Q7NI42
Gene name |
gatB |
Protein name |
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
Names |
Asp/Glu-ADT subunit B |
Species |
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421) |
KEGG Pathway |
gvi:gll2342 |
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 Q7NI42
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q7NI42-F1 | Predicted | AlphaFoldDB |
No variants for Q7NI42
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7NI42 | |||||
No associated diseases with Q7NI42
3 regional properties for Q7NI42
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| glutamyl-tRNA(Gln) amidotransferase complex | A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms. |
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 |
| MTSTAPPKVQ | YEAVIGLEVH | VQLSTETKLF | CRCSTRFGNT | PNTNICPICT | GQPGTLPVLN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QQALDYAVLT | ASALNCQIHP | QGLSKFDRKQ | YFYPDLPKNY | QISQYDLPLA | ERGWLEIEVE |
| 130 | 140 | 150 | 160 | 170 | 180 |
| GEPAKRIGIT | RLHMEEDAGK | LVHAGADRLS | GSTHSLVDFN | RAGVALCEIV | SEPDIRTAAE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AAAYAGELRR | IVRYLGVCDG | NMQEGSLRFD | LNISVRPAGE | GKFGTKVEIK | NLNSFNSLQR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AVEYEFARQV | DCLLSGERIV | QETRLWDEAT | QRTISMRSKE | EANDYRYFPE | PDLVPIALNG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| TQIDAYRQRL | GELPAQKRHR | YRETLGLSSY | DAGVLTDERE | VAEYFEQVVA | LGIPAKQAAN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FVSGAVAAHL | NETRRSISQI | KVTPEVSAEL | LALINQGIIS | NRIANELLPD | LFEKGGSPRA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LVEERGLTQI | SDRGQLEQIV | DEVLAGESDS | VAAYRGGRTK | LLGFFVGKVM | KKTAGRADPQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VVNDLLQSKL | AEQPTAPPPE | PESAAETPEA | PPAVEDAPPE | APTEAITAEA | GSAEAITAAS |
| 550 | |||||
| EEPDTPVSHQ | DAHA |