Q1GVA9
Gene name |
thrS |
Protein name |
Threonine--tRNA ligase |
Names |
Threonyl-tRNA synthetase, ThrRS |
Species |
Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis) |
KEGG Pathway |
sal:Sala_0692 |
EC number |
6.1.1.3: 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 Q1GVA9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1GVA9-F1 | Predicted | AlphaFoldDB |
No variants for Q1GVA9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1GVA9 | |||||
No associated diseases with Q1GVA9
7 regional properties for Q1GVA9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 348 - 555 | IPR002314 |
| domain | TGS | 3 - 64 | IPR004095 |
| domain | Anticodon-binding | 568 - 657 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 252 - 561 | IPR006195 |
| domain | Threonyl/alanyl tRNA synthetase, SAD | 176 - 228 | IPR012947 |
| domain | Threonine-tRNA ligase catalytic core domain | 252 - 566 | IPR033728 |
| domain | Threonine-tRNA ligase, class IIa, anticodon-binding domain | 566 - 656 | IPR047246 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.3 | 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. |
| metal ion binding | Binding to a metal ion. |
| threonine-tRNA ligase activity | Catalysis of the reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). |
| tRNA binding | Binding to a transfer RNA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| threonyl-tRNA aminoacylation | The process of coupling threonine to threonyl-tRNA, catalyzed by threonyl-tRNA synthetase. The threonyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a threonine-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 |
| MSDMIRVTLP | DGSAREVARG | TTPAEIAAAI | GPGLAKAALA | AKIDGELRDI | MRPLEEDTNL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ALVTSRDEAD | ALELARHDYA | HVLAEAVQTL | FPGTQITFGP | ATSDGFYYDF | APTAEHGPFR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DEELPLIEEE | MRRIIAADKP | LRREVWDRDA | LIARWKKDGE | TFKAEWAAEL | PAGEEISVYW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SGDDWMDMCR | GPHLASTGKL | DPAAFKLTRV | SGAYWRGDQK | NAQLSRIYGT | GWLNRKQLAE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| HLVRLEEAAK | RDHRRLGQEM | DLFHLQQEAH | GSVFWHPNGF | VVWRELEAYM | RRAIDAAGYR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EVKTPQVMDA | RQWEQSGHWG | KYRENMFVIP | DEVPNTEDEG | PIVSDDAEWM | ALKPMNCPAH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VLIFRQGMKS | YRDLPLRLYE | NGCCHRNEPH | GALHGLMRVR | QFTQDDAHIF | CREDQIVEEV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RNFCALADRI | YKDFGFTYAI | KLALRPEKRF | GSDAMWDKSE | DELRNAVIEA | GLATEQYGWE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ELPGEGAFYA | PKLEWHLTDA | IGRTWQVGTI | QSDRVLPDRL | DASYIGEDGE | RHRPVMLHRA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IFGSYERFIG | ILIEHFVGRF | PTWLAPVQAV | VATIVSDADD | YAKAATARLV | AAGIRTESDL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RNEKINYKVR | EHSLAKVPHL | LVVGKREAEE | GTVAIRTLGQ | DGQRIMPLAE | AIAMLKTQAT |
| PPDLKVR |