Q5ZJQ2
Gene name |
FARSA (FARSLA, RCJMB04_16g22) |
Protein name |
Phenylalanine--tRNA ligase alpha subunit |
Names |
Phenylalanyl-tRNA synthetase alpha subunit, PheRS |
Species |
Gallus gallus (Chicken) |
KEGG Pathway |
gga:100859604 |
EC number |
6.1.1.20: Ligases forming aminoacyl-tRNA and related compounds |
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 Q5ZJQ2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5ZJQ2-F1 | Predicted | AlphaFoldDB |
No variants for Q5ZJQ2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5ZJQ2 | |||||
No associated diseases with Q5ZJQ2
5 regional properties for Q5ZJQ2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phenylalanyl-tRNA synthetase | 213 - 442 | IPR002319 |
| domain | Aminoacyl-tRNA synthetase, class II | 232 - 443 | IPR006195 |
| domain | PheRS DNA binding domain 2 | 137 - 168 | IPR040586 |
| domain | PheRS, DNA binding domain 1 | 1 - 64 | IPR040724 |
| domain | PheRS, DNA binding domain 3 | 78 - 135 | IPR040725 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.20 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| phenylalanine-tRNA ligase complex | An enzyme complex that catalyzes the ligation of phenylalanine to tRNA(Phe), forming L-phenylalanyl-tRNA(Phe). |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| phenylalanine-tRNA ligase activity | Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). |
| tRNA binding | Binding to a transfer RNA. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| phenylalanyl-tRNA aminoacylation | The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
| protein heterotetramerization | The formation of a protein heterotetramer, a macromolecular structure consisting of four noncovalently associated subunits, of which not all are identical. |
4 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P08312 | pheS | Phenylalanine--tRNA ligase alpha subunit | Escherichia coli (strain K12) | PR |
| Q9Y285 | FARSA | Phenylalanine--tRNA ligase alpha subunit | Homo sapiens (Human) | PR |
| Q505J8 | Farsa | Phenylalanine--tRNA ligase alpha subunit | Rattus norvegicus (Rat) | PR |
| Q1JPX3 | farsa | Phenylalanine--tRNA ligase alpha subunit | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSPSVAELLL | QRLERTPPGP | EGGLCSLEAA | AALGLDHQTL | VGAVKSLQAL | GEVIEAETRA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TTRWELSAEG | EEVLRDGSPE | VRLFRSVPSE | GLPQSDAMKL | PGAQVGFSKA | MANKWLRLDK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GAPGGPRIFR | AVDAVQDVVQ | SSLRQVQEGN | GGSLSERERT | DLKRRKLLLE | VTLKSYWIRK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GSAFSTAVVR | QETDLTPEMI | ATGSWRKLPF | KAYNFSALGL | PPTCGHLHPL | LKVRSQLRQI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FLEMGFTEMP | TDNFVESSFW | NFDALFQPQQ | HPARDQHDTF | FLQDPAEAPE | LPANYMARVK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KVHSQGGYGS | QGYKYEWKVE | EARKNLLRTH | TTSASARALY | HLARQGKFTP | VKYFSIDRVF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RNESLDATHL | AEFHQVEGVV | ADRGLTLGHL | MGTLQQFFTK | LGISKLRFKP | AYNPYTEPSM |
| 430 | 440 | ||||
| EVFSYHEGLK | KWVEVGNSGV | FRS |