Q9PJF9
Gene name |
thrS |
Protein name |
Threonine--tRNA ligase |
Names |
Threonyl-tRNA synthetase, ThrRS |
Species |
Chlamydia muridarum (strain MoPn / Nigg) |
KEGG Pathway |
cmu:TC_0870 |
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 Q9PJF9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9PJF9-F1 | Predicted | AlphaFoldDB |
No variants for Q9PJF9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9PJF9 | |||||
No associated diseases with Q9PJF9
7 regional properties for Q9PJF9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 312 - 522 | IPR002314 |
| domain | TGS | 1 - 58 | IPR004095 |
| domain | Anticodon-binding | 535 - 624 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 261 - 528 | IPR006195 |
| domain | Threonyl/alanyl tRNA synthetase, SAD | 164 - 213 | IPR012947 |
| domain | Threonine-tRNA ligase catalytic core domain | 237 - 533 | IPR033728 |
| domain | Threonine-tRNA ligase, class IIa, anticodon-binding domain | 533 - 623 | 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 |
| MIHVTCNQEA | FELPEGASAM | DLASKMKNSH | CFAGALINDQ | EKDLSTTLKD | GDTVLFLTWD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DPQGREIFLH | TSAHILAQAV | LRLWPSAQPT | IGPVIDQGFY | YDFANLSISE | EDFPAIEAMA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KAIAEEKLAI | SRQVFSDKEE | TLAYFSDNPF | KIELITELPE | EATISAYKQG | EFLDLCRGPH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LPSTAPVKAF | KLLRTSAAYW | RGDPSKESLI | RIYGIAFPTT | KELKEHLHQL | EEAKKRDHRV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LGTKLDLFSQ | QSYSAGMPFF | HPRGMVIWNA | LIDYWKRLHQ | LAGYQQIQTP | QLMSRELWEI |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SGHWENYKEN | MYTLTVDEED | YAIKPMNCPG | CMLYYKTQLH | SYREFPLRIA | EIGHVHRHEL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| SGALSGLMRV | RTFHQDDAHV | FLTPEQVEEE | TLNILNLVSE | LYGTFGLDYH | LELSTRPEQG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TIGSDDLWEL | ATEALKNALV | KSQKPFIISP | GEGAFYGPKI | DIHVKDAINR | TWQCGTIQLD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| MFLPERFDLK | YTNPQGEKST | PIMLHRALFG | SIERFLGILI | EHFKGRFPLW | LSPEHVRIIT |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VADRHEARAQ | ELAKYFTQQG | ILATVDQASE | SVSKKIRNAQ | NMQVNYMITI | GDKELETQLL |
| 610 | 620 | 630 | |||
| AVRTRDNRVL | NDISVEHFTN | TILEELRSLS | LTSSL |