Q12PX7
Gene name |
alaS |
Protein name |
Alanine--tRNA ligase |
Names |
Alanyl-tRNA synthetase, AlaRS |
Species |
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013) |
KEGG Pathway |
sdn:Sden_1213 |
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 Q12PX7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q12PX7-F1 | Predicted | AlphaFoldDB |
No variants for Q12PX7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q12PX7 | |||||
No associated diseases with Q12PX7
4 regional properties for Q12PX7
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. |
4 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). |
| 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 |
| MFETTAKLRS | AFLAYFETQG | HQVVDSSSLV | PHNDPTLLFT | NAGMNQFKDV | FLGMDKRSYS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RAVSSQRCVR | AGGKHNDLDN | VGYTARHHTF | FEMLGNFSFG | DYFKEEAIRF | AWTFLTETLK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LPTERLCVTI | YETDDEAFEL | WNKKIGVAAE | NIIRIGDNKG | APYASDNFWQ | MGDTGPCGPC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| SEIFYDHGDH | IWGGRPGTPE | EDGDRFIEIW | NIVFMQYNRQ | ADGAMLPLPK | PSVDTGMGIE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RIAAIMQGVH | SNYEIDIFKQ | LIAKTAEIIG | VSDLENKSLR | VIADHIRSCA | FLIADGVMPS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| NEGRGYVLRR | IIRRAVRHGN | KLGATDTFFY | KLVPTLISVM | GDAAKGLVET | QVIVEKALKA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EEEQFARTLE | RGLGLLDNAL | NELSGKVLDG | DTAFKLYDTY | GFPVDLTADV | CRERDITVDE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| AGFEAAMAEQ | RSRAQAAGNF | GADYNKQLII | DEETQFCGYK | GLSGEANVVA | LYLDGQAVNE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VTQGQDAVVV | LNNTPFYAES | GGQVGDKGVL | SAQGINFSVT | DTQKFGQATG | HQGKVLEGSI |
| 550 | 560 | 570 | 580 | 590 | 600 |
| KVGTKLAAEV | NKDLRQRTEL | NHSVTHLLHA | ALRQVIGTHV | TQKGSLVNPE | RLRFDFAHFE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GVKAAELKQV | EELVNAQIRC | NHELNTAEMA | IDEAKEKGAM | ALFGEKYDEK | VRVVTMGDFS |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IELCGGTHVG | RTGDIGLFKI | TSEAGIAAGV | RRIEAVTGAA | AMAYVAEQQA | MLDEAAGLLK |
| 730 | 740 | 750 | 760 | 770 | 780 |
| SDSASVVAKL | KAQLDKTKQL | EKELSQLKDK | LAAAASADMA | GDAQDINGVK | VLVKKLEGVD |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PGSLRGLQDE | LKQKLKSAII | LLGTAKDGKV | NLIAGVSNDL | TAKVKAGELV | AMVAQQVGGK |
| 850 | 860 | 870 | |||
| GGGRPDMAQA | GGTQVENLDA | ALASASTWIA | ERLA |