P75225
Gene name |
thrS |
Protein name |
Threonine--tRNA ligase |
Names |
Threonyl-tRNA synthetase, ThrRS |
Species |
Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae) |
KEGG Pathway |
mpn:MPN_553 |
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 P75225
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P75225-F1 | Predicted | AlphaFoldDB |
No variants for P75225
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P75225 | |||||
No associated diseases with P75225
5 regional properties for P75225
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 249 - 458 | IPR002314 |
| domain | Anticodon-binding | 471 - 562 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 198 - 464 | IPR006195 |
| domain | Threonine-tRNA ligase catalytic core domain | 167 - 469 | IPR033728 |
| domain | Threonine-tRNA ligase, class IIa, anticodon-binding domain | 469 - 561 | 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 |
| MLAGVLLLQS | WLKANYPQVQ | FGSYGVQEGE | FYLDFKVEKS | FSIKEFEQLE | QDLNAYFNQL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NNVVQTKIDK | TKSLKFFQAD | PFTTTLIESI | ESNSLVVTTV | NEQTFWVHDL | VLPLPKQGFV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KLLNVSANYF | LGDPTKPQLQ | RLVGIFAASK | EQLKSLIAAN | EQKYQNDHRA | IGKRLEIFTF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DPLVGAGFPI | WLEKGAVLKK | IIGDFVHYQQ | LMFGFKTVSS | PVLANLELYK | ISGHYVHYSE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DMFPSVKLEN | QMMMLRPMTC | PHHCLIFKHK | RRSYKELPQR | FCEDSILHRF | EASGGLTGLE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RVRCMTLLDN | HIFCRTDQIK | AEIKNAFKLI | QTVNNKFGFS | FDRIDLALHD | PNNKAKFIDN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DQLWANSESQ | IESVFKELNV | PYKIDVGAAA | FYGPKIDFQF | KTALNKMITI | ATIQLDFLLP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ERFELRYFDE | QSNAQTPVII | HVGIVGTYER | FIAALLEKTH | GNLPLWMAPV | QVVVIPVNID |
| 490 | 500 | 510 | 520 | 530 | 540 |
| KHEKAAKKLY | QKLLKENIRV | SLDESEDRLG | KKVRTAIVNK | IPLQIIVGDK | EMQDLTRITC |
| 550 | 560 | ||||
| RGFKGEKVQK | LYWANFVKKV | RKDG |