P38525
Gene name |
fusA (fus, TM_1503) |
Protein name |
Elongation factor G |
Names |
EF-G |
Species |
Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
KEGG Pathway |
tma:TM1503 |
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 P38525
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P38525-F1 | Predicted | AlphaFoldDB |
No variants for P38525
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P38525 | |||||
No associated diseases with P38525
9 regional properties for P38525
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Elongation factor EFG, domain V-like | 601 - 688 | IPR000640 |
| domain | Translational (tr)-type GTP-binding domain | 9 - 283 | IPR000795 |
| domain | Translation elongation factor EFTu-like, domain 2 | 323 - 390 | IPR004161 |
| domain | Small GTP-binding protein domain | 10 - 181 | IPR005225 |
| domain | Translation elongation factor EFG/EF2, domain IV | 478 - 599 | IPR005517 |
| domain | Elongation factor G, domain III | 404 - 479 | IPR009022 |
| conserved_site | Tr-type G domain, conserved site | 52 - 67 | IPR031157 |
| domain | EFG, domain V | 604 - 681 | IPR035649 |
| domain | Elongation Factor G, domain II | 403 - 477 | IPR041095 |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
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. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| ribosome disassembly | The disaggregation of a ribosome into its constituent components; includes the dissociation of ribosomal subunits. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEARYVDLDK | LRNIGIMAHI | DAGKTTTTER | ILYYTGRKHF | IGDVDEGNTT | TDWMPQEKER |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GITIQSAATT | CFWKGYRINI | IDTPGHVDFT | AEVERALRVL | DGAIAVFDAT | AGVEPQSETV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| WRQADKYNVP | RIAFMNKMDK | VGADFYMAVE | TLVTKLRANP | IPVQMPIGSE | KDFQGVIDLI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KMKAIYWVSE | DGSVYEERDI | PEELREEAEM | RREEMLEKIA | ELDEEILEKY | LEGEEISEEE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IKRVLRKATI | ENKAVPVLCG | AAKANKGIQP | LLDAVIDYLP | SPLDLPPVKG | WRVSDGEVVY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| RKPDENEPFT | ALVFKVQVDP | YIGKLVYFRV | YSGRLEKGSY | VYNSTKGQRE | RISRIVFMHA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DKREEVDYVR | PGDIAAGVGL | KVSQTGDTLC | DEKEPIILEK | IDFPEPVISL | AVEPVTKADE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| EKLVKALLAL | SEEDPTLQVR | VDKETGETII | SGMGELHLEI | VVDRLKREFG | VNVRVGQPQV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AYRETIKKSA | EAEGKYIRQT | GGRGQYGHVI | LRIEPIPEEE | GKNFEFIDKT | VGGVIPKEFM |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PAIEAGIKEA | MMAGPLAGYP | VVRVRAIVLD | GSYHEVDSSE | MAFKIAASMA | FKEAMKKAQP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VLLEPIMKLE | ITTPEEYMGN | IISDLNSRRA | KVESLETRGH | LKVIVAKVPL | SETFGYATVL |
| 670 | 680 | 690 | |||
| RSLSQGRASY | IMQFSHYQEV | PEKIAEKIIK | VV |