Q5SHN5
Gene name |
fusA (fus, TTHA1695) |
Protein name |
Elongation factor G |
Names |
EF-G |
Species |
Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8) |
KEGG Pathway |
ttj:TTHA1695 |
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
19 structures for Q5SHN5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1DAR | X-ray | 240 A | A | 1-691 | PDB |
| 1EFG | X-ray | 270 A | A | 1-691 | PDB |
| 1ELO | X-ray | 280 A | A | 1-691 | PDB |
| 1ZN0 | EM | 1550 A | B | 6-688 | PDB |
| 2EFG | X-ray | 260 A | A | 1-691 | PDB |
| 4V5F | X-ray | 360 A | AY/CY | 1-691 | PDB |
| 4V5M | EM | 780 A | AY | 1-691 | PDB |
| 4V5N | EM | 760 A | AY | 1-691 | PDB |
| 4V8U | X-ray | 370 A | AY/CY | 1-691 | PDB |
| 4V90 | X-ray | 295 A | AY | 1-691 | PDB |
| 4V9H | X-ray | 286 A | AY | 10-689 | PDB |
| 4WPO | X-ray | 280 A | BZ/DZ | 8-691 | PDB |
| 4WQF | X-ray | 280 A | BZ/DZ | 8-691 | PDB |
| 4WQU | X-ray | 280 A | BZ/DZ | 8-691 | PDB |
| 4WQY | X-ray | 280 A | BZ/DZ | 8-691 | PDB |
| 5HAU | X-ray | 300 A | 1z/2z | 8-691 | PDB |
| 5OT7 | EM | 380 A | U | 4-690 | PDB |
| 6UCQ | X-ray | 350 A | 1v/2v | 8-691 | PDB |
| AF-Q5SHN5-F1 | Predicted | AlphaFoldDB |
No variants for Q5SHN5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q5SHN5 | |||||
No associated diseases with Q5SHN5
9 regional properties for Q5SHN5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Elongation factor EFG, domain V-like | 600 - 687 | IPR000640 |
| domain | Translational (tr)-type GTP-binding domain | 10 - 284 | IPR000795 |
| domain | Translation elongation factor EFTu-like, domain 2 | 323 - 389 | IPR004161 |
| domain | Small GTP-binding protein domain | 13 - 181 | IPR005225 |
| domain | Translation elongation factor EFG/EF2, domain IV | 479 - 598 | IPR005517 |
| domain | Elongation factor G, domain III | 405 - 480 | IPR009022 |
| conserved_site | Tr-type G domain, conserved site | 53 - 68 | IPR031157 |
| domain | EFG, domain V | 603 - 680 | IPR035649 |
| domain | Elongation Factor G, domain II | 404 - 478 | 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 |
| MAVKVEYDLK | RLRNIGIAAH | IDAGKTTTTE | RILYYTGRIH | KIGEVHEGAA | TMDFMEQERE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RGITITAAVT | TCFWKDHRIN | IIDTPGHVDF | TIEVERSMRV | LDGAIVVFDS | SQGVEPQSET |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VWRQAEKYKV | PRIAFANKMD | KTGADLWLVI | RTMQERLGAR | PVVMQLPIGR | EDTFSGIIDV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LRMKAYTYGN | DLGTDIREIP | IPEEYLDQAR | EYHEKLVEVA | ADFDENIMLK | YLEGEEPTEE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ELVAAIRKGT | IDLKITPVFL | GSALKNKGVQ | LLLDAVVDYL | PSPLDIPPIK | GTTPEGEVVE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IHPDPNGPLA | ALAFKIMADP | YVGRLTFIRV | YSGTLTSGSY | VYNTTKGRKE | RVARLLRMHA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NHREEVEELK | AGDLGAVVGL | KETITGDTLV | GEDAPRVILE | SIEVPEPVID | VAIEPKTKAD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QEKLSQALAR | LAEEDPTFRV | STHPETGQTI | ISGMGELHLE | IIVDRLKREF | KVDANVGKPQ |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VAYRETITKP | VDVEGKFIRQ | TGGRGQYGHV | KIKVEPLPRG | SGFEFVNAIV | GGVIPKEYIP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AVQKGIEEAM | QSGPLIGFPV | VDIKVTLYDG | SYHEVDSSEM | AFKIAGSMAI | KEAVQKGDPV |
| 610 | 620 | 630 | 640 | 650 | 660 |
| ILEPIMRVEV | TTPEEYMGDV | IGDLNARRGQ | ILGMEPRGNA | QVIRAFVPLA | EMFGYATDLR |
| 670 | 680 | 690 | |||
| SKTQGRGSFV | MFFDHYQEVP | KQVQEKLIKG | Q |