Q505J8
Gene name |
Farsa (Farsla) |
Protein name |
Phenylalanine--tRNA ligase alpha subunit |
Names |
Phenylalanyl-tRNA synthetase alpha subunit, PheRS |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:288917 |
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 Q505J8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q505J8-F1 | Predicted | AlphaFoldDB |
No variants for Q505J8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q505J8 | |||||
No associated diseases with Q505J8
No regional properties for Q505J8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for Q505J8 | |||
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 |
|---|---|---|---|---|
| Q5ZJQ2 | FARSA | Phenylalanine--tRNA ligase alpha subunit | Gallus gallus (Chicken) | PR |
| P08312 | pheS | Phenylalanine--tRNA ligase alpha subunit | Escherichia coli (strain K12) | PR |
| Q9Y285 | FARSA | Phenylalanine--tRNA ligase alpha subunit | Homo sapiens (Human) | PR |
| Q1JPX3 | farsa | Phenylalanine--tRNA ligase alpha subunit | Danio rerio (Zebrafish) (Brachydanio rerio) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MADNPVLEQL | LRRLEVADGG | LDSAELATQL | GVEHQAVVGA | VKSLQALGEV | IEAELRSTKC |
| 70 | 80 | 90 | 100 | 110 | 120 |
| WELTTEGEEI | AREGSHEARV | FRSIPLEGLV | QSELMQLPSG | KVGFSKAMSN | KWIRVDKSAA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DGPRVFRVVD | SIEDEVQRRL | QQVQAGQAEK | LAEKERNELR | KRKLLTEVIL | KTYWVSKGKG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FSTSVSKQEA | ELSPEMISSG | SWRDRPFKPY | NFSARGVLPD | SGHLHPLLKV | RSQFRQIFLE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| MGFTEMPTDN | FIESSFWNFD | ALFQPQQHPA | RDQHDTFFLR | DPAEALQLPM | DYVQRVKRTH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SQGGYGSQGY | KYTWKLEEAR | KNLLRTHTTA | ASARALYRLA | QKKPFTPAKY | FSIDRVFRNE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TLDATHLAEF | HQIEGVIADH | GLTLGHLMGV | LREFFTKLGI | TQLRFKPAYN | PYTEPSMEVF |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SYHQGLKKWV | EVGNSGVFRP | EMLLPMGLPE | NVSVIAWGLS | LERPTMIKYG | INNIRELVGH |
| 490 | 500 | ||||
| KVNLQMVYDS | PVCRLDIEPR | SSKTQEAA |