Q7T287
Gene name |
aptx |
Protein name |
Aprataxin |
Names |
Forkhead-associated domain histidine triad-like protein, FHA-HIT |
Species |
Xenopus laevis (African clawed frog) |
KEGG Pathway |
xla:398657 |
EC number |
3.6.1.71: In phosphorus-containing anhydrides |
Protein Class |
|
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 Q7T287
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7T287-F1 | Predicted | AlphaFoldDB |
No variants for Q7T287
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7T287 | |||||
No associated diseases with Q7T287
5 regional properties for Q7T287
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | HIT-like domain | 173 - 278 | IPR011146 |
| conserved_site | Histidine triad, conserved site | 252 - 270 | IPR019808 |
| domain | Aprataxin, C2HE/C2H2/C2HC zinc finger | 288 - 345 | IPR032566 |
| domain | PNK, FHA domain | 4 - 99 | IPR041388 |
| domain | Aprataxin, forkhead associated domain | 2 - 101 | IPR047289 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.6.1.71 | In phosphorus-containing anhydrides |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| nucleolus | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. |
| nucleoplasm | That part of the nuclear content other than the chromosomes or the nucleolus. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| DNA 5'-adenosine monophosphate hydrolase activity | Catalysis of the reaction: 5'-AMP-DNA + H2O = AMP + DNA; nucleophilic release of a covalently linked adenylate residue from a DNA strand, leaving a 5' phosphate terminus. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| DNA-3'-diphospho-5'-guanosine diphosphatase | Catalysis of the reaction: (DNA)-3'-diphospho-5'-guanosine + H2O = (DNA)-3'-phosphate + GMP. |
| metal ion binding | Binding to a metal ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MFECWLVSKD | GKHGRIRLPH | AETVVIGRGP | ETQITDKKCS | RHQVQLMADC | NKGYVKVKQM |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GTNPTSINGV | DIGNEHKVEL | KPGHTLYIVN | NLYPYMIEFL | EGSTNPRAKI | ENENRSSSKR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TPENSLNVDT | ETPRKLVKKE | SNVSPSSSSG | RISSCPTQGK | SNVQEVKSQG | HWSQDLKVSM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QDPTMQVFKD | DKIVVIKDKY | PKARYHWLVL | PWQSIASLKV | LRAEHLELVQ | HMDAVGHNIA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| REHTNSKCAP | FRFGYHAIPS | MSHVHLHVIS | QDFDSPCLKN | KKHWNSFTTD | YFLESQAVIE |
| 310 | 320 | 330 | 340 | ||
| MLKTHGKVNV | KERISDVLKT | PLLCHMCKKE | QATMPQLKEH | LKKHWPT |