Q8TWY1
Gene name |
alaS |
Protein name |
Alanine--tRNA ligase |
Names |
Alanyl-tRNA synthetase, AlaRS |
Species |
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) |
KEGG Pathway |
mka:MK0900 |
EC number |
6.1.1.7: 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 Q8TWY1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8TWY1-F1 | Predicted | AlphaFoldDB |
No variants for Q8TWY1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8TWY1 | |||||
No associated diseases with Q8TWY1
1 regional properties for Q8TWY1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Amidohydrolase-related | 50 - 431 | IPR006680 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.7 | 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. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| alanine-tRNA ligase activity | Catalysis of the reaction: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala). |
| aminoacyl-tRNA editing activity | The hydrolysis of an incorrectly aminoacylated tRNA. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| tRNA binding | Binding to a transfer RNA. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| alanyl-tRNA aminoacylation | The process of coupling alanine to alanyl-tRNA, catalyzed by alanyl-tRNA synthetase. The alanyl-tRNA synthetase is a class-II synthetases. The activated amino acid is transferred to the 3'-OH group of an alanine 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 |
| MKVDPSEFEL | EFFEEIGFER | KRCPECGEYF | WGPPEAEVCN | ETPCVEYSFI | GDPPASVKLD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VWEAGEEFFR | FFERHDHEVL | DRYPVVARWR | DDIHLTIASI | ACFQPWVTSG | EVPPPANPLV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| INQPCIRLND | IDNVGRTGRH | FTLFHMGGHH | AFNNHPHDRR | DIYWKEETVR | LCYEFTVEKL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GIPEEKIAFK | ESWWEGGGNA | GPCFEVVVDG | LELATLVFMQ | YEQVGGEYRE | LPQKIVDTGY |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GIERYAWITT | GEPTAYDAVF | GDLVDATARD | LGVEIDGEAR | EILGELARVA | GLMDVETESD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LRVLRNRVAR | RLDLDVNELV | RVAEPVEFVY | GILDHARCLA | FMLGDGVVPS | NAGEGYLARL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VIRRALRLLD | GLDAEREYLL | EVVERVLEDL | RGTYPELAER | EEYIQDALEC | EIDRYTRALK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RGKKEVRKRL | EEKGELSFED | LVELYDSHGI | PPEVAREIAE | DEGVEVEVPD | DFYSRVAERH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| EGPEEVEEGL | EELERIAVEE | ELPETELAFY | DDEKRLEFKA | EVIGTYEVNG | DAWVVLDRTY |
| 550 | 560 | 570 | 580 | 590 | 600 |
| FYPEGGGQEA | DRGTMRWKDG | EAEVKDVQKV | RGVVFHRIDG | DVPPEGAEVE | CEVDGERRMR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LTRNHTATHV | ILEAARRVLG | DHVWQAGAHK | STDEARLDVT | HHRRISDEEL | REIERLANEI |
| 670 | 680 | 690 | 700 | 710 | 720 |
| VMKDLPVNKR | FMDRNEAERR | YGFELYQGGV | VPGREIRVVE | IEGWNVQACA | GTHCDSTGEI |
| 730 | 740 | 750 | 760 | 770 | 780 |
| GPIKIVGRER | IQDGVERIRF | AAGEAALERI | WETEDLLRET | CEVLRVNPEN | LPKTVKRFFE |
| 790 | 800 | 810 | 820 | 830 | 840 |
| EWKEQRKRIE | RLERELVEAK | LRAAPAEGRR | VGDFTVTLVE | LEDVEVGSVA | GTVEELVKEH |
| 850 | 860 | 870 | 880 | 890 | 900 |
| ENLVLVAKIV | SNGSCQVVVG | SGESAPPAGE | LMREIGKLIE | GGGGGDERLA | QGGGRNPDGL |
| 910 | |||||
| TEDRLVEIVE | DLAGG |