Q0IDK4
Gene name |
hisS |
Protein name |
Histidine--tRNA ligase |
Names |
Histidyl-tRNA synthetase, HisRS |
Species |
Synechococcus sp (strain CC9311) |
KEGG Pathway |
syg:sync_0232 |
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 Q0IDK4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q0IDK4-F1 | Predicted | AlphaFoldDB |
No variants for Q0IDK4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q0IDK4 | |||||
No associated diseases with Q0IDK4
4 regional properties for Q0IDK4
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 |
| MSQLQTLRGM | VDLLPEQTRR | WQAVESVARE | HFRCAGLDEI | RTPLLEFTDL | FARGIGEGTD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VVGKEMYTFL | DRGDRSCTLR | PEGTASVVRA | ALQHGLLSQG | AQRLWYGGPM | FRYERPQAGR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QRQFHQIGVE | FLGASSPRSD | AEVIALAWDL | LTDLGIQGLN | LEINSLGTPD | DRQRFRSELV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QWLEERVEQL | DAESQARLTT | NPLRILDSKD | KGTQQLLNDA | PTLLKALSKE | SVDRFEQVCA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LLTALQIPYQ | LNPRLVRGLD | YYGHTAFEIT | SDQLGAQATV | CGGGRYDGLI | QQLGGPVTPA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IGWALGMERL | LLVISAAAQA | DPDGAAARLT | ATPSPLVYVI | NRGEQAEPQA | LSLARQWRGA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLAVELDGSS | ASFGKQFKRA | DRSGAPWAVV | LGDEEASAGQ | VRLKPLRGEG | EEKQLTWEDA |
| LSYLMKQR |