Q8SRH2
Gene name |
ECU07_1570 |
Protein name |
Probable threonine--tRNA ligase, cytoplasmic |
Names |
Threonyl-tRNA synthetase, ThrRS |
Species |
Encephalitozoon cuniculi (strain GB-M1) (Microsporidian parasite) |
KEGG Pathway |
ecu:ECU07_1570 |
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
1 structures for Q8SRH2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8SRH2-F1 | Predicted | AlphaFoldDB |
No variants for Q8SRH2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8SRH2 | |||||
No associated diseases with Q8SRH2
6 regional properties for Q8SRH2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 320 - 523 | IPR002314 |
| domain | TGS | 1 - 63 | IPR004095 |
| domain | Anticodon-binding | 537 - 605 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 266 - 529 | IPR006195 |
| domain | Threonyl/alanyl tRNA synthetase, SAD | 168 - 217 | IPR012947 |
| domain | Threonine-tRNA ligase catalytic core domain | 240 - 534 | IPR033728 |
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. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| 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). |
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 |
| MYEVKLKVEL | EDKVLEVTQG | TTPYDILCDY | FKDRKDVISC | RIDGVYSDMS | SEILKDCKLE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LMTFEDDGAR | DIFWHSSAHV | LGNALVNLYP | DAKLVHGPPI | EEGFFYDVDV | TDPISSEDYE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KIEEEMVKIM | KKNYRFERVI | KSKEELLEAY | RDNPCKTHFI | MKGVDKESSV | YRNGDFFDMC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LGPHIRSTGV | IKAVKVLKNS | SAYFLNDPNL | KSLQRIYAIT | FPSKGMMDEY | LKRKEEAKER |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DHRKIGTELD | LFFFSKYSPG | SCFFLPNGTT | MYNTLIEFLR | EEYRKRGFKE | VITPNIFCTQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LWEESGHLQN | YKENMFIIEG | DTFALKPMNC | PGHCVMFRHQ | DHSFRDLPLR | LADFGVLHRN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ELSGTLTGLT | RVRRFQQDDA | HIFCTKDQVK | EEIKGCLEFL | SFVYGVFGFR | FELVLSTRPE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KYLGSVDEWD | RAEKALADAM | DESNMPFKIN | AGDGAFYGPK | IDITLHDALG | RRIQCATIQL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DFQLPQRFEL | KYRDSDGQCR | TPVIIHRAIL | GSIERMIAII | LESFGKRLPF | WISPRQIAIV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| NMGNPDYVGK | VRSVLARFRL | DVIDDGNTLS | KRIRTAETSG | YALVCVVGKK | EAEANEINIR |
| 610 | 620 | 630 | |||
| FNKSNRNIGL | YELRDILDRM | ADEKVELDSI | LPIDKVSISK |