Q9WZS9
Gene name |
pheT (TM_0822) |
Protein name |
Phenylalanine--tRNA ligase beta subunit |
Names |
Phenylalanyl-tRNA synthetase beta subunit, PheRS |
Species |
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
KEGG Pathway |
tma:TM0822 |
EC number |
6.1.1.20: 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 Q9WZS9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9WZS9-F1 | Predicted | AlphaFoldDB |
No variants for Q9WZS9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9WZS9 | |||||
No associated diseases with Q9WZS9
6 regional properties for Q9WZS9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | tRNA-binding domain | 39 - 147 | IPR002547 |
| domain | Ferrodoxin-fold anticodon-binding domain | 694 - 787 | IPR005121 |
| domain | B3/B4 tRNA-binding domain | 211 - 384 | IPR005146 |
| domain | tRNA synthetase, B5-domain | 399 - 472 | IPR005147 |
| domain | Phenylalanly tRNA synthetase, tRNA-binding-domain | 45 - 146 | IPR033714 |
| domain | Phenylalanyl tRNA synthetase beta chain, core domain | 474 - 680 | IPR041616 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.1.1.20 | 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 |
|---|---|
| phenylalanine-tRNA ligase complex | An enzyme complex that catalyzes the ligation of phenylalanine to tRNA(Phe), forming L-phenylalanyl-tRNA(Phe). |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| magnesium ion binding | Binding to a magnesium (Mg) ion. |
| phenylalanine-tRNA ligase activity | Catalysis of the reaction: ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + L-phenylalanyl-tRNA(Phe). |
| tRNA binding | Binding to a transfer RNA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| phenylalanyl-tRNA aminoacylation | The process of coupling phenylalanine to phenylalanyl-tRNA, catalyzed by phenylalanyl-tRNA synthetase. The phenylalanyl-tRNA synthetase is a class-II synthetase. However, unlike other class II enzymes, The activated amino acid is transferred to the 2'-OH group of a phenylalanine-accepting tRNA. The 2'-O-aminoacyl-tRNA will ultimately migrate to the 3' position via transesterification. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRVPESWLRE | FVDLDWDIEQ | IAERLTFSGT | SVEDILRPFN | VSGEIITARV | IERFDHPASE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KLIVCKVDTG | KRIYTVITAD | KTVNEGDYVI | LALEGATLNN | GLKIEPREFK | GVISEGMLCS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LEELGLEEKS | DRVYRFPDPV | ELGVNVVEEY | GLNERVLDIE | ITPNRPDCLS | IIGVARELSA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LSGRPLNKPQ | PDVSFVDEDV | QFDVEIEDVE | GCPRYSARIM | KGVTVKDSPL | WMKARLVAAG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VRSLNNVVDA | TNYVMIELGH | PVHAFDLNRL | KNKRIVVKSA | KGGERVLLLD | EKEYELKGGE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VLITDGENVL | ALGGIMGGME | SGVYDDTRDL | VLEVAYFDPV | RIRKAAKALG | ISSESSYRFE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RGVDPNDVEL | VSLRLAELIQ | KLAGGYVLRK | FWDVYPRKIE | PKKVMLRKAR | IEKILGTKVE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EPGDILRRLE | FQVEDRGDSY | EVLVPTFRPD | VEREIDLIEE | IGRIYGYEKV | ESKVISVPAV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NRGWGEKQLF | RREISQFMKG | MGFDEVVTFS | FVDSQKVKKW | PLVDREPIAL | SNPIASDMDV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| MRTSQFYSLI | QVLAENFKRQ | NRDLKLFEIG | KIYFKENGNF | REIETLSAMS | CGLENPGDYT |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DKRSVSFYTI | KGVLDELFFR | LGVNVVYRAA | EIPGLFPTRS | ARIYVENREI | GFIGMVDPKL |
| 670 | 680 | 690 | 700 | 710 | 720 |
| LDEYDVKEDT | YFFEIDMELL | RKYASKRPAY | RPTPRFPAVR | RDISFLLPKG | FESVKIIELF |
| 730 | 740 | 750 | 760 | 770 | 780 |
| KKSGGDLVEE | VGVFDIYEGK | GIPENMVSVT | LYVVFRHPER | TLTDEEVNKI | FEEMVQKAER |
| EFGIRRRF |