A5UM78
Gene name |
gatB |
Protein name |
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
Names |
Asp/Glu-ADT subunit B |
Species |
Methanobrevibacter smithii (strain ATCC 35061 / DSM 861 / OCM 144 / PS) |
KEGG Pathway |
msi:Msm_1101 |
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 A5UM78
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5UM78-F1 | Predicted | AlphaFoldDB |
No variants for A5UM78
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5UM78 | |||||
No associated diseases with A5UM78
No regional properties for A5UM78
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for A5UM78 | |||
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. |
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 |
| MMCGLEIHVQ | LETESKLFCD | CPTNYKEAPA | NSNICPVCLN | QPGAKPYPTN | EKAIENALMI |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLMLNCKIDK | GFTYFMRKHY | DYPDLPSGYQ | RTSVPIGYEG | ELNGVRIREI | HMEEDPGQYK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PDRGTVDFNR | SGIPLIEIVT | EPDIKSPEEA | RTFLKELIRV | LQYSGGARGE | GTMRADVNIS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IEGGNRVEMK | NINSIKGAYK | ALKFELVRQK | NLMKRGVEIK | QETRAYLESQ | MITVGMRLKE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DADDYRFIPD | PDLPPMEISD | AQIENVLEIM | PEAPHNKVRR | FTEEYGIDAE | SAKVLTSELD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LAIAYEAVAK | QVDPKFASMW | MRDELKRVLS | YNKLDFADSG | ILVEDIVELL | EMLQNKEITT |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KAGQRIIEHM | PNNKQTPKAI | AEELGLLGVV | KDDEVIAAVK | QAIEENPKAV | NDYLEGQKSS |
| 430 | 440 | ||||
| LNFLVGQVMR | LTRGKADPGE | TVKILKENIE |