Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q9F417
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9F417-F1 | Predicted | AlphaFoldDB |
No variants for Q9F417
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9F417 | |||||
No associated diseases with Q9F417
11 regional properties for Q9F417
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Hint domain C-terminal | 331 - 379 | IPR003586 |
| domain | Hint domain N-terminal | 8 - 112 | IPR003587 |
| domain | Homing endonuclease, LAGLIDADG | 122 - 297 | IPR004860 |
| ptm | Intein N-terminal splicing region | 10 - 92 | IPR006141 |
| domain | Intein | 79 - 92 | IPR006142-1 |
| domain | Intein | 121 - 133 | IPR006142-2 |
| domain | Intein | 350 - 367 | IPR006142-3 |
| domain | Intein | 368 - 377 | IPR006142-4 |
| conserved_site | DNA recombination/repair protein RecA, conserved site | 383 - 391 | IPR020584 |
| domain | DNA recombination and repair protein RecA, monomer-monomer interface | 368 - 423 | IPR020587 |
| domain | Intein C-terminal splicing region | 352 - 374 | IPR030934 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| ATP-dependent activity, acting on DNA | Catalytic activity that acts to modify DNA, driven by ATP hydrolysis. |
| endonuclease activity | Catalysis of the hydrolysis of ester linkages within nucleic acids by creating internal breaks. |
| single-stranded DNA binding | Binding to single-stranded DNA. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA recombination | Any process in which a new genotype is formed by reassortment of genes resulting in gene combinations different from those that were present in the parents. In eukaryotes genetic recombination can occur by chromosome assortment, intrachromosomal recombination, or nonreciprocal interchromosomal recombination. Interchromosomal recombination occurs by crossing over. In bacteria it may occur by genetic transformation, conjugation, transduction, or F-duction. |
| DNA repair | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. |
| intein-mediated protein splicing | The removal of an internal amino acid sequence (an intein) from a protein during protein maturation; the excision of inteins is precise and the N- and C-terminal exteins are joined by a normal peptide bond. Protein splicing involves 4 nucleophilic displacements by the 3 conserved splice junction residues. |
| SOS response | An error-prone process for repairing damaged microbial DNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| REKIGVMFGC | FNYSTRVQLA | DGTTEKIGKI | VNNKMDVEVL | SYDPVADQVV | PRKVVNWFNN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GPAEQFLQFT | VEKSGGNGRS | QFAATPNHLI | RTPAGWSEAG | DLIAGDRVMA | SEPHRLSDQQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FQVVLGSLMG | DGNLSPNRRD | RNGVRFRMGH | GAKQGDYLQW | KTDLLANIAH | SAHENAKGAR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FVDFTPLPEL | AELQRAVYLG | DGKKFLSEEY | LKALTPLALA | IWYMDDGGFT | VRSKGLQQRT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EGGSGRIEIC | VEAMSVGSRD | RLRDYLRDTH | GLDVRLRHAG | AAGKAMLVFT | TAASAKFQEI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VAPYMAPSME | YKLLPRFRGQ | GTVAPQFVEP | TERLVPARIL | DIHVKPHTRS | MNRFDIEVEG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NHNYFVDGVM | VHNSPETTTG | GKALKFYASV | RIDVRRIETL | KDGTDAVGNR | TRAKIVKNKV |
| SPP |