Q3UQ84
Gene name |
Tars2 (Tarsl1) |
Protein name |
Threonine--tRNA ligase, mitochondrial |
Names |
Threonyl-tRNA synthetase, ThrRS, Threonyl-tRNA synthetase-like 1 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:71807 |
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 Q3UQ84
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q3UQ84-F1 | Predicted | AlphaFoldDB |
48 variants for Q3UQ84
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388652541 | 11 | G>R | No | EVA | |
| rs3388645080 | 36 | W>* | No | EVA | |
| rs3388638942 | 65 | A>T | No | EVA | |
| rs3393398117 | 71 | P>H | No | EVA | |
| rs3388651796 | 73 | G>C | No | EVA | |
| rs3388649901 | 76 | V>I | No | EVA | |
| rs3388645087 | 88 | L>Q | No | EVA | |
| rs3388651649 | 102 | A>D | No | EVA | |
| rs33141404 | 118 | T>R | No | EVA | |
| rs3388638905 | 125 | L>Q | No | EVA | |
| rs3388630611 | 134 | A>T | No | EVA | |
| rs3388649881 | 135 | V>L | No | EVA | |
| rs3388649288 | 163 | E>A | No | EVA | |
| rs3388645083 | 166 | F>L | No | EVA | |
| rs3388646387 | 169 | D>V | No | EVA | |
| rs3393251128 | 171 | F>C | No | EVA | |
| rs228733212 | 277 | T>A | No | EVA | |
| rs3388644521 | 290 | E>* | No | EVA | |
| rs33138953 | 298 | R>Q | No | EVA | |
| rs238103334 | 301 | A>E | No | EVA | |
| rs3388641381 | 301 | A>S | No | EVA | |
| rs3388648944 | 328 | F>C | No | EVA | |
| rs3388650200 | 331 | P>S | No | EVA | |
| rs3388644593 | 376 | Y>F | No | EVA | |
| rs3388652560 | 380 | M>I | No | EVA | |
| rs3388649244 | 386 | P>L | No | EVA | |
| rs212086913 | 392 | D>N | No | EVA | |
| rs3388651659 | 420 | M>I | No | EVA | |
| rs3388637944 | 440 | A>G | No | EVA | |
| rs3388648865 | 456 | L>M | No | EVA | |
| rs3388630625 | 470 | P>A | No | EVA | |
| rs3388641334 | 471 | H>L | No | EVA | |
| rs3388649275 | 526 | K>M | No | EVA | |
| rs3388652621 | 543 | P>H | No | EVA | |
| rs3388637938 | 615 | W>* | No | EVA | |
| rs3388637949 | 615 | W>* | No | EVA | |
| rs3388652527 | 619 | L>F | No | EVA | |
| rs250983498 | 619 | L>R | No | EVA | |
| rs3388651683 | 621 | V>M | No | EVA | |
| rs3388649826 | 631 | E>K | No | EVA | |
| rs33136965 | 651 | D>H | No | EVA | |
| rs3388644426 | 659 | S>I | No | EVA | |
| rs3402727894 | 674 | F>I | No | EVA | |
| rs3388652539 | 681 | Q>* | No | EVA | |
| rs3388642581 | 690 | T>A | No | EVA | |
| rs214432069 | 700 | D>G | No | EVA | |
| rs3388652613 | 709 | L>P | No | EVA | |
| rs3388644522 | 721 | E>V | No | EVA |
No associated diseases with Q3UQ84
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 | |
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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminoacyl-tRNA editing activity | The hydrolysis of an incorrectly aminoacylated tRNA. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| protein homodimerization activity | Binding to an identical protein to form a homodimer. |
| threonine-tRNA ligase activity | Catalysis of the reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). |
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. |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| P07236 | MST1 | Threonine--tRNA ligase, mitochondrial | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) | PR |
| A6QNM8 | TARS3 | Threonine--tRNA ligase 2, cytoplasmic | Bos taurus (Bovine) | PR |
| P26639 | TARS1 | Threonine--tRNA ligase 1, cytoplasmic | Homo sapiens (Human) | PR |
| Q9NYK5 | MRPL39 | 39S ribosomal protein L39, mitochondrial | Homo sapiens (Human) | PR |
| Q9D0R2 | Tars1 | Threonine--tRNA ligase 1, cytoplasmic | Mus musculus (Mouse) | PR |
| Q9JKF7 | Mrpl39 | 39S ribosomal protein L39, mitochondrial | Mus musculus (Mouse) | PR |
| Q68FW7 | Tars2 | Threonine--tRNA ligase, mitochondrial | Rattus norvegicus (Rat) | PR |
| Q8GZ45 | At1g17960 | Probable threonine--tRNA ligase, cytoplasmic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGLCLRWRRL | GFPLPEFRRC | ELHTVREASA | PTPPHWLAER | FGLFEELWTA | HVKKLASMTQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KKARAIKISL | PEGQKVDAVA | WNTTPYQLAH | QISVTLADTA | VAAEVNGELY | DLDRPLETDC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HLRFLTFDSP | EGKAVFWHSS | AHVLGAAAEQ | QLGAVLCRGP | STESGFYHDF | FLGKERTVRS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AELPILERIC | QELIAAAQPF | RRLEASRDQL | RQLFKDNHFK | LHLIEEKVTG | PTATVYGCGM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SVDLCRGPHL | RHTGQIGALK | LLTNSSALWR | SLGAPETLQR | VSGISFPKVE | LLRNWEARRE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AAELRDHRRI | GKEQELFFFH | ELSPGSCFFL | PRGTRVYNAL | VAFIRAEYAR | RGFSEVKTPT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LFSTKLWEQS | GHWEHYRADM | FSLKPPGTDG | VDNSQSGHPA | RCPKDTLALK | PMNCPAHCLM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| FAHRPRSWRE | LPVRLADFGA | LHRAEASGSL | GGLTRLWRFQ | QDDAHIFCAP | HQLEAEIQGC |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LDFLRCVYSV | LGFSFHLALS | TRPPGFLGEP | RLWDQAEQVL | QQALEKFGEP | WDLNPGDGAF |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YGPKIDVHLH | DALGRPHQCG | TIQLDFQLPL | RFDLQYKGPA | GTPECPVLIH | RAVLGSVERL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LGVLAESCGG | KWPLWLSPLQ | VVVIPVRTEQ | EEYARQVQQC | LQAAGLVSDL | DADSGLTLSR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| RVRRAQLAHY | NFQFVVGQRE | QSQRTVNVRT | RDNRQLGERD | LAESVQRLLE | LQNARVPNAE |
| EVF |