Q3SKD9
Gene name |
lysS |
Protein name |
Lysine--tRNA ligase |
Names |
Lysyl-tRNA synthetase, LysRS |
Species |
Thiobacillus denitrificans (strain ATCC 25259) |
KEGG Pathway |
tbd:Tbd_0893 |
EC number |
6.1.1.6: 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 Q3SKD9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3SKD9-F1 | Predicted | AlphaFoldDB |
No variants for Q3SKD9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q3SKD9 | |||||
No associated diseases with Q3SKD9
5 regional properties for Q3SKD9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 159 - 497 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 65 - 142 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 183 - 495 | IPR006195 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 173 - 498 | IPR018149 |
| domain | Lysine-tRNA ligase, class II, N-terminal | 64 - 170 | IPR044136 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.6 | 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. |
| lysine-tRNA ligase activity | Catalysis of the reaction: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate + L-lysyl-tRNA(Lys). |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| nucleic acid binding | Binding to a nucleic acid. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| lysyl-tRNA aminoacylation | The process of coupling lysine to lysyl-tRNA, catalyzed by lysyl-tRNA synthetase. The lysyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a lysine-accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTDPTNAPAL | DENQIIAERR | AKLAAIREAG | VAFPNDFERR | DYAGRLAHEH | GDKSKEALEA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EAVDVQLAGR | MMLKRVMGKA | SFATLQDMSG | RIQVYVSNDL | TGLDAHEAFK | RWDLGDFVGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SGTLFKTNKG | ELTIQAKSVR | LLSKALRPLP | EKFHGLADQE | QKYRQRYLDL | ITNDDARSTF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VRRSKIIQAI | REFMTGHGFL | EVETPMMHPI | PGGAAAKPFV | THHNALDMEL | FLRIAPELYL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KRLVVGGFEK | VFEINRNFRN | EGLSTRHNPE | FTMMEFYEAY | REYRYLMDFT | EALIRHTAVA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ATGSTTISYQ | GSTIELGTPF | DRLTIVEAVR | KYHPEYTVEQ | LNDRDWLTAQ | FTAMKAKYRE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HDGLGGLQLT | FFEETTEALL | VQPTFIVDYP | AEVSPLARRS | DTQPEITERF | ELFITGREMA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NGFSELNDAE | DQAERFMEQV | RAKEAGDEEA | MHYDADFIRA | LEHGLPPTGG | CGIGIDRLVM |
| 490 | 500 | ||||
| LLTDSPSIRD | VILFPQMRRE | A |