Q67LA3
Gene name |
thrS |
Protein name |
Threonine--tRNA ligase |
Names |
Threonyl-tRNA synthetase, ThrRS |
Species |
Symbiobacterium thermophilum (strain T / IAM 14863) |
KEGG Pathway |
sth:STH2558 |
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 Q67LA3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q67LA3-F1 | Predicted | AlphaFoldDB |
No variants for Q67LA3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q67LA3 | |||||
No associated diseases with Q67LA3
7 regional properties for Q67LA3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 324 - 530 | IPR002314 |
| domain | TGS | 1 - 64 | IPR004095 |
| domain | Anticodon-binding | 542 - 629 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 233 - 535 | IPR006195 |
| domain | Threonyl/alanyl tRNA synthetase, SAD | 172 - 221 | IPR012947 |
| domain | Threonine-tRNA ligase catalytic core domain | 245 - 540 | IPR033728 |
| domain | Threonine-tRNA ligase, class IIa, anticodon-binding domain | 540 - 630 | 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| metal ion binding | Binding to a metal ion. |
| 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. |
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 |
| MSSVVHVTLP | DGSVREYPQG | ITIAEAVAQI | GPRLAKAALA | AKVDGRLVDL | SARLEKDCTL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QVLTFKDEEG | REVFRHTSTH | IMAQAVKRLF | PEAKLTVGPP | LENSFYYDFD | LPRPLTPEDL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EKIEAEMAKI | VEADYPIVRQ | EVDREEAKRF | FAERGEDYKV | LLVDKIPEDE | VVSIYTQGEF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TDLCVGPHLP | STGRVKAFKL | LSVAGAYWEG | NQANKQLQRV | YGTSFESKKD | LEDYLFRLEE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ARRRDHRRLG | PELGLYRFEE | VAPGFAFWLD | KGYRLYRELE | NWSRKLQEAR | GYEEVSTPWI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VSSKLYETSG | HWQHYRQNMF | EIRAEDQDFA | TKPMNCPCHC | VLYKSQIRSY | RDLPLKIAEY |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GPLSRFEASG | TLHGLLRVRG | FHQDDAHLFV | RPDQIEEQIR | EVIGLVDTIY | GTLGLEYEIK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LSTRPEDFMG | DIELWNEAEA | ALARALDGMG | RSYKLNPGDG | AFYGPKLDFD | VTDALGRKWQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| CATVQLDFQL | PIKFDLTYIG | EDGKEHRPVM | IHRAIMGTLE | RFIGILTEHY | AGNFPLWMAP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VQARVLPITD | RHHAYAGEVV | AKLQEAGLRV | EGDYRNEKVG | YKIREAELLK | IPFILVVGDK |
| 610 | 620 | 630 | 640 | 650 | |
| EAEAGAVAVR | RRGMKDLGPM | PLADFLALAQ | SEIASKAMDE | ACRKAASGTR | D |