ID A0A164VYR7_9CRUS Unreviewed; 629 AA.
AC A0A164VYR7;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Phosphodiesterase {ECO:0000256|RuleBase:RU363067};
DE EC=3.1.4.- {ECO:0000256|RuleBase:RU363067};
GN ORFNames=APZ42_022009 {ECO:0000313|EMBL:KZS12790.1};
OS Daphnia magna.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Branchiopoda;
OC Diplostraca; Cladocera; Anomopoda; Daphniidae; Daphnia.
OX NCBI_TaxID=35525 {ECO:0000313|EMBL:KZS12790.1, ECO:0000313|Proteomes:UP000076858};
RN [1] {ECO:0000313|EMBL:KZS12790.1, ECO:0000313|Proteomes:UP000076858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xinb3 {ECO:0000313|EMBL:KZS12790.1,
RC ECO:0000313|Proteomes:UP000076858};
RC TISSUE=Complete organism {ECO:0000313|EMBL:KZS12790.1};
RA Gilbert D.G., Choi J.-H., Mockaitis K., Colbourne J., Pfrender M.;
RT "EvidentialGene: Evidence-directed Construction of Genes on Genomes.";
RL Submitted (MAR-2016) 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 -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC {ECO:0000256|RuleBase:RU363067}.
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:KZS12790.1}.
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DR EMBL; LRGB01001348; KZS12790.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A164VYR7; -.
DR STRING; 35525.A0A164VYR7; -.
DR Proteomes; UP000076858; 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; 2.
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 InterPro; IPR013706; PDEase_N.
DR PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR PANTHER; PTHR11347:SF226; DUAL SPECIFICITY CALCIUM_CALMODULIN-DEPENDENT 3',5'-CYCLIC NUCLEOTIDE PHOSPHODIESTERASE 1; 1.
DR Pfam; PF00233; PDEase_I; 2.
DR Pfam; PF08499; PDEase_I_N; 1.
DR PRINTS; PR00387; PDIESTERASE1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS00126; PDEASE_I_1; 1.
DR PROSITE; PS51845; PDEASE_I_2; 2.
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|PIRSR:PIRSR623088-3};
KW Reference proteome {ECO:0000313|Proteomes:UP000076858}.
FT DOMAIN 295..451
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT DOMAIN 453..615
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT REGION 15..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..238
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 187..217
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..238
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 372
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 372..376
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 376
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 412
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 413
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 413
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 466
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 466
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 517
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 629 AA; 69964 MW; 11D73D2F3A51ACB7 CRC64;
MTTIVVKETL RKCPSDPARL STTTSSTSKS SLTPATKSAA AASKSSSSTS ALHLAPFSKC
VLTLDGYNYV ISKSNNTHTY RRQQLLKCLL RLLDKGEVRP EVMQKNLTLA IQVLDAVYID
EAGSPDCEDD VGDEEALWPD TNDASSPAPL TNNTSPHLLL PRLAKPCCSR ASRVGLRPAV
TSFTTCSSPT RSCSSTATTP TASTTATTAT TSKASVRRPT LFKKRRTPEE DDDLSEVRAD
AVPPEVRAWL ASTFTRQISS HRKPGEEKPK FRSVAQAIRA GILVERIYRR MSSSSFLQFP
VEVARNLKLI DEWTFDVFAL SDVSAGSPLR YLGIDLLNRY GVIHKFKIPS STLEAFLNQT
EAGYCKHRNL YHNNTHAADV AQTLHYVLYQ TGLMNWLTDL EIFAAIIAAI IHDFEHTGTT
NSFHVMSGSE TALLYNDRSV QENHHISAAF SVDKSKILSL VLHCCDVAHP SKPWLLHRHW
TDLLLEEFFR QGDHEKELGL PYSPLCDRNN TLVAESQIGF IEFIVEPTMA VMGDLLDKIL
IPIRPQSAPI RNDHRDSISE EKCDAGGEVV TVPTTPEKNK KEGANSKVSG EKIIRPWDVY
LEENKGKWKE LSVKDQQRRQ EEAKLKAED
//
