Q2JNH3
Gene name |
gatB |
Protein name |
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B |
Names |
Asp/Glu-ADT subunit B |
Species |
Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium Yellowstone B-Prime) |
KEGG Pathway |
cyb:CYB_0708 |
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 Q2JNH3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q2JNH3-F1 | Predicted | AlphaFoldDB |
No variants for Q2JNH3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q2JNH3 | |||||
No associated diseases with Q2JNH3
6 regional properties for Q2JNH3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Immunodeficiency lentiviral matrix, N-terminal | 2 - 131 | IPR000071 |
| domain | Retroviral nucleocapsid Gag protein p24, N-terminal | 143 - 249 | IPR000721 |
| domain | Zinc finger, CCHC-type | 391 - 408 | IPR001878-1 |
| domain | Zinc finger, CCHC-type | 413 - 429 | IPR001878-2 |
| domain | Gag protein p6 | 450 - 486 | IPR014817 |
| domain | Retroviral nucleocapsid Gag protein p24, C-terminal domain | 276 - 348 | IPR045345 |
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 |
| MTVAAPAKVQ | YEAVIGLEVH | CQLSTRSKIF | SSSATAFGAP | PNTQIDPICM | GLPGTLPVLN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EKVLEYAVKA | GLALNCTIAP | YSKFDRKQYF | YPDLPKNYQI | SQYDLPIATH | GWIEIQLSDG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RTKRIGITRL | HMEEDAGKLV | HAGSDRLSGS | SYSLVDFNRA | GVPLIEIVSE | PDIRSGEEAA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EYVQELRRIL | RYAGLCDGNL | QEGSLRCDVN | ISVRPLGSQT | FGTKVEIKNM | NSFNAIQRAI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EYEFNRQVKA | VEAGERIVQE | TRLWEENSQR | TISMRKKEGS | SDYRYFPEPD | LPPIRVTEAQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KTRWQAELPE | LPGVKRRRYQ | EVYGLSVYDA | RYLSDERNTA | EYFEAVIAAG | ADPKAAANWM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| MSDIASYLNT | HKLDYPDIAL | KPETLAELIG | LIEQGTISSK | IAKEILPELL | EKGGSARALV |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EAKGMTQISD | SALLGQMIAE | VLAENPEQLQ | QYRGGKTKLF | GYFVGQLMKK | TQGRADPKLA |
| NDLLKQHLDG |