P07236
Gene name |
MST1 (YKL194C) |
Protein name |
Threonine--tRNA ligase, mitochondrial |
Names |
Threonyl-tRNA synthetase, ThrRS |
Species |
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
KEGG Pathway |
sce:YKL194C |
EC number |
|
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
11 variants for P07236
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| s11-78644 | 3 | I>T | No | SGRP | |
| s11-78623 | 10 | C>Y | No | SGRP | |
| s11-78620 | 11 | S>C | No | SGRP | |
| s11-78609 | 15 | L>F | No | SGRP | |
| s11-78351 | 101 | E>K | No | SGRP | |
| s11-77883 | 257 | G>C | No | SGRP | |
| s11-77861 | 264 | P>L | No | SGRP | |
| s11-77601 | 351 | V>I | No | SGRP | |
| s11-77573 | 360 | V>A | No | SGRP | |
| s11-77522 | 377 | L>R | No | SGRP | |
| s11-77449 | 401 | E>D | No | SGRP |
No associated diseases with P07236
5 regional properties for P07236
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 114 - 337 | IPR002314 |
| domain | Anticodon-binding | 349 - 456 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 67 - 342 | IPR006195 |
| domain | Threonine-tRNA ligase catalytic core domain | 44 - 347 | IPR033728 |
| domain | Threonine-tRNA ligase, class IIa, anticodon-binding domain | 347 - 459 | IPR047246 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| threonine-tRNA ligase activity | Catalysis of the reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| mitochondrial threonyl-tRNA aminoacylation | The process of coupling threonine to threonyl-tRNA in a mitochondrion, catalyzed by threonyl-tRNA synthetase. In tRNA aminoacylation, the amino acid is first activated by linkage to AMP and then transferred to either the 2'- or the 3'-hydroxyl group of the 3'-adenosine residue of the tRNA. |
| 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. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| A6QNM8 | TARS3 | Threonine--tRNA ligase 2, cytoplasmic | Bos taurus (Bovine) | PR |
| P26639 | TARS1 | Threonine--tRNA ligase 1, cytoplasmic | Homo sapiens (Human) | PR |
| Q3UQ84 | Tars2 | Threonine--tRNA ligase, mitochondrial | Mus musculus (Mouse) | PR |
| Q9D0R2 | Tars1 | Threonine--tRNA ligase 1, cytoplasmic | Mus musculus (Mouse) | PR |
| Q68FW7 | Tars2 | Threonine--tRNA ligase, mitochondrial | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKIQLVRWHC | SRNALWNRAF | YSTRKATKNA | SSATPATMTS | MVSQRQDLFM | TDPLSPGSMF |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FLPNGAKIFN | KLIEFMKLQQ | KFKFGFNEVV | TPLIYKKTLW | EKSGHWENYA | DDMFKVETTD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EEKEEYGLKP | MNCPGHCLIF | GKKDRSYNEL | PLRFSDFSPL | HRNEASGALS | GLTRLRKFHQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DDGHIFCTPS | QVKSEIFNSL | KLIDIVYNKI | FPFVKGGSGA | ESNYFINFST | RPDHFIGDLK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VWNHAEQVLK | EILEESGKPW | KLNPGDGAFY | GPKLDIMVTD | HLRKTHQVAT | IQLDFQLPER |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FDLKFKDQDN | SYKRPIMIHR | ATFGSIERFM | ALLIDSNEGR | WPFWLNPYQA | VIIPVNTKNV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QQLDMCTALQ | KKLRNELEAD | DMEPVPLNDW | HFNVDLDIRN | EPVGYRIKSA | ILKNYSYLII |
| 430 | 440 | 450 | 460 | ||
| VGDEEVQLQK | YNIRERDNRK | SFEKLTMSQI | WEKFIELEKN | YK |