Q74E25
Gene name |
tyrS |
Protein name |
Tyrosine--tRNA ligase |
Names |
Tyrosyl-tRNA synthetase, TyrRS |
Species |
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA) |
KEGG Pathway |
gsu:GSU1139 |
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 Q74E25
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q74E25-F1 | Predicted | AlphaFoldDB |
No variants for Q74E25
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q74E25 | |||||
No associated diseases with Q74E25
4 regional properties for Q74E25
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aldo/keto reductase, conserved site | 39 - 56 | IPR018170-1 |
| conserved_site | Aldo/keto reductase, conserved site | 145 - 162 | IPR018170-2 |
| conserved_site | Aldo/keto reductase, conserved site | 261 - 276 | IPR018170-3 |
| domain | NADP-dependent oxidoreductase domain | 17 - 289 | IPR023210 |
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 | |
1 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| 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 |
|---|---|
| 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. |
| tyrosyl-tRNA aminoacylation | The process of coupling tyrosine to tyrosyl-tRNA, catalyzed by tyrosyl-tRNA synthetase. The tyrosyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tyrosine-accetping tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSVADQMALI | KRGAVEILVE | KELEEKLEKS | AKTGVPLKIK | AGFDPTAPDL | HLGHTVLLHK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| MRQFQQLGHE | VIFLIGDFTG | MIGDPTGKSE | TRKALSREDV | LRNAETYKEQ | VFKILDPEKT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RVAFNSEWLA | KLDAGGMIGL | AAKYTVARML | ERDDFGKRFA | NQLPISIHEF | LYPLIQGYDS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VALQADVELG | GTDQKFNLLV | GRELQREWGQ | TPQTVITMPL | LEGLDGVNKM | SKSLGNYIGI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NEPADEIFGK | IMSISDELML | RYYELLSDLS | MAEIDGMRTG | IRDGSVHPME | AKKQLGREVV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ARYHGAAAAT | DAEEHFVKRF | RDNQTPDEMP | ELTLAATDEK | VALCRLLAEA | GLVKSNSEGR |
| 370 | 380 | 390 | 400 | ||
| RAIQQGGVKV | NGEKVSDESL | ELAATGVYVI | QFGKRRFARI | TFA |