Q2W3D5
Gene name |
aspS (amb2837) |
Protein name |
Aspartate--tRNA(Asp/Asn) ligase |
Names |
Aspartyl-tRNA synthetase, AspRS, Non-discriminating aspartyl-tRNA synthetase, ND-AspRS |
Species |
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264) |
KEGG Pathway |
mag:amb2837 |
EC number |
6.1.1.23: 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 Q2W3D5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2W3D5-F1 | Predicted | AlphaFoldDB |
No variants for Q2W3D5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2W3D5 | |||||
No associated diseases with Q2W3D5
6 regional properties for Q2W3D5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 118 - 558 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 18 - 99 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 138 - 555 | IPR006195 |
| domain | GAD domain | 307 - 406 | IPR029351 |
| domain | Aspartate-tRNA ligase, type 1, anticodon recognition domain | 2 - 134 | IPR047089 |
| domain | Aspartate-tRNA ligase, type 1, core domain | 138 - 558 | IPR047090 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.23 | 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. |
4 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). |
| aspartate-tRNA(Asn) ligase activity | Catalysis of the reaction: tRNA(Asx) + L-aspartate + ATP = aspartyl-tRNA(Asx) + diphosphate + AMP. |
| 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 |
| MAATDTPWRP | FRQAGALRRP | MIDPAFVQGH | PAYPDAFAQF | FAGHGRYGHF | AERVGNRNSR |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NGWRRRALAP | GPAVGAEIVA | RHHEAAAQAG | QGGDAARHQH | RVDRLGQHHV | RAAFEQVGRH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| FRLRGRSEHD | RHRKGIVGAD | SPAHPPHQIA | RLLHAEIRVH | HQKVDHFRPE | VVFGIVAVVK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AQQIPASQHA | KGAGDDITAA | EVEIAQQGAH | TWGVVGHGLP | SWQERTTFWP | PAFRSPSDRS |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ATSEFVAGLV | NIGLSRLDKI | WPGMPSSRFG | FKRAYEGFMH | VYRSHTCGQL | KAADAGIQAR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSGWVHRKRD | HGNLLFVDLR | DHYGITQCVI | DVSSPVFAAL | DKARPESVIT | VTGKVVKRSA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ETINPRLPTG | EIELQVAEVE | IQSIADVLPI | QVAGDQEYPE | DMRLRYRFLD | LRREDVHANM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MLRSRVIAYL | RQAMIGQGFT | EFQTPILTAS | SPEGARDYLV | PSRIHPGKFY | ALPQAPQQFK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QLLMVAGFDK | YFQIAPCFRD | EAGRADRSPG | EFYQLDFEMS | YVTQDDVFAA | IEPVLEGVFK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| EFGKGRAVTP | APFPRITYAD | SMLKYGSDKP | DLRNPIIIAD | VTEPFRGSGF | GLFAKLVDKG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| AVVRAIPAPG | AAGQPRSWFD | KLNDWARENG | AGGLGYIQFA | ADGPKGPIAK | NLEPARVEAI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| KAAANLKDGD | AVFFACDKAL | PAAKFAGLVR | TKIGNELDLL | EKDVFKFCWT | VDFPMYEINE |
| 730 | 740 | 750 | 760 | 770 | 780 |
| ETGLVEFSHN | PFSMPQGGMD | ALLNQDPLTI | NAYQYDIVCN | GVELSSGAIR | NHRPDIMYKA |
| 790 | 800 | 810 | 820 | 830 | 840 |
| FEIAGYSAAH | VEEHFGGMLN | AFKFGAPPHG | GSAPGVDRIV | MLLADQPNIR | EIILFPMNQQ |
| 850 | 860 | 870 | |||
| AQDLLMQAPA | EIAMERLREL | HIKVDLPKPK | KEVKEG |