEuPathDB; TriTrypDB:TCSYLVIO_007026; -.
DR BRENDA; 3.1.4.53; 6524.
DR Proteomes; UP000246078; 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; 3.
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}.
FT DOMAIN 590..918
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 669
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 669..673
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 673
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 709
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 710
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 710
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 822
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 822
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 874
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 918 AA; 102484 MW; C363F86C761534B4 CRC64;
MFTQQRLRPN TQELLKETNH LCEAFAISES ILARYQRNNR QLSESEKKAF ASLLLRVPHD
FLTETVASLG TSKTSSIGPT TDLGSLIDNV FGFGKPLKDV FQLLNQELGN CLNSPRCRVY
YLDPTDNLLK DPVYATASTL DETTPLGKAV LTGIQREIAG TLYLPLSFEG KVIACVESAW
GSPEKGDKRR IKETLQFVAC AMHNAIESER LRWNKEKAEA MLEMATQLAR DNLDEAVLAN
SIMNTAKVLT ESDRCSIFLV KDDTLEAHFE DGNIVAIPIA TGIAGYVAQT GQTVKISDAY
SDDRFNREVD KATGYRTKTI LCMPVTYEGS IVAVAQLINK LDMVTESGLR LPRTFGKRDE
ELFQTFSMFA GASLRNCRIN EKLINEKRKS DAILDVVTLL SNTDIRDVDG IVRHVLHGAK
RLLYADRSAL FLVDKERNEL YSRIADSVAG KEIRFPCGQG IAGIVASTGI GENILDAYQD
PRFNREVDKQ LGYRTQALLC EPIVLNGEIL AVVQLVNKLN EAGEVTVFTE SDRETFRVFS
LFAGISINNS HLLEFAVKAG REMMELNENR ALAGGRTGSL RNIKRPLAIT EAERQAVRDI
NLAHLDITSI DFDLFYLREN MELPLDAAAA VAYRLIVGTG LPQKFRCRDD TLLNFILQCR
KKYRNVPYHN FYHVVDVCQT VYTFLYKGAV CEKLTELDCF VLLVTALVHD LDHMGLNNSF
YLKTDSPLGI LSSASGNASV LEVHHCNLAV EILSDPDSDV FEGLDAADRT LAYRSMIDCV
LATDMAKHGK SLESFLSVLG NPETSEQRIA ELTMQIVLKA GDVSNVTKPF DISRLWAMAV
TEEFYRQGDM EKEKGVEVLP MFDRSKNTEL AKGQIGFIDF VAGPFFKKIV SASLTGMQWT
VERVESNRLE WQRSLDAK
//
