A2QU25
Gene name |
guf1 (An09g04110) |
Protein name |
Translation factor guf1, mitochondrial |
Names |
Elongation factor 4 homolog, EF-4, GTPase guf1, Ribosomal back-translocase |
Species |
Aspergillus niger (strain CBS 51388 / FGSC A1513) |
KEGG Pathway |
ang:ANI_1_510084 |
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 A2QU25
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A2QU25-F1 | Predicted | AlphaFoldDB |
No variants for A2QU25
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A2QU25 | |||||
No associated diseases with A2QU25
6 regional properties for A2QU25
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | DNA gyrase B subunit, C-terminal | 574 - 634 | IPR002288 |
| domain | Histidine kinase/HSP90-like ATPase | 39 - 183 | IPR003594 |
| domain | TOPRIM domain | 429 - 543 | IPR006171 |
| domain | DNA topoisomerase, type IIA, subunit B, domain 2 | 232 - 401 | IPR013506 |
| conserved_site | DNA topoisomerase, type IIA, conserved site | 433 - 441 | IPR018522 |
| domain | DNA gyrase subunit B, TOPRIM domain | 429 - 542 | IPR034160 |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial inner membrane | The inner, i.e. lumen-facing, lipid bilayer of the mitochondrial envelope. It is highly folded to form cristae. |
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| mitochondrial ribosome binding | Binding to a mitochondrial ribosome. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| positive regulation of translation | Any process that activates or increases the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. |
| 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 |
| MRGCLQLARW | LRAAPKCPAA | SLLKPPSGLA | NPARFFTTST | ACWASRSRAP | ASQPSSDLES |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RIAAIPIDRY | RNFCIVAHVD | HGKSTLSDRL | LELTGTIQPG | MNKQVLDKLD | VERERGITVK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AQTCTMIYNH | NGEDYLLHLV | DTPGHVDFRA | EVSRSYASCG | GALLLVDASQ | GIQAQTVANF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YLAFSQGLEL | IPVINKVDLP | SADPERALDQ | MEQSFELDTE | SAVLVSAKTG | LNVQQLLPTV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VEKIPAPVGD | VNNPLRMLLV | DSWYDSYRGV | ICLVRVFDGE | IRAGDQLVSF | ATGIKYFVGE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VGIMYPNETA | QSVLRAGQVG | YIFFNPGMKR | SKEAKIGDTY | TKVGFEKVVE | PLPGFEEPKA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| MVFVAAYPVD | ADHFEHLEDS | INQLCLNDRS | ITVQKESSHA | LGAGFRLGFL | GTLHCSVFED |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RLRQEHGASI | IITPPSVPVK | LIWKDGKEEI | ISNPAKFPED | EELRGKISEI | QEPYVVATLT |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LPDEYLGKVI | ELCESNRGVQ | KSLEYFTSTQ | VILKYELPLA | QLVDDFFGKL | KGSTKGYATL |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DYEESAWQTS | NIVKLQLLVN | KAPVDAVARL | VHYSQVERLG | RQWVTKFKEH | VDRQLFEIVI |
| 610 | 620 | 630 | 640 | 650 | 660 |
| QAAVGRKVVA | RETVKPYRKD | VLAKLHASDV | SRRRKLLEKQ | KEGRKKLRAV | GNVVIEQKAF |
| QAFLAK |