A5D5I7
Gene name |
fusA |
Protein name |
Elongation factor G |
Names |
EF-G |
Species |
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI) |
KEGG Pathway |
pth:PTH_0317 |
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 A5D5I7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A5D5I7-F1 | Predicted | AlphaFoldDB |
No variants for A5D5I7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A5D5I7 | |||||
No associated diseases with A5D5I7
9 regional properties for A5D5I7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Elongation factor EFG, domain V-like | 606 - 694 | IPR000640 |
| domain | Translational (tr)-type GTP-binding domain | 8 - 290 | IPR000795 |
| domain | Translation elongation factor EFTu-like, domain 2 | 329 - 396 | IPR004161 |
| domain | Small GTP-binding protein domain | 9 - 186 | IPR005225 |
| domain | Translation elongation factor EFG/EF2, domain IV | 484 - 604 | IPR005517 |
| domain | Elongation factor G, domain III | 410 - 485 | IPR009022 |
| conserved_site | Tr-type G domain, conserved site | 51 - 66 | IPR031157 |
| domain | EFG, domain V | 609 - 687 | IPR035649 |
| domain | Elongation Factor G, domain II | 409 - 483 | IPR041095 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
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. |
| translation elongation factor activity | Functions in chain elongation during polypeptide synthesis at the ribosome. |
No GO annotations of biological process
| Name | Definition |
|---|---|
| No GO annotations for biological process |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MARQFPLEKT | RNIGIMAHID | AGKTTTTERI | LFYTGRVHKI | GEVHEGTATM | DWMAQEQERG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ITITSAATSC | RWRDCQINII | DTPGHVDFTV | EVERSLRVLD | GAVAVFCSVG | GVEPQSETVW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RQADKYGVPR | IAYINKMDRV | GADFHRGIQM | IRERLGANPV | AIQLPIGVED | GFCGVVDLVR |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NRAIIYTDDL | GTTSEETEIP | PELAGEAAAF | RERLIEAVAE | FDESLMEKYL | ENGELTEEEI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KEGLRRATLA | VKIVPVLCGS | SFKNKGVQPL | LDAIVDYLPA | PTDIPAIRGV | NPVSGAGEVR |
| 310 | 320 | 330 | 340 | 350 | 360 |
| EARDDEPFSA | LAFKIMTDPY | VGKLTFFRVY | SGRLKSGSYV | YNSTRNRRER | VGRILRMHAN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HREDIEEVCA | GDIVAAVGLK | TTTTGDTLCD | EKEPVILESM | EFPEPVIQVA | IEPKTKADQE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KMGVALQKLA | EEDPTFRVST | DPETGQTLIS | GMGELHLEII | VDRMMREFKV | EANVGRPQVA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YKETVRKKAR | AEGKFIRQTG | GRGQYGHVVL | EVEPREPGSG | YLFTSKIIGG | VIPKEYIPAV |
| 550 | 560 | 570 | 580 | 590 | 600 |
| DAGAKEAMEN | GVLAGFPVID | VGVTLLDGSY | HEVDSSEMAF | KIAGSIGFKD | AARRADPVLL |
| 610 | 620 | 630 | 640 | 650 | 660 |
| EPVMKVEVVV | NEEYMGDVIG | DLNSRRGRIE | EMEARNGMQV | IHAYVPLAEM | FGYATDLRSR |
| 670 | 680 | 690 | |||
| TQGRGNYTMQ | FSHYAQVPDN | IAEGIIARRV | GR |