ID A0A1J4L3K8_9EUKA Unreviewed; 1139 AA.
AC A0A1J4L3K8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=3'5'-cyclic nucleotide phosphodiesterase family protein {ECO:0000313|EMBL:OHT16501.1};
GN ORFNames=TRFO_41783 {ECO:0000313|EMBL:OHT16501.1};
OS Tritrichomonas foetus.
OC Eukaryota; Metamonada; Parabasalia; Tritrichomonadida; Tritrichomonadidae;
OC Tritrichomonas.
OX NCBI_TaxID=1144522 {ECO:0000313|EMBL:OHT16501.1, ECO:0000313|Proteomes:UP000179807};
RN [1] {ECO:0000313|Proteomes:UP000179807}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K {ECO:0000313|Proteomes:UP000179807};
RA Benchimol M., Almeida L.G., Vasconcelos A.T., Perreira-Neves A., Rosa I.A.,
RA Tasca T., Bogo M.R., de Souza W.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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:OHT16501.1}.
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DR EMBL; MLAK01000106; OHT16501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J4L3K8; -.
DR VEuPathDB; TrichDB:TRFO_41783; -.
DR OrthoDB; 241650at2759; -.
DR Proteomes; UP000179807; 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; -; 3.
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 PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF230; HIGH AFFINITY CGMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE 9A; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00065; GAF; 2.
DR SUPFAM; SSF55781; GAF domain-like; 3.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 4: Predicted;
KW cGMP {ECO:0000256|ARBA:ARBA00022535};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000179807}.
FT DOMAIN 811..1134
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 401..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..420
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 887
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 887..891
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 891
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 927
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 928
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 928
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1039
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1039
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1091
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1139 AA; 128638 MW; 9BC8B74BF806FA6B CRC64;
MKHYGIDPRK LEVGYSSIRA GGIPNKASSQ LKGHIGLSHE KHRSNSSLNV QKSRISPFAE
PQTAKERVNR LFDAFIKAIQ TEPLYSSLEK VSREIFMVNM ANVWFFVKDI ENYTSQSGTL
FSQSLSKAVP VDNCLLSKCI YRENVSAGQS AVTFPNLGSN NKNSNNKEKN PYENVVIIEK
PTTEASFNRD VDYQQPTMLI PVYDSDNNPF MVIQLGASNK NFGKEDENLG IYFTRKLSYY
SHFFAQPSRL KLNKIGDTHL LFTEICHKLS KLFNCRAVEF WGTDVFNTCI MKYNENAGKF
VPVGKKCGVV KELFKTNIPM INITDVTTFA SYDQEMDGKN SESALLHLMI VNSHNYAIVL
RGKSSGFFNV VDERILAYIV PLTIRLMTYV NGKDSGNFKE IAENGNGKNN NTSGNSNNNN
RAHAEFMKAE VNVDFAERLK ALLEVAEIIS GVLDIDILIP TIMEIACSLM NTERCSLFLV
DPVKQELITR FHGGLNRSIR MPLNRGIVGH TAVTGNIVNI MDAYSDPRFD KQVDLATGFK
TKTILTVPIY NNRGEIAGVT EMINKFDDQK FDEEDIKVLM AFNVFCGISL DNAKLYATSL
ELTRQLRGFV EMSTALNNTK KIHSVLQEIL ESAQSVINAT RATIFMAEEN ELIPTVSIGE
SLVHGSIFAD DIFKDKKPRI FSREEIFYKI QTFQDKPIDG LVTSKSLKAV GKHSSSTSSS
GLSRIASVLV QENNGGADGG GNENICGIPL ISSDKKILGV LELSSTGKIM PEDLKLLDCF
AVFTSVSIER SELQEIAQLG HAEVQMKQYL TQEERKSFDI PVKMRIDATH LLENNFDAVA
WDGIGHYKVL WAIVNEFNLL HEFKIPNEKW FRFVIEISET YKKVPYHNWR HAVDVCQFTS
YEIKLTKMDQ RLTKFELLGF IVAAICHDAN HDGFTNVYNE KAETPLGILY KNQSVMETHH
CTVAITVLSK EECNLFSELS GDQFKSMWTL IFQLILITDM AKHFDFLKQI SADIENGPYD
ESVPENRLKM MQLILKCGDI SNVSRPFELA DKWCDVLCEE FFRQGDLEMA HGMEYTSPLN
DREHLDKPKS QIGFYTFVCL PLYQLAAKVF PELQVNVDQV QSNLSVWKAA TEAREKKEQ
//
