A5UK12
Gene name |
gatE |
Protein name |
Glutamyl-tRNA(Gln) amidotransferase subunit E |
Names |
Glu-ADT subunit E |
Species |
Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS) |
KEGG Pathway |
msi:Msm_0335 |
EC number |
|
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 A5UK12
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5UK12-F1 | Predicted | AlphaFoldDB |
No variants for A5UK12
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5UK12 | |||||
No associated diseases with A5UK12
4 regional properties for A5UK12
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic | 9 - 437 | IPR006075 |
| conserved_site | Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site | 175 - 189 | IPR017958 |
| domain | Asn/Gln amidotransferase | 475 - 617 | IPR018027 |
| domain | GAD domain | 291 - 381 | IPR029351 |
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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| aminoacyl-tRNA ligase activity | Catalysis of the formation of aminoacyl-tRNA from ATP, amino acid, and tRNA with the release of diphosphate and AMP. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| translation | The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDWEKLGLKM | GLEIHQQLNT | KHKLFCPCKT | ELVDEDYNEI | VERNLRPTQS | ELGEIDRAAL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QESLRGLNFK | YESYDHHTCL | VESDDEPPHS | LNKEALEICI | TIAALMNMHI | VDEFHTMRKQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VIDGSNTGGF | QRTGLAATDG | YLDTPYGRVA | IESLGLEEDA | ARRIETTEDY | TEFRLDRLGI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| PLAEITTDPS | MHHPDQVREV | AYMIGQVLRS | TNVKRGLGTI | RQDLNISIEK | GARVEIKGVQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| NLDLMSEIVE | NEVQRQLALI | EIKEELNKRN | AEVLEEIHDL | DSLFENTKSK | ILSSAESIKA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VVLKGFNGLI | GKEVQPGRRF | GTEIASYAKK | RGVSGIFHSD | ELPAYGITQD | EVNSVKDYLN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VGSQDAFIIV | AHDENVAISA | LEEVKRRANL | GFEGVVEETR | KSLDDGNTEY | MRPLPTANRM |
| 430 | 440 | 450 | 460 | 470 | 480 |
| YLETDIPLFK | ITDELVEPIK | NNLPELPDVK | KERIIKEYNL | SEDLASQLVK | RLEADVFEEI |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LTDVEVDPTP | VASLLAYDLR | EIKREGLDID | ILTTRHLKDI | FQLLADSKIA | KDSVTKLTTC |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VIQSPDEEIE | ITAKNNNLTL | LSHEEVTQII | EDIVNKNEAM | VKERQMGAMG | PLMGMSMKEL |
| 610 | 620 | ||||
| KGKADGSIVN | RIVKESIQKM | L |