Q1LTU2
Gene name |
glyS |
Protein name |
Glycine--tRNA ligase beta subunit |
Names |
Glycyl-tRNA synthetase beta subunit, GlyRS |
Species |
Baumannia cicadellinicola subsp Homalodisca coagulata |
KEGG Pathway |
bci:BCI_0160 |
EC number |
6.1.1.14: 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 Q1LTU2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1LTU2-F1 | Predicted | AlphaFoldDB |
No variants for Q1LTU2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1LTU2 | |||||
No associated diseases with Q1LTU2
1 regional properties for Q1LTU2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | DALR anticodon binding | 585 - 680 | IPR008909 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.14 | 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| arginine-tRNA ligase activity | Catalysis of the reaction: ATP + L-arginine + tRNA(Arg) = AMP + diphosphate + L-arginyl-tRNA(Arg). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glycine-tRNA ligase activity | Catalysis of the reaction: ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| arginyl-tRNA aminoacylation | The process of coupling arginine to arginyl-tRNA, catalyzed by arginyl-tRNA synthetase. The arginyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of an alanine accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
| glycyl-tRNA aminoacylation | The process of coupling glycine to glycyl-tRNA, catalyzed by glycyl-tRNA synthetase. The glycyll-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a glycine-accepting tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKQHIFLVEI | GTEELPAKEL | RRLAQYFTAN | FINELNANGI | NYNDINWFAA | PRRLAIKVNS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| INSIPTKSYM | EKRGPAINKA | FDAEGKPTPA | AIGWARNCGI | TVNQAERFTT | DKGEWLIYRM |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LVETKPVQKL | LCSMVYNALT | KFSSLTKIMR | WGEKNYKFIR | PVRTITLLLD | DLVIPGNIFG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IDSNRIILGH | RFMGESVISL | LHADYYPNVL | LERGRVIADY | ELRKDTIRRN | IEIMVKKIGG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FTKINDKLLE | EVTSLVDWPI | VLTASFNANF | LRIPAEALIY | TMENNQKYFP | VYDAKGKLLP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| YFIFVTNIES | TNTNQIVVGN | EKVMRSRLAD | VEFFFNIDRK | QKLEDYLLLL | GQVKFQMELG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TLLDKSYRLE | ILASWIAEII | STDIKQAARA | ALISKCDLMT | QMVFEYPEIQ | GIIGMHYATL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DGETELVALA | QKEQYLPLFS | GDNLPTTLVS | CAVSIADKMD | NLAGIFGINQ | QYTKQANDPL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ALRRAALGIL | RIIIEKQLPI | DLLSLIDKAV | FLYNKKLTNT | IVVEQIIHFM | LNRLLSWYKK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| QGYSIDTINA | VMAVYKPTGK | LIHFDARLRA | VHYLRQIPHA | ENLTKRIFNI | IAKHKDLING |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EVNFTLLKQP | EEVILINSIT | QLHKKLILFF | EKGKYQEALW | ELINLREIIN | TFFSKIIIMT |
| 670 | 680 | 690 | |||
| ENKELCINRL | NIINKVRQLF | LIIADFSLLQ | CSKEKSNVD |