Q6MDC0
Gene name |
pheS |
Protein name |
Phenylalanine--tRNA ligase alpha subunit |
Names |
Phenylalanyl-tRNA synthetase alpha subunit, PheRS |
Species |
Protochlamydia amoebophila (strain UWE25) |
KEGG Pathway |
pcu:PC_RS03390 |
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 Q6MDC0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6MDC0-F1 | Predicted | AlphaFoldDB |
No variants for Q6MDC0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6MDC0 | |||||
No associated diseases with Q6MDC0
6 regional properties for Q6MDC0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | tRNA-binding domain | 39 - 156 | IPR002547 |
| domain | Ferrodoxin-fold anticodon-binding domain | 713 - 806 | IPR005121 |
| domain | B3/B4 tRNA-binding domain | 220 - 393 | IPR005146 |
| domain | tRNA synthetase, B5-domain | 409 - 488 | IPR005147 |
| domain | Phenylalanly tRNA synthetase, tRNA-binding-domain | 45 - 155 | IPR033714 |
| domain | Phenylalanyl tRNA synthetase beta chain, core domain | 486 - 698 | IPR041616 |
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 |
| MRSSVQPLIN | EIRQQFLHDL | EQVQTTLELE | QLKIKFLGKK | GSLQGLMKEL | KNVEPDQRPL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VGKFINELKE | FMSNHCDELE | HQLIAKEENA | QLAHETIDVT | LPGRQRFVGR | KHPLTQAMDQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| IIHILSKMGF | SVQYGPDIDT | DYYNFEILNF | PPEHPARDMQ | DTFYISPHVL | LRTHTSNIQA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RAMELNRPPI | RIIAPGKVYR | NETITARSHV | FFHQVEAVYI | DQHVSFADLF | ATMDEFLKKL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FKQTIETRYR | PSYFPFVEPG | LEVDISCLVC | EGKGCQLCKH | TGWVEVAGAG | MIHPEVLKNG |
| 310 | 320 | 330 | 340 | ||
| GIDPEHYSGF | AWGMGLERLV | MMLRGIQDIR | LFTENDLRFL | QQFTLL |