Q5LMR4
Gene name |
fusA |
Protein name |
Elongation factor G |
Names |
EF-G |
Species |
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) (Silicibacter pomeroyi) |
KEGG Pathway |
sil:SPO3499 |
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 Q5LMR4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q5LMR4-F1 | Predicted | AlphaFoldDB |
No variants for Q5LMR4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5LMR4 | |||||
No associated diseases with Q5LMR4
9 regional properties for Q5LMR4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Elongation factor EFG, domain V-like | 609 - 696 | IPR000640 |
| domain | Translational (tr)-type GTP-binding domain | 8 - 291 | IPR000795 |
| domain | Translation elongation factor EFTu-like, domain 2 | 332 - 399 | IPR004161 |
| domain | Small GTP-binding protein domain | 9 - 188 | IPR005225 |
| domain | Translation elongation factor EFG/EF2, domain IV | 487 - 607 | IPR005517 |
| domain | Elongation factor G, domain III | 413 - 488 | IPR009022 |
| conserved_site | Tr-type G domain, conserved site | 51 - 66 | IPR031157 |
| domain | EFG, domain V | 612 - 689 | IPR035649 |
| domain | Elongation Factor G, domain II | 412 - 486 | 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 |
| MAREYPLNLY | RNFGIMAHID | AGKTTCSERI | LYYTGKSHNI | GEVHDGAATM | DWMEQEQERG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ITITSAATTT | FWERTEDGAT | ADTPKHRLNI | IDTPGHVDFT | IEVERSLAVL | DGAVCVLDAN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AGVEPQTETV | WRQADRYKVP | RMVFVNKMDK | IGADFFNCVR | MIEDRTGARA | VPVGIPIGAE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TELEGLVDLV | TMEEWLWQGE | DLGASWVKAP | IRDSLKDMAE | EWRGKMIEAA | VEEDDDAMME |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YLEGNEPDVP | TLRKLLRKGT | LALHFVPVLG | GSAFKNKGVQ | PLLNAVIDYL | PSPLDVVDYM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GFKPGDEEEV | RNIARRADDN | MAFSGLAFKI | MNDPFVGSLT | FTRVYSGVLK | KGDTMLNSTK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GKKERVGRMM | MMHSNNREEI | DEAFAGDIIA | LAGLKDTTTG | DTLCDAKDPV | VLETMTFPDP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| VIEIAVEPKT | KGDQEKMSQG | LARLAAEDPS | FRVETDIESG | QTIMKGMGEL | HLDILVDRLK |
| 490 | 500 | 510 | 520 | 530 | 540 |
| REFKVEANIG | APQVAYRETI | SKEVEHTYTH | KKQSGGSGQF | AEVKLVITPT | EPGEGYSFES |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RIVGGAVPKE | YIPGVEKGIK | SVMDSGPLAG | FPVIDFKVAL | IDGKFHDVDS | SVLAFEIAAR |
| 610 | 620 | 630 | 640 | 650 | 660 |
| MGMREGMKKA | GAKLLEPIMK | VEVITPEEYT | GGIIGDLTSR | RGQVSGQESR | GNAIAINAFV |
| 670 | 680 | 690 | 700 | ||
| PLANMFGYIN | TLRSMSSGRA | QFTMLFDHYD | PVPQNISDEI | QAKYA |