Q9X1B6
Gene name |
alaS |
Protein name |
Alanine--tRNA ligase |
Names |
Alanyl-tRNA synthetase, AlaRS |
Species |
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
KEGG Pathway |
tma:TM1396 |
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 Q9X1B6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9X1B6-F1 | Predicted | AlphaFoldDB |
No variants for Q9X1B6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9X1B6 | |||||
No associated diseases with Q9X1B6
4 regional properties for Q9X1B6
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 |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
6 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). |
| amino acid binding | Binding to an amino acid, organic acids containing one or more amino substituents. |
| 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). |
2 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. |
| tRNA modification | The covalent alteration of one or more nucleotides within a tRNA molecule to produce a tRNA molecule with a sequence that differs from that coded genetically. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRYMTSEEIR | EAFLKFFEKK | GHKILPSASL | IPDDPQLLFT | VAGMVPFKPI | FWGKVEPVYT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RVATCQKCLR | TVDIENVGKT | PRHHTFFEML | GNFSFGDYFK | EEAIEWAWEF | LTQVLGVPEE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KLWVSVYEED | EEAFRIWNEK | IGLPEKRILR | MGKEDNFWGP | AGPTGPCGPD | TEIFYDTGYS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KGCPEGEGCT | PANSEGRFVE | IWNLVFTEYY | QDEEGKLHPL | PRKNIDTGAG | LERFCAMMQG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VYSNFDTDLF | QPIIKRIEEL | TGVGYKTDEE | KDVSIRVIAD | HIRAITFLIS | EGVFPSNEGR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GYVLRRIIRR | AMRHGILLGM | SEPFLYRIVD | AVVEKMGKVY | PEIVRGEGMV | KEVLSAEENR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FLKTLEQGMK | VFDEIVEKKG | KIDSEDAFRL | YDTYGLPLEL | TLEIAKEKGV | EVDVQEFNKY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MEEQQRKSRA | AMGDVEFARR | YEYLEKLPKD | FRTEFTGYEK | LEDEGEVVLV | ARDDETVEEA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SEGTVEVVFS | RTPFYAEKGG | QVSDTGMVEW | RDGKALVEYV | FEASEGVIVH | RIKILDGTLR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RGQKVILRVD | KKRREATMRN | HTATHLLHAA | LKKVLGDHVR | QAGSLVAPDR | LRFDFTHFKG |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LSSAEIEQVE | DLVNEWIMEA | IPVEVRYTSY | EEAVKSGVVA | LFTEKYGDVV | RVVEVPGVSK |
| 670 | 680 | 690 | 700 | 710 | 720 |
| ELCGGTHVKN | TGQIGLFKII | SEESVSSGVR | RIEAVTGFSA | LELLRNQKKL | IDQLKEILGA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| REDELTDRVL | SLREKVKELE | KKLSQGRISE | ERIAMKQLED | GVKVFHGVFE | GVEAKHLGGI |
| 790 | 800 | 810 | 820 | 830 | 840 |
| ADNVLKKEGE | GIVILFSKFE | NKVSLVVKVS | ENLLGKYDAS | SIARNIAKEL | GGNGGGRKNF |
| 850 | 860 | ||||
| AQAGGRHPER | IKDVLERLEE | FLR |