Q63TM7
Gene name |
pheT |
Protein name |
Phenylalanine--tRNA ligase beta subunit |
Names |
Phenylalanyl-tRNA synthetase beta subunit, PheRS |
Species |
Burkholderia pseudomallei (strain K96243) |
KEGG Pathway |
bps:BPSL1940 |
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 Q63TM7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q63TM7-F1 | Predicted | AlphaFoldDB |
No variants for Q63TM7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q63TM7 | |||||
No associated diseases with Q63TM7
6 regional properties for Q63TM7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | tRNA-binding domain | 39 - 147 | IPR002547 |
| domain | Ferrodoxin-fold anticodon-binding domain | 698 - 791 | IPR005121 |
| domain | B3/B4 tRNA-binding domain | 211 - 384 | IPR005146 |
| domain | tRNA synthetase, B5-domain | 400 - 475 | IPR005147 |
| domain | Phenylalanly tRNA synthetase, tRNA-binding-domain | 45 - 146 | IPR033714 |
| domain | Phenylalanyl tRNA synthetase beta chain, core domain | 473 - 686 | 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 |
|---|---|
| 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. |
| 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 |
| MQFPESWLRT | FVDPQLTTDE | LSHALTMAGL | EVESLRPAAP | PTEKIVVGRV | LEVVKHPDAD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KLNVCQVDAG | TGATLQIVCG | APNVAPGIKV | PVALVGAKLP | PAEEGGAPFA | IKLSKLRGVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SQGMLCSARE | LKLSEDHSGL | MILPEGTPVG | QDIREALNLD | DTVFEIKLTP | NKADCLSVFG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IARETAAITG | APLAAPDIRP | VLAELTETLP | VKISAPDLCG | RFSGRVIRGV | NARAKTPHWM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VERLERAGQR | SVSALVDISN | YVMFELGRPS | HVFDLDKIHG | GIDVRWGKRG | ESLKLLNGNT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IELDETVGVI | SDGAQVESLA | GIMGGDSTAV | TLDTTNIYLE | AAFWWPDSIR | GRARKYNFST |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DAAHRFERGV | DYSTTVEHVE | RITQLILDIC | GGQAGPVDDQ | IVSLPQRAPV | SMRASRANRI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IGVEIGEDEI | AQIFTRLGLA | FERDGDVFRV | TPPPHRFDIE | IEEDLIEEVA | RIYGFEKIPA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| RPPVAKSEMR | ATDETRRSVH | AIRHALAARD | YAETVNFSFV | DAEWERDFAG | NDNPVRLLNP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| IASQLSVMRT | TLFGSLVGVL | RHNLNRRAER | VRVFEAGRVF | VADPSVKAGE | LAVEGYAQPK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RIGALAYGPV | VEEQWGTATR | QVDYFDVKGD | LEALLAPVPA | RFVKAEHPAL | HPGRSARIEV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| DGHAVGWIGE | LHPRLMQKYE | LPHAPVMFEI | DTDALVARAL | PAPSEVSKFP | PVRRDIAVVV |
| 730 | 740 | 750 | 760 | 770 | 780 |
| DQKVEVQALF | DEMKKALADD | ACKFVQRVAL | FDEFRAKSNT | SGGLSAHEKS | LAFRVTLQDA |
| 790 | 800 | ||||
| AGTLQDETVD | QAIQTLVDRM | ARVYGARLRG |