National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory
Protein Information |
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|---|---|
| Protein Name | Protein adenylyltransferase fic-1 |
| Accession Code | Q23544 |
| Gene | fic |
| Organism | Caenorhabditis elegans (Taxonomy: 6239) |
| Part of Reference Proteome? | Yes |
| Sequence (Length: 508) |
Structure Viewer (PDB: 5JJ6) |
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Description |
Position in the Nuclear Envelope |
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|---|---|---|
| Location | Location ID | Description |
| Nuclear Envelope | SL-0178 | The nuclear envelope is a membrane system which surrounds the nucleoplasm of eukaryotic cells. It is composed of the nuclear lamina, nuclear pore complexes and two nuclear membranes. The space between the two membranes is called the nuclear intermembrane space. |
| Nuclear Membrane | SL-0182 | The membrane surrounding the nucleus. This term is used when it is not known if the protein is found in or associated with the inner or outer nuclear membrane. | Membrane Topology |
| Topology | Source | Annotation Type |
| Transmembrane | UniProt | Sequence Analysis {ECO:0000255} | Assigned Ontology terms |
Description |
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|---|---|
| Protein that can both mediate the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-274 determines which of the two opposing activities (AMPylase or de-AMPylase) will take place (By similarity). Adenylyltransferase that mediates the addition of adenosine 5'- monophosphate (AMP) to specific residues of target proteins (PubMed:27138431). In vivo target proteins include the heat-shock 70 family proteins hsp-1 and hsp-3 and the translation elongation factors eef-1A, eef-1G and eef-2 (PubMed:27138431). Can AMPylate core histone H3 in vitro (PubMed:27138431). Can also act as a phosphodiesterase by mediating removal of ATP (de-AMPylation) from target proteins (By similarity). Decreases susceptibility to P.aeruginosa-mediated killing and might therefore play a role in the innate immune response (PubMed:27138431). {By SimilarityUniProtKB:A0A061I403, By SimilarityUniProtKB:Q8SWV6, Experimental EvidencePubMed:27138431}. | Assigned Ontology terms |
Database | Links |
| UNIPROT | Q23544 |
| PDB | 5JJ6 5JJ7 |
| Pfam | PF02661 |
| PROSITE | PS51459 PS50005 PS50293 |
National and Kapodistrian University of Athens
Department of Biology
Biophysics & Bioinformatics Laboratory