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
No variants for Q46455
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q46455 | |||||
No associated diseases with Q46455
6 regional properties for Q46455
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Translational (tr)-type GTP-binding domain | 1 - 173 | IPR000795 |
| domain | Translation elongation factor EFTu-like, domain 2 | 194 - 260 | IPR004161 |
| domain | Small GTP-binding protein domain | 2 - 162 | IPR005225 |
| domain | Translation elongation factor SelB, winged helix, type 1 | 377 - 437 | IPR015189 |
| domain | Translation elongation factor SelB, winged helix, type 2 | 449 - 504 | IPR015190 |
| domain | Translation elongation factor SelB, winged helix, type 3 | 587 - 630 | IPR015191 |
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. |
4 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. |
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| translation elongation factor activity | Functions in chain elongation during polypeptide synthesis at the ribosome. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| selenocysteine incorporation | The incorporation of selenocysteine into a peptide; uses a special tRNA that recognizes the UGA codon as selenocysteine, rather than as a termination codon. Selenocysteine is synthesized from serine before its incorporation; it is not a posttranslational modification of peptidyl-cysteine. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDYIVVGTAG | HVDHGKTVLV | KALTGVDTDR | LKEEKERGIS | IELGFAPLTL | PSGRQLGLVD |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VPGHERFIRQ | MLAGVGGMDL | VMLVVAADEG | VMPQTREHLA | IIDLLQIKKG | IIVITKIDLV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EADWLELVRE | EVRQAVKGTV | LEDAPLVEVS | ALTGEGIAEL | REQLDALAAV | TPPRPAAGRV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLPIDRVFSV | TGFGTVVTGT | LWSGTIKVGD | ELEVQPEGLK | TRARNLQVHG | RTVKEARAGQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RVAVNLAGIE | TEAVHRGSSL | LTPGFLTPTY | RLDASFKLLN | GARPLANRDR | VHFYLGTSEA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LGRVVLLDRD | ELNGGEEALI | QLLMEKPVVA | SREDRFILRS | YSPMETIGGG | IIIDPVPPKH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RRFQPEVLVS | LQRRLEGSPE | KILAQIIQEH | REGLDWQEAA | TRASLSLEET | RKLLQSMAAA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GQVTLLRVEN | DLYAISTERY | QAWWQAVTRA | LEEFHSRYPL | RPGLAREELR | SRYFSRLPAR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VYQALLEEWS | REGRLQLAAN | TVALAGFTPS | FSETQKKLLK | DLEDKYRVSR | WQPPSFKEVA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| GSFNLDPSEL | EELLHYLVRE | GVLVKINDEF | YWHRQALGEA | REVIKNLAST | GPFGLAEARD |
| 610 | 620 | 630 | |||
| ALGSSRKYVL | PLLEYLDQVK | FTRRVGDKRV | VVGN |