ID   A0A158RAB4_TAEAS        Unreviewed;       881 AA.
AC   A0A158RAB4;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE            EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN   ORFNames=TASK_LOCUS8900 {ECO:0000313|EMBL:VDK41239.1};
OS   Taenia asiatica (Asian tapeworm).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Cestoda;
OC   Eucestoda; Cyclophyllidea; Taeniidae; Taenia.
OX   NCBI_TaxID=60517 {ECO:0000313|Proteomes:UP000046400, ECO:0000313|WBParaSite:TASK_0000889901-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:TASK_0000889901-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (APR-2016) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDK41239.1, ECO:0000313|Proteomes:UP000282613}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Purine metabolism; 3',5'-cyclic GMP degradation; GMP from
CC       3',5'-cyclic GMP: step 1/1. {ECO:0000256|ARBA:ARBA00037913}.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       {ECO:0000256|RuleBase:RU363067}.
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DR   EMBL; UYRS01018923; VDK41239.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A158RAB4; -.
DR   STRING; 60517.A0A158RAB4; -.
DR   WBParaSite; TASK_0000889901-mRNA-1; TASK_0000889901-mRNA-1; TASK_0000889901.
DR   Proteomes; UP000046400; Unplaced.
DR   Proteomes; UP000282613; 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   Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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; PF00233; PDEase_I; 1.
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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363067};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU363067};
KW   Reference proteome {ECO:0000313|Proteomes:UP000282613}.
FT   DOMAIN          258..682
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   REGION          723..749
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          763..804
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          846..881
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        723..739
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        783..804
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..867
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   881 AA;  96796 MW;  BEC0D78DC180594C CRC64;
     MVDESWLFDL SKELEKRLGE TFQPQHLHQA PPPNRFRATQ FEEALRRFRE SLSVRQGKFS
     VPFVSTTSHS SCSSASSHST DTEIISGRGY PFNDLSSYIP SLQPLLSNLA DLRKELASLH
     HDHYEYQCKQ YRQACQNDSS STAIGGSAAA PTTTAAAAAV SVPISRRRPV TASDPVTGAT
     AAAASFLVGV ECALASCDVD LPGMRTAPPP HPSLGTIRQS REACWTVWNE YYHTRHQPLS
     ADLRKQLRQP TFNNWPYTDA QLLRFVRYFF TGDADSTSSI PSSQCGSTMA GPETEVEVVV
     DDRLRLAQRC DIPEEILDAW LCAVYAKYNH VSFHNFKHAF MVAQMVGSVS FSFALYMVLK
     GGETDSTEFN YHMEGSLDKA TVESRFESAH DRLIHSVMYT SIWCADLASL FCHLDLFTLL
     FAAICHDLDH PGLTNAYQVG ETDCPLHENN ILFWCLQNNA HSRLSICYNS LSPLENHHCA
     VAFELIRTPA TNIFVNFSAK EMEIVRENAV QCILGTDMAK HTDILEAFTA KMLEHSIEAA
     TVAIHDVSES ASSAAINGAA PTTAQLVGIF DEDDESHALT MVVLLKMCDI STEIRPVEVA
     RPWLMGLINE LTNQRDLERK SNLTLSPVMD ESNMVDCQIN FLSYVMLPLA KSLISIIPAL
     ESCFLTPTKD QLAYYHRLAA EQATLSLSVE DTVLEQDEDQ YIYDENSVEG VRFGDGSVEL
     SHAKSTIGTE GEESNGTPPT SPSLPIPSTN VTVATAQPHQ PLHLSISASN PDREPLGHAL
     HHNYGHTSSS SGVGSGDSQQ PKRTSIVSSA GLIAAELTPP HRPLRRSLGE LPWSAHALLL
     THFEDTYHLA PPPPPPPPPP PPPRSSRPMA MGGMMGPKPS S
//