ID U6LFD3_9EIME Unreviewed; 1362 AA.
AC U6LFD3;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=3', 5'-cyclic nucleotide phosphodiesterase domain-containing protein, putative {ECO:0000313|EMBL:CDJ47284.1};
GN ORFNames=EBH_0015320 {ECO:0000313|EMBL:CDJ47284.1};
OS Eimeria brunetti.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Eimeriidae; Eimeria.
OX NCBI_TaxID=51314 {ECO:0000313|EMBL:CDJ47284.1};
RN [1] {ECO:0000313|EMBL:CDJ47284.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ47284.1};
RA Reid A.J., Blake D., Billington K., Browne H., Dunn M., Hung S.,
RA Kawahara F., Miranda-Saavedra D., Mourier T., Nagra H., Otto T.D.,
RA Rawlings N., Sanchez A., Sanders M., Subramaniam C., Tay Y., Dear P.,
RA Doerig C., Gruber A., Parkinson J., Shirley M., Wan K.L., Berriman M.,
RA Tomley F., Pain A.;
RT "Genomic analysis of the causative agents of coccidiosis in chickens.";
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CDJ47284.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Houghton {ECO:0000313|EMBL:CDJ47284.1};
RA Aslett M.;
RL Submitted (OCT-2013) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; HG710671; CDJ47284.1; -; Genomic_DNA.
DR EnsemblProtists; CDJ47284; CDJ47284; EBH_0015320.
DR VEuPathDB; ToxoDB:EBH_0015320; -.
DR OrthoDB; 199847at2759; -.
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; -; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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; PF00233; PDEase_I; 2.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 2.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR623088-3}.
FT DOMAIN 968..1354
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 123..188
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 289..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 802..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 368..386
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..824
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 1039
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 1039..1043
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1043
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1079
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1080
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1080
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1080
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1259
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 1259
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 1311
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 1362 AA; 148705 MW; B7264D3E6E77F2FF CRC64;
MAFCFVRDVE TEQLLGTYAV RPAASPVQQA CSTASGHDNH GECVQGVSQP SSALGKHKMV
KSIHSRSAST LQRCFNALTI DAEKPHLYSE SRQCGEPSLV GVSPEAVAFL SALLAEDARA
SKPYLPPLAQ PPADNKKPSR APSRSLSRSK SFQWPSSEET AVGPSYVKLG QPPGGSNPGD
PKTGKPGDEV VLGALFPLSE LIAVSSASSV GFLVNDLKDG SGVYCYEPAR GRLSAVPAME
LSQTDQSGAP RDSPPSATAR GFLIACRIED EGARSACTAM AAGRVAYVGP ETRRPPPHPS
ASHQGAQPDG TALGSRLPSI GPVVSAGDAL KTSSLPHTAG MTHQADRRRK SNGPHGFIPL
LFSATLEQPT AEVDTTSQSP EIPTSGRGSC VSGGPHSAGA SSRRTLGSDN PLLTAQPDLG
LSVASWRAGA PDFPIERPSV DNDSHDDSSV ATSNLHCVHS DTTLGIVFCL NAKRVDAQAL
LSAIAQACAP PMALLLQQQW LRRDRFKRVL QLELHRTVFQ ETSIPIRMMQ RLLALLHAAV
GAEVAAFFIA DTQNRNFICL GGHKRATGLS LSVDHRLLGE AARQRGKTVV FNFLPQGFNG
EYDSRARFES KHAMLVPLLN TQGHVKAVVV LLNRNQCTCE RMKQIAEVAD KQCACEGHVR
ALEPLALAVD AWSAAITPCE HCSRRNVNEL SYGEFLTRPP SSFDVDCSRH FIGGHEALMR
AVQCEMQHWL GGQLTNVCMA GMSLLQPMET MVSYVMGGQQ GGNRDTRPLG AVMEQIQNFV
LRDRRKMLLS LRRCASVAVN EPTSSRAYPR AREEQGSSIS SPGQRAVKGR PIRHPLSIPA
APGMAVSASG ERKASKQISA CFEGADKDSV SAGQDSWASL PVAATVEGDV PDDPSSVKYP
EQEVRLVHSS SAPLVLYSEL RHSSTGGEEL TFAPQLAEDK TSDEMVASRH RRTASLPSLV
FSATLQKCTR PFDAIRKQLS LEPYRRLDLD IWRRTADELQ LFFFLALEEL GVMVKSEKAG
LQSFFTLIRD AYHTDNPYHN FYHAMHVSQM CWLFLTRYSC RDALTPTEQL GLMLAALAHD
VDHPGVNNCS LIEEHHPLAI VYNDKAVLEN HHAAFAASAQ SVDFRLKFVC SMMKLGLFSR
KTKNTRKFSS PRSSALSRGA SVRGGVQPFV ASSAFGHLRH HYEGEHDCAE HEDDHTFYPS
FAEVRRVLIT CILATDMELF RHHHEAMRKR GQMKRTTGDF LNNDEDHAFL VTCLIHCADI
SNPLLPERRN VQWASLIIQE FNAQVEMERH KGLPVTVFMD VRTELSRTQS QIGFLSFVVL
DQFRALADLV PGAEELVIQG EKNLDDWQAA MDILREADRR EA
//
