Q5I0L3
Gene name |
Yars2 |
Protein name |
Tyrosine--tRNA ligase, mitochondrial |
Names |
Tyrosyl-tRNA synthetase, TyrRS |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:287924 |
EC number |
6.1.1.1: 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 Q5I0L3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5I0L3-F1 | Predicted | AlphaFoldDB |
No variants for Q5I0L3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5I0L3 | |||||
No associated diseases with Q5I0L3
1 regional properties for Q5I0L3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 76 - 86 | IPR001412 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.1 | Ligases forming aminoacyl-tRNA and related compounds |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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. |
| nuclear body | Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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. |
| tRNA binding | Binding to a transfer RNA. |
| tyrosine binding | Binding to 2-amino-3-(4-hydroxyphenyl)propanoic acid. |
| tyrosine-tRNA ligase activity | Catalysis of the reaction: L-tyrosine + ATP + tRNA(Tyr) = L-tyrosyl-tRNA(Tyr) + AMP + diphosphate + 2 H(+). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| mitochondrial tyrosyl-tRNA aminoacylation | The process of coupling tyrosine to tyrosyl-tRNA in a mitochondrion, catalyzed by tyrosyl-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. |
| tRNA aminoacylation | The chemical reactions and pathways by which the various amino acids become bonded to their corresponding tRNAs. The most common route for synthesis of aminoacyl tRNA is by the formation of an ester bond between the 3'-hydroxyl group of the most 3' adenosine of the tRNA and the alpha carboxylic acid group of an amino acid, usually catalyzed by the cognate aminoacyl-tRNA ligase. A given aminoacyl-tRNA ligase aminoacylates all species of an isoaccepting group of tRNA molecules. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAAPMLRHLC | RVPQSGVWTR | GPRAVRPGAR | GMLVAPRARG | LFKEFFPESG | TKTELPELFD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RRRAGSPQTV | YCGFDPTGDS | LHVGHLLTLL | GLFHFQRAGH | NVIALVGGST | ALLGDPSGRT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KEREALSAEC | VRANARALQR | GLETLAANHA | RLFADGRPWG | TFTVLDNAAW | FQKQHLMDFL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ATVGGHFRMG | TLLSRLSVQS | RLKSPEGMSL | AEFFYQVLQA | YDFYYLFRHY | GCRVQLGGSD |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QLGNIMSGYE | FIHKLTGEDV | FGITVPLITS | TTGAKLGKSA | GNAVWLNREK | TSPFELYQFF |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IRQQDDSVER | YLKLFTFLPL | PEIDHIMQLH | VKEPEKRIAQ | KRLAAEVTKL | VHGQEGLDSA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KRCTQALYHS | SIEALEVMSD | QELKELFKEA | SFSELVLDPG | TSVIDTCRKA | NAIPDGPRGY |
| 430 | 440 | 450 | 460 | 470 | |
| RMITEGGVSI | NHRQVTNPES | VLVIGQHILK | NGLSLLKIGK | RNFYIIKWLQ | L |