Q8THJ0
Gene name |
gatB |
Protein name |
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
Names |
Asp/Glu-ADT subunit B |
Species |
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A) |
KEGG Pathway |
mac:MA_4524 |
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 Q8THJ0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8THJ0-F1 | Predicted | AlphaFoldDB |
No variants for Q8THJ0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8THJ0 | |||||
No associated diseases with Q8THJ0
3 regional properties for Q8THJ0
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity | Catalysis of the reaction: L-glutamine + aspartyl-tRNA(Asn) + ATP = L-glutamate + asparaginyl-tRNA(Asn) + phosphate + ADP. |
| 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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| glutaminyl-tRNAGln biosynthesis via transamidation | A tRNA aminoacylation process in which glutaminyl-tRNAGln is formed by a tRNA-dependent two-step pathway. In the first step a non-discriminating glutamyl-tRNAGlx synthetase generates the misacylated L-glutamyl-tRNAGln species, and in the second step it is amidated to the correctly charged L-glutaminyl-tRNAGln by a glutamyl-tRNAGln amidotransferase. |
| 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 |
| MVYENPDGIR | IGLEIHVQLN | KLKTKMFCGC | STDYHNAAPN | THTCPICLGL | PGTLPVLNKK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VVEAAIKVGL | ALEGEIAEET | QFHRKNYFYP | DLPKGFQVTQ | YDYPIVSKGK | VVIEGEDGEH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VVGITRAHME | EDPGKLVHIG | SIGKSKGVLI | DYNRSGMPLI | ETVTEPDMRS | PKEARRFLDK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| FRNILEYLDV | FDGNLEGAMR | VDANVSVHWG | TRVEVKNISS | HKGVERALLY | EIMRQKNVIR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RGGTIVQETR | HFDEGRGVTL | SMRTKEEAED | YRYFREPDLM | PMRITDWIPA | IKETLPELPD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| AKRTRFIEQY | GITDMHARAL | TSKIMLADFY | EGVCAKGVDP | KIAATWTADV | FLGELNYRDL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AISSYGGKTI | GFIHAKDPEV | ENSFKGSDMV | ELVTLFAEGK | ISDRAAVEVI | RTILDGTEEK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TPSQIIEEKG | LFKAEDDLVT | KAVAETIAEN | AAAVQDYLGG | TEKSLNFLVG | QVMKKTKGTA |
| 490 | |||||
| DAKTARELIL | KELKG |