Q9UZ14
Gene name |
thrS |
Protein name |
Threonine--tRNA ligase |
Names |
Threonyl-tRNA synthetase, ThrRS |
Species |
Pyrococcus abyssi (strain GE5 / Orsay) |
KEGG Pathway |
pab:PAB1490 |
EC number |
6.1.1.3: 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
18 structures for Q9UZ14
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1Y2Q | X-ray | 195 A | A | 1-143 | PDB |
| 2HKZ | X-ray | 210 A | A | 1-143 | PDB |
| 2HL0 | X-ray | 186 A | A | 1-143 | PDB |
| 2HL1 | X-ray | 225 A | A/B | 1-147 | PDB |
| 2HL2 | X-ray | 260 A | A/B | 1-143 | PDB |
| 3PD2 | X-ray | 186 A | A/B | 1-147 | PDB |
| 3PD3 | X-ray | 186 A | A/B | 1-147 | PDB |
| 3PD4 | X-ray | 240 A | A/B | 1-147 | PDB |
| 3PD5 | X-ray | 229 A | A/B | 1-147 | PDB |
| 4RRQ | X-ray | 179 A | A/B | 1-147 | PDB |
| 4RRR | X-ray | 186 A | A/B | 1-147 | PDB |
| 4S02 | X-ray | 195 A | A | 1-143 | PDB |
| 4S03 | X-ray | 205 A | A | 1-143 | PDB |
| 4S0I | X-ray | 236 A | A | 1-143 | PDB |
| 4S0J | X-ray | 210 A | A | 1-143 | PDB |
| 4S0K | X-ray | 210 A | A | 1-143 | PDB |
| 4S0L | X-ray | 250 A | A | 1-143 | PDB |
| AF-Q9UZ14-F1 | Predicted | AlphaFoldDB |
No variants for Q9UZ14
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9UZ14 | |||||
No associated diseases with Q9UZ14
6 regional properties for Q9UZ14
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 288 - 491 | IPR002314 |
| domain | Anticodon-binding | 512 - 602 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 209 - 505 | IPR006195 |
| domain | Threonyl-tRNA synthetase, editing domain, archaea | 1 - 139 | IPR015011 |
| domain | Threonine-tRNA ligase catalytic core domain | 206 - 510 | IPR033728 |
| domain | Threonine-tRNA ligase, class IIa, anticodon-binding domain | 510 - 600 | IPR047246 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.3 | 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 |
|---|---|
| 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. |
| threonine-tRNA ligase activity | Catalysis of the reaction: ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + L-threonyl-tRNA(Thr). |
| tRNA binding | Binding to a transfer RNA. |
| zinc ion binding | Binding to a zinc ion (Zn). |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| threonyl-tRNA aminoacylation | The process of coupling threonine to threonyl-tRNA, catalyzed by threonyl-tRNA synthetase. The threonyl-tRNA synthetase is a class-II synthetase. The activated amino acid is transferred to the 3'-OH group of a threonine-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 |
| MRVLLIHSDY | IEYEVKDKAL | KNPEPISEDM | KRGRMEEVLV | AFISVEKVDE | KNPEEVSLKA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IEEISKVAEQ | VKAENVFVYP | FAHLSSELAK | PSVAMDILNR | VYQGLKERGF | NVGKAPFGYY |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KAFKISCKGH | PLAELSRTIV | PEEARVEEVP | EALRKEEEEL | VSYWYILTPE | GELIEVDKFD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FTGYENLRKF | VNYEIAKNRI | AEKEPPHVKL | MLEHELVDYE | PGSDPGNLRY | YPKGRLIKSL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LEQYVTEKVI | EYGAMEVETP | IMYDFEHPAL | EKYLNRFPAR | QYIVLSGDKR | YFLRFAACFG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QFMIKKDAII | SYRNLPLRMY | ELTRYSFRRE | KRGELSGLRR | LRAFTMPDMH | TLAKDIEQAK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EEFKKQFKLS | MEVLEGVGLT | PEDYEVAIRF | TEDFWKEHKD | FIVELVKLIG | KPVLIEMWKQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RFFYFILKFE | FNFVDNLDKA | AALSTVQIDV | ENAERFGITY | YDENGEEKYP | LILHCSPSGA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IERVMYAILE | KQAKLMNEGK | KPMFPLWLSP | IQVRVIPVSE | EYLDYALYVA | GKLEGAKIRV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DVDDEDERLN | KKIRRAEKEW | IPYIVVVGAR | EKENGTITVR | RREDGKQYET | RIEELIKEIK |
| 610 | 620 | ||||
| EKTEGFPYKP | RPLPLLLSKR | PKFRG |