P43817
Gene name |
aspS |
Protein name |
Aspartate--tRNA ligase |
Names |
Aspartyl-tRNA synthetase, AspRS |
Species |
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd) |
KEGG Pathway |
hin:HI_0317 |
EC number |
6.1.1.12: 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 P43817
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P43817-F1 | Predicted | AlphaFoldDB |
No variants for P43817
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P43817 | |||||
No associated diseases with P43817
6 regional properties for P43817
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 119 - 559 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 19 - 102 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 139 - 556 | IPR006195 |
| domain | GAD domain | 308 - 407 | IPR029351 |
| domain | Aspartate-tRNA ligase, type 1, anticodon recognition domain | 3 - 135 | IPR047089 |
| domain | Aspartate-tRNA ligase, type 1, core domain | 139 - 559 | IPR047090 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.12 | 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aspartate-tRNA ligase activity | Catalysis of the reaction: ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-aspartyl-tRNA(Asp). |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| nucleic acid binding | Binding to a nucleic acid. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| aspartyl-tRNA aminoacylation | The process of coupling aspartate to aspartyl-tRNA, catalyzed by aspartyl-tRNA synthetase. The aspartyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of an aspartic acid 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 |
| MMRTHYCGAL | NRNNIGQDVT | LSGWVHRRRD | LGGLIFIDMR | DRDGIVQVCF | DPKYQDALTA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AAGLRNEFCI | QIKGEVIARP | DNQINKNMAT | GEVEVLAKEL | RIYNASDVLP | LDFNQNNTEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QRLKYRYLDL | RRPEMAQRLK | TRAKITSFVR | RFMDDNGFLD | IETPMLTKAT | PEGARDYLVP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SRVHKGKFYA | LPQSPQLFKQ | LLMMSGFDRY | YQIVKCFRDE | DLRADRQPEF | TQIDVETSFL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TAPEVREIME | RMVHGLWLDT | IGVDLGKFPV | MTWQEAMRRF | GSDKPDLRNP | LEMVDVADIV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KDVEFKVFNE | PANNPNGRVA | VIRVPNGAEI | TRKQIDEYTQ | FVGIYGAKGL | AWAKVNDINA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GLEGVQSPIA | KFLNEDVWKG | LAERVNAQTG | DILFFGADKW | QTTTDAMGAL | RLKLGRDLGL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TRLDEWQPLW | VIDFPMFERD | EEGNLAAMHH | PFTSPKDFSP | EQLEADPTSA | VANAYDMVIN |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GYEVGGGSVR | IFDPKMQQTV | FRILGIDEEQ | QREKFGFLLD | ALKFGTPPHA | GLAFGLDRLT |
| 550 | 560 | 570 | 580 | ||
| MLLTGTENIR | DVIAFPKTTA | AACLMTEAPS | FANPQALEEL | AISVVKAE |