C5A5Y9
Gene name |
pheS |
Protein name |
Phenylalanine--tRNA ligase alpha subunit |
Names |
Phenylalanyl-tRNA synthetase alpha subunit, PheRS |
Species |
Thermococcus gammatolerans (strain DSM 15229 / JCM 11827 / EJ3) |
KEGG Pathway |
tga:TGAM_1149 |
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 C5A5Y9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C5A5Y9-F1 | Predicted | AlphaFoldDB |
No variants for C5A5Y9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C5A5Y9 | |||||
No associated diseases with C5A5Y9
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 | |
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. |
| 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. |
1 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MELSYQEKLT | LIKLNELKRA | KFEELVKATG | LEQVAVMRAV | LGLQAKGLAK | LHERSEKVVK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LTETGKKYAE | IGLPEWRALK | LLRERGKVTL | DDLREVLSDD | ELKPIVGLLR | KEGWASVRKE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DGKLILEITE | KGLEAEERPI | DRALKLLAEK | NVVPVKEIEK | LIPVKELKRR | KIGEEETVTE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RTVEITPAGE | ELAPKVELKR | EVSVLTPELI | KSGKWREVEF | RRFDIKAPVR | RIYPGKKQPY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RAFLDKIRRR | LIEMGFIEMT | VDSLIETQFW | NFDALFQPQN | HPAREWTDTY | QLKYPKSGFL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PEEELVERVK | TAHERGLAGS | RGWGYVWSPE | RAMLLMPRAH | GTALSGRQLA | KGVEIPGKYF |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TIQRVFRPDV | LDRTHLIEFN | QIDGFVVGEE | LNFRHLLGIL | KRFAVEIAGA | KKVKFLPDYY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PFTEPSVQMS | AYHPELGWVE | FGGAGIFREE | MTKALGIEVP | VIAWGIGIDR | LAMFKLGIDD |
| 490 | |||||
| IRYLFSYDLR | WLREAKLVW |