ID   A0A0R3R5R2_9BILA        Unreviewed;       196 AA.
AC   A0A0R3R5R2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=3',5'-cyclic-nucleotide phosphodiesterase {ECO:0000313|WBParaSite:BTMF_0001535601-mRNA-1};
GN   ORFNames=BTMF_LOCUS13348 {ECO:0000313|EMBL:VDO45521.1};
OS   Brugia timori.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Brugia.
OX   NCBI_TaxID=42155 {ECO:0000313|Proteomes:UP000050602, ECO:0000313|WBParaSite:BTMF_0001535601-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:BTMF_0001535601-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
RN   [2] {ECO:0000313|EMBL:VDO45521.1, ECO:0000313|Proteomes:UP000280834}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG   Pathogen Informatics;
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the cyclic nucleotide phosphodiesterase family.
CC       {ECO:0000256|ARBA:ARBA00007648}.
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DR   EMBL; UZAG01020013; VDO45521.1; -; Genomic_DNA.
DR   STRING; 42155.A0A0R3R5R2; -.
DR   WBParaSite; BTMF_0001535601-mRNA-1; BTMF_0001535601-mRNA-1; BTMF_0001535601.
DR   Proteomes; UP000050602; Unplaced.
DR   Proteomes; UP000280834; Unassembled WGS sequence.
DR   GO; GO:0004114; F:3',5'-cyclic-nucleotide phosphodiesterase activity; IEA:UniProtKB-EC.
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; IPR023088; PDEase.
DR   InterPro; IPR002073; PDEase_catalytic_dom.
DR   InterPro; IPR036971; PDEase_catalytic_dom_sf.
DR   InterPro; IPR023174; PDEase_CS.
DR   PANTHER; PTHR11347:SF219; CAMP-SPECIFIC 3',5'-CYCLIC PHOSPHODIESTERASE, ISOFORM I; 1.
DR   PANTHER; PTHR11347; CYCLIC NUCLEOTIDE PHOSPHODIESTERASE; 1.
DR   Pfam; PF00233; PDEase_I; 1.
DR   PRINTS; PR00387; PDIESTERASE1.
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};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR623088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280834}.
FT   DOMAIN          1..196
FT                   /note="PDEase"
FT                   /evidence="ECO:0000259|PROSITE:PS51845"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         19
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
SQ   SEQUENCE   196 AA;  22494 MW;  5C85341DD157A121 CRC64;
     NVFSELEVLA SIFAGAIHDV DHPGFTNHYL INTNSELAIM YNDESVLEQH HLAVAFKLLQ
     DSNCNFIVSL NKKQRQLFRK LTIEMVLATD MSKHMSILAD LKTMVEAKKV AGSSVLTLDK
     TDRIQVMQTM IHLADLSNPT KPIDLYSIWV KNIMEEYWRQ GDRERDLGID ISPMCDRNNI
     TIAKSQVVTK NYYIYQ
//