Q6AY47 (FICD_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
March 6, 2013.
Version 68.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Adenosine monophosphate-protein transferase FICD EC=2.7.7.n1 Alternative name(s): AMPylator FICD FIC domain-containing protein | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| Taxonomic identifier | 10116 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus![]() |
Protein attributes
| Sequence length | 458 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at transcript level |
General annotation (Comments)
| Function | Adenylyltransferase that mediates the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins By similarity. |
| Catalytic activity | ATP + [protein] = diphosphate + [protein]-AMP. |
| Enzyme regulation | Adenylyltransferase activity is inhibited by the inhibitory helix present at the N-terminus: Glu-234 binds ATP and competes with ATP-binding at Arg-374, thereby preventing adenylyltransferase activity. Activation dissociates ATP-binding from Glu-234, allowing ordered binding of the entire ATP moiety with the alpha-phosphate in an orientation that is productive for accepting an incoming target hydroxyl side chain By similarity. |
| Subunit structure | Interacts with HD By similarity. |
| Subcellular location | Membrane; Single-pass membrane protein Potential. |
| Domain | The fido domain mediates the adenylyltransferase activity By similarity. |
| Sequence similarities | Belongs to the fic family. Contains 1 fido domain. Contains 2 TPR repeats. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Membrane |
| Domain | Repeat TPR repeat Transmembrane Transmembrane helix |
| Ligand | ATP-binding Nucleotide-binding |
| Molecular function | Nucleotidyltransferase Transferase |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Cellular_component | integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein adenylyltransferase activityInferred from sequence or structural similarity. Source: UniProtKB |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 458 | 458 | Adenosine monophosphate-protein transferase FICD | PRO_0000317303 | |||||
Regions | |||||||||
| Transmembrane | 24 – 44 | 21 | Helical; Potential | ||||||
| Repeat | 106 – 139 | 34 | TPR 1 | ||||||
| Repeat | 140 – 173 | 34 | TPR 2 | ||||||
| Domain | 285 – 420 | 136 | Fido | ||||||
| Nucleotide binding | 260 – 261 | 2 | ATP By similarity | ||||||
| Nucleotide binding | 368 – 370 | 3 | ATP By similarity | ||||||
| Motif | 230 – 235 | 6 | Inhibitory (S/T)XXXE(G/N) motif | ||||||
Sites | |||||||||
| Binding site | 234 | 1 | ATP By similarity | ||||||
| Binding site | 374 | 1 | ATP By similarity | ||||||
Sequences
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References
| [1] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Testis. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | BC079197 mRNA. Translation: AAH79197.1. |
| IPI | IPI00371233. |
| RefSeq | NP_001010946.1. NM_001010946.1. |
| UniGene | Rn.162153. |
3D structure databases | |
| ProteinModelPortal | Q6AY47. |
| ModBase | Search... |
Proteomic databases | |
| PRIDE | Q6AY47. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSRNOT00000000892; ENSRNOP00000000892; ENSRNOG00000000703. |
| GeneID | 288741. |
| KEGG | rno:288741. |
| UCSC | RGD:1359391. rat. |
Organism-specific databases | |
| CTD | 11153. |
| RGD | 1359391. Ficd. |
Phylogenomic databases | |
| eggNOG | COG3177. |
| GeneTree | ENSGT00390000008873. |
| HOGENOM | HOG000008059. |
| HOVERGEN | HBG095654. |
| InParanoid | Q6AY47. |
| OMA | MKYINTT. |
| OrthoDB | EOG4RR6HD. |
Gene expression databases | |
| Genevestigator | Q6AY47. |
Family and domain databases | |
| Gene3D | 1.25.40.10. 1 hit. |
| InterPro | IPR003812. Fido. IPR013026. TPR-contain_dom. IPR011990. TPR-like_helical. [Graphical view] |
| Pfam | PF02661. Fic. 1 hit. [Graphical view] |
| SUPFAM | SSF140931. SSF140931. 1 hit. |
| PROSITE | PS51459. FIDO. 1 hit. PS50005. TPR. False negative. PS50293. TPR_REGION. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 628637. |
Entry information
| Entry name | FICD_RAT | ||||||||
| Accession | Primary (citable) accession number: Q6AY47 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

Clusters with
