We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
ProRule PRU01192
View rule in raw text format (no links)
PURL: https://purl.expasy.org/prosite/rule/PRU01192
General rule information
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| Accession | PRU01192 |
| Dates | 31-OCT-2017 (Created)
19-NOV-2022 (Last updated, Version 5) |
| Data class | Domain; |
| Predictors |
PROSITE; PS51845; PDEASE_I_2 |
Name | 3'5'-cyclic nucleotide phosphodiesterase (PDEase) domain |
| Function | 3'5'-cyclic nucleotide phosphodiesterases (EC 3.1.4.17) (PDEases) contain a catalytic domain of approximately 270 amino acids at the carboxyl terminus. |
| Scope(s) |
Eukaryota |
| Example(s) | P16586; |
Propagated annotation
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Comments
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| case <FTGroup:1> | |
| COFACTOR | Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; Note=Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions |
| end case | |
| SIMILARITY | Belongs to the cyclic nucleotide phosphodiesterase family. |
Keywords
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| Metal-binding | |
| end case | |
| case <FTTag:act_site> and <FTGroup:1> | |
| Hydrolase | |
| end case | |
Gene Ontology
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| case <FTGroup:1> | |
| GO:0046872; Molecular function:metal ion binding | |
Cross-references
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| PROSITE | PS00126; PDEASE_I_1; 1; |
Features
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| From: PS51845 | ||||||||||||
| Key | From | To | Description | Tag | Condition | FTGroup | ||||||
| DOMAIN | from | to | /note="PDEase #" | |||||||||
| ACT_SITE | 77 | 77 | /note="Proton donor" | act_site | H | |||||||
| BINDING | 81 | 81 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
H | 1 | |||||||
| BINDING | 117 | 117 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
H | 1 | |||||||
| BINDING | 118 | 118 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
D | 1 | |||||||
| BINDING | 118 | 118 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="2" |
D | 1 | |||||||
| BINDING | 229 | 229 | /ligand="a divalent metal cation" /ligand_id="ChEBI:CHEBI:60240" /ligand_label="1" |
D | 1 | |||||||
Additional information
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| Size range | 300-450 amino acids |
| Related rules |
None |
| Fusion | None |
| Repeats | 1 |
| Topology | Undefined |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
UniProtKB rule member sequences
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- UniProtKB/Swiss-Prot sets
Eukaryota [103] All [ 103 ]
- Retrieve set of proteins with 3D structure for this domain