A5WAC2
Gene name |
argS |
Protein name |
Arginine--tRNA ligase |
Names |
Arginyl-tRNA synthetase, ArgRS |
Species |
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1) |
KEGG Pathway |
ppf:Pput_4962 |
EC number |
6.1.1.19: 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 A5WAC2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5WAC2-F1 | Predicted | AlphaFoldDB |
No variants for A5WAC2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5WAC2 | |||||
No associated diseases with A5WAC2
4 regional properties for A5WAC2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 127 - 138 | IPR001412 |
| domain | Arginyl tRNA synthetase N-terminal domain | 3 - 91 | IPR005148 |
| domain | DALR anticodon binding | 462 - 578 | IPR008909 |
| domain | Arginyl-tRNA synthetase, catalytic core domain | 101 - 448 | IPR035684 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.19 | 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. |
2 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. |
1 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKDTIRQLIQ | QALTQLVTDG | VLPEGLSPAI | QVENARDKTH | GDFASNIAMM | LAKPAGMKPR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DLAEKLINAL | PASADISKVE | IAGPGFLNFF | QNTDALANRL | DAALADAHLG | ARKAGPAQKV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIDMSAPNLA | KEMHVGHLRS | TIIGDSVARV | LEFLGDNVIR | QNHVGDWGTQ | FGMLMAYLQE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NPITSDELSD | LENFYRAAKK | RFDESEEFAT | RARGLVVKLQ | AGDPECLALW | TRFKDISLSH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CQKTYELLNV | KLTMADVMGE | SAYNDDLANV | VADLKAKGLL | VEDQGAQCVF | LDEFKNSEGD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PLPVIVQKAD | GGYLYATTDL | AAVRYRSNVL | KADRALYFVD | QRQALHFNQV | FEVARRAGFV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GHPMQMEHMG | FGTMNGADGR | PFKTRDGGTV | KLIDLLTEAK | ERAYALVKEK | NPSLADDELR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| HIGEVVGIGA | VKYADLSKHR | TSDYSFNFEL | MLNFEGNTAP | YLLYAYTRVA | GVFRKLGKGF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DEVDGKIVLH | AAHEQDLAAR | LAQFGEILNN | VAEKGTPHVL | CSYLYDLAGL | FSSFYENCPI |
| 550 | 560 | 570 | |||
| LAAETPSQQQ | SRLRLAALTG | RTLKQGLELL | GLETLERM |