B4RE95
Gene name |
thrS |
Protein name |
Threonine--tRNA ligase |
Names |
Threonyl-tRNA synthetase, ThrRS |
Species |
Phenylobacterium zucineum (strain HLK1) |
KEGG Pathway |
pzu:PHZ_c0423 |
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 B4RE95
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B4RE95-F1 | Predicted | AlphaFoldDB |
No variants for B4RE95
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B4RE95 | |||||
No associated diseases with B4RE95
7 regional properties for B4RE95
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (G/ P/ S/T) | 318 - 530 | IPR002314 |
| domain | TGS | 1 - 61 | IPR004095 |
| domain | Anticodon-binding | 542 - 629 | IPR004154 |
| domain | Aminoacyl-tRNA synthetase, class II | 243 - 535 | IPR006195 |
| domain | Threonyl/alanyl tRNA synthetase, SAD | 169 - 219 | IPR012947 |
| domain | Threonine-tRNA ligase catalytic core domain | 242 - 540 | IPR033728 |
| domain | Threonine-tRNA ligase, class IIa, anticodon-binding domain | 540 - 614 | 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 |
| MIELVFPDGS | KREFPDGVTG | REIAAGISKS | LEKKAILVEV | DGELLDLERP | LEKGGAFKIL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| TREAPEALET | IRHDVSHILA | EAVQELFPGT | QVTIGPAIED | GFYYDFAREE | PFSLDDLAKI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EQRMKEIVDR | DEPIRREEWD | RDEAIRHFRE | IGEEYKAQII | EAIPAGEKIT | VYRQGQWKDL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| CRGPHLPSTR | HAGKAFKLTK | LAGAYWRGDH | RNAQLQRIYG | TAWASEADLE | AYIQRLEEAE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KRDHRKLGRQ | MDLFHMQEEG | KGMVFWHEKG | LTLWRTVESY | VRRRLDEAGY | QEVRTPQVLD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RVFWEKSGHW | DKYRPNMFVC | ETEEGEELSL | KPMNCPGHVQ | IFKFGQKSYR | DLPLRMAEFG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ACHRYEPSGA | LHGLMRVRAF | TQDDAHIFCR | EDQIEEETAR | FIELANSIHA | DFGLERDHIA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LATRPEVRAG | SDEFWDKAEA | QMLAAARKAG | VEPVIAEGDG | AFYAPKLDWV | LKDSIGRTWT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| CGTIQLDYVL | PERLGAEYVA | EDGSKQRPVM | LHRAICGSLE | RFIGVLIENY | AGAFPLWLAP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VQVVVATITS | DADDYARAAA | AELKAKGLRV | ELDLRNEKIN | YKVREHSLAK | VPVIAVVGRR |
| 610 | 620 | 630 | 640 | 650 | |
| EAEEGKVALR | RLGSDGQQIL | ALGEAAEALA | MEALPPDLAR | KRQDGGVQAG | LGGEREAG |