Q46127
Gene name |
trpS |
Protein name |
Tryptophan--tRNA ligase |
Names |
Tryptophanyl-tRNA synthetase, TrpRS |
Species |
Clostridium longisporum |
KEGG Pathway |
|
EC number |
6.1.1.2: 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 Q46127
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q46127-F1 | Predicted | AlphaFoldDB |
No variants for Q46127
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q46127 | |||||
No associated diseases with Q46127
1 regional properties for Q46127
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | Aminoacyl-tRNA synthetase, class I, conserved site | 12 - 21 | IPR001412 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.2 | 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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| tryptophan-tRNA ligase activity | Catalysis of the reaction: ATP + L-tryptophan + tRNA(Trp) = AMP + diphosphate + L-tryptophanyl-tRNA(Trp). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| tryptophanyl-tRNA aminoacylation | The process of coupling tryptophan to tryptophanyl-tRNA, catalyzed by tryptophanyl-tRNA synthetase. The tryptophanyl-tRNA synthetase is a class-I synthetase. The activated amino acid is transferred to the 2'-OH group of a tryptophan-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 |
| MAKEIILTGD | RPTGKLHIGH | YVGSLKNRVQ | LQNSGDYRSF | IMIADQQALT | DNARNPEKIR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NSLIEVALDY | LAVGIDPLKS | TILVQSQIPE | LNELTMHYLN | LVTLSRLERN | PTVKAEIKQK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NFENSIPAGF | LIYPVSQAAD | ITAFKATTVP | VGEDQLPMIE | QAREIVRSFN | TIYGKEVLVE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PKAVIPKGTI | GRLPGTDGKA | KMSKSIGNAI | YLADEADVIK | QKVMSMYTDP | NHIKVTDPGQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VEGNTVFTYL | DTFCKDTETL | EEMKAHYSRG | GLGDVKVKKF | LNEILQAELE | PIRNRRKEFQ |
| 310 | 320 | 330 | 340 | ||
| KDIPEVYRIL | KEGSEKAREV | AAGTLKEVRE | TIGIEYFNNI | F |