ID A0A2C9K9Q7_BIOGL Unreviewed; 866 AA.
AC A0A2C9K9Q7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN Name=106065025 {ECO:0000313|EnsemblMetazoa:BGLB016797-PA};
GN Synonyms=LOC106065025 {ECO:0000313|RefSeq:XP_055874330.1};
OS Biomphalaria glabrata (Bloodfluke planorb) (Freshwater snail).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC Heterobranchia; Euthyneura; Panpulmonata; Hygrophila; Lymnaeoidea;
OC Planorbidae; Biomphalaria.
OX NCBI_TaxID=6526 {ECO:0000313|EnsemblMetazoa:BGLB016797-PA, ECO:0000313|Proteomes:UP000076420};
RN [1] {ECO:0000313|EnsemblMetazoa:BGLB016797-PA}
RP IDENTIFICATION.
RC STRAIN=BB02 {ECO:0000313|EnsemblMetazoa:BGLB016797-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) to UniProtKB.
RN [2] {ECO:0000313|RefSeq:XP_055874330.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
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 AMP degradation; AMP from
CC 3',5'-cyclic AMP: step 1/1. {ECO:0000256|ARBA:ARBA00004703}.
CC -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC PDE8 subfamily. {ECO:0000256|ARBA:ARBA00006437}.
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DR RefSeq; XP_013079222.1; XM_013223768.1.
DR RefSeq; XP_013079223.1; XM_013223769.1.
DR RefSeq; XP_055874330.1; XM_056018355.1.
DR STRING; 6526.A0A2C9K9Q7; -.
DR EnsemblMetazoa; BGLB016797-RA; BGLB016797-PA; BGLB016797.
DR EnsemblMetazoa; BGLB016797-RB; BGLB016797-PB; BGLB016797.
DR KEGG; bgt:106065025; -.
DR VEuPathDB; VectorBase:BGLB016797; -.
DR OrthoDB; 5479253at2759; -.
DR UniPathway; UPA00762; UER00747.
DR Proteomes; UP000076420; Unassembled WGS sequence.
DR Proteomes; UP001165740; Chromosome 1.
DR GO; GO:0004115; F:3',5'-cyclic-AMP phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006198; P:cAMP catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR023088; PDEase.
DR InterPro; IPR002073; PDEase_catalytic_dom.
DR InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR InterPro; IPR023174; PDEase_CS.
DR InterPro; IPR013938; PDEase_PDE8.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF206; HIGH AFFINITY CAMP-SPECIFIC AND IBMX-INSENSITIVE 3',5'-CYCLIC PHOSPHODIESTERASE 8; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF08629; PDE8; 1.
DR Pfam; PF00233; PDEase_I; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 1.
PE 3: Inferred from homology;
KW cAMP {ECO:0000256|ARBA:ARBA00023149};
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:UP001165740}.
FT DOMAIN 275..345
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 515..859
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 81..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 591
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 591..595
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 595
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 631
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"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 632
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 765
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 765
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 817
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 866 AA; 97332 MW; B0916D4E77BEE10D CRC64;
MGCTPSIHVS QTGVVYCRES EDSNSPHPSS LNATFHAASG HSHVIRGETT VIGLAGEDHV
HSTTPAGPTL ATSTVAVTTL STTRASGRNS KRSSNASNPG GLAVSLSEAE TQTSRHSMKN
VERDVRFGPM LLNQKAMSVL LVFAKEDGQS DGFWWAAEKL GYRCTIASTS ENALETFLKY
HYDVVIVDAR MSVHNGLDAE ALCRSIKATK SSEFTVIMAV TKRCPNEHTE EPSIVPLLKA
GVTRRFEENW CLSACINELQ SLEFGEVRSA LKLQTTHALI VALENVNEAV EITNSDHEIQ
FVNHAYERLC GYSSDDILGK DSLELFRCDK NREAIETISG HMKKGKHWEG TYYTRRKSGD
TLPFHCKVTP ILGPTGSISH YVSVKSSSTD IYNQMVNGNM MSFPRRRESV VRTHSMTIEA
PITKVINIIN AAQENSPLTV AQALDKVLEI LQTSELYSPF QHQEMGANDD PMASDLVEGL
MTQNVKRKLS GHDIQRQAHQ VSHGYQHIPS TPTCSLAQIP ENIMSVLNTD TSWDFDIIQL
EKITNKRPLL HLGLTIFARF GVCEFLNISE TCLVNWLQMI ESNYHAKNHY HNSTHAADVL
HATAYFLDKE RSKEILDQLD QVSSLIAAVV HDVDHPARTN AFLINEKHHL AILYNDQAVL
ENHHASMCFR LTHKDPTADI FKNLRSDEYK TMRQSIIDQV LATDMKQHFE HLSKFTTSIT
KHLQKLEGDS VDIESHDADM NTILSDLALH ENRVLIKRMM IKCADVSNPL RPLALCKQWA
YRIAEEYCQQ TDEEKSRGLP VVMAQFDRKT LNIPKCQLAF INLFITTMFD AWDVYCDIPE
LMHHLQLNYD YWKEQEQAST HTIANS
//
