Q46ZI4
Gene name |
hisS |
Protein name |
Histidine--tRNA ligase |
Names |
Histidyl-tRNA synthetase, HisRS |
Species |
Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator (strain JMP 134)) |
KEGG Pathway |
reu:Reut_A2085 |
EC number |
6.1.1.21: 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 Q46ZI4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q46ZI4-F1 | Predicted | AlphaFoldDB |
No variants for Q46ZI4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q46ZI4 | |||||
No associated diseases with Q46ZI4
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.21 | 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. |
| histidine-tRNA ligase activity | Catalysis of the reaction: ATP + L-histidine + tRNA(His) = AMP + diphosphate + L-histidyl-tRNA(His). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| histidyl-tRNA aminoacylation | The process of coupling histidine to histidyl-tRNA, catalyzed by histidyl-tRNA synthetase. The histidyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3''-OH group of a histidine-accetping tRNA. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTQNENPSAQ | SGAKPEDKAR | PAKALQGVKG | MNDMLPADAP | LWEHFENAAR | AMLRAYGYQQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IRTPIVEHTQ | LFVRGIGEVT | DIVEKEMYSF | TDALNGEQLT | LRPEGTAAAV | RATIEHNLLY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DGPKRLWYTG | PMFRHERPQR | GRYRQFHQLG | AEALGFAGPD | VDAEIILMCQ | RLWDDLGLTG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| VRLEINSLGQ | AHERAAHREE | LIKYLEGFKD | ILDEDGKRRL | YTNPLRVLDT | KNPALQEMAA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NAPKLIDFLG | EESLAHFEGV | QRLLKANNIP | YKINPRLVRG | LDYYNLTVFE | WITDKLGAQG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TIAGGGRYDP | LIAQMGGKAA | PACGWAMGIE | RIIELIREEG | VVPDAVGCDV | YLVHQGEAAQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QQATVAAERL | RDAGLDVVLH | ATPDGKSGSF | KSQMKRADAS | GAAYAVIIGE | DEVAAGVVQV |
| 430 | 440 | 450 | |||
| KELRQGAQAE | GGGQQAQVPA | ENLVDYLIDA | MVGASE |