ID A0A0C2GJ68_9BILA Unreviewed; 360 AA.
AC A0A0C2GJ68;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=3'5'-cyclic nucleotide phosphodiesterase {ECO:0000313|EMBL:KIH61255.1};
GN ORFNames=ANCDUO_08479 {ECO:0000313|EMBL:KIH61255.1};
OS Ancylostoma duodenale.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Ancylostomatidae;
OC Ancylostomatinae; Ancylostoma.
OX NCBI_TaxID=51022 {ECO:0000313|EMBL:KIH61255.1, ECO:0000313|Proteomes:UP000054047};
RN [1] {ECO:0000313|EMBL:KIH61255.1, ECO:0000313|Proteomes:UP000054047}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Zhejiang {ECO:0000313|EMBL:KIH61255.1,
RC ECO:0000313|Proteomes:UP000054047};
RA Mitreva M.;
RT "Draft genome of the parsitic nematode Ancylostoma duodenale.";
RL Submitted (DEC-2013) 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; KN730280; KIH61255.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C2GJ68; -.
DR Proteomes; UP000054047; 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 CDD; cd00077; HDc; 1.
DR Gene3D; 1.10.1300.10; 3'5'-cyclic nucleotide phosphodiesterase, catalytic domain; 1.
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 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; PF00233; PDEase_I; 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; 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:UP000054047}.
FT DOMAIN 7..350
FT /note="PDEase"
FT /evidence="ECO:0000259|PROSITE:PS51845"
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-1"
FT BINDING 83..87
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 87
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 123
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 124
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 124
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 256
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
FT BINDING 256
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-3"
FT BINDING 308
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000256|PIRSR:PIRSR623088-2"
SQ SEQUENCE 360 AA; 40946 MW; 21302BB590976AC9 CRC64;
MPGPHGDRRR VSADVKNALE NDSDWTYDIL QLEKVTEHHA LTQLGFKIFD RWKVADALSC
NEDILHRWLC TIEAHYHAGN AYHNATHAAD VLQATSYFLD SPTVAAHISE NHAIAAILAA
AVHDLDHPGR GNAFLINTRQ SLAVLYNDHS VLENHHVALA FQLTLQQNSN VNIFSNLSRE
EFTSMRHAMV EMVLATDISR HFEYLVKFNK VSRLSLRGAY TLCESIEFQM NVVDVPDDAR
DGNSLTICNM LVKCADISNP TREWSLCQKW AYRIVEEYFD QTKEEREKGL PVTMEVFDRK
TCNVPLTQCG FIDMFVREAF ANFSEFANLG HLSAQLEANY EQWKSQTSSW TPANNVSLHT
//
