Q6FK21
Gene name |
TIF32 |
Protein name |
Eukaryotic translation initiation factor 3 subunit A |
Names |
eIF3a, Eukaryotic translation initiation factor 3 110 kDa subunit homolog, eIF3 p110, Translation initiation factor eIF3, p110 subunit homolog |
Species |
Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) (Yeast) (Torulopsis glabrata) |
KEGG Pathway |
cgr:CAGL0M01804g |
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 Q6FK21
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q6FK21-F1 | Predicted | AlphaFoldDB |
No variants for Q6FK21
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q6FK21 | |||||
No associated diseases with Q6FK21
1 regional properties for Q6FK21
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Proteasome component (PCI) domain | 298 - 509 | IPR000717 |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasmic stress granule | A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. |
| eukaryotic 43S preinitiation complex | A protein complex composed of the 40S ribosomal subunit plus eIF1A, eIF3, and eIF2-GTP-bound methionyl-initiator methionine tRNA. |
| eukaryotic 48S preinitiation complex | A protein complex composed of the small ribosomal subunit, eIF3, eIF1A, methionyl-initiatior methionine and a capped mRNA. The complex is initially positioned at the 5'-end of the capped mRNA. |
| eukaryotic translation initiation factor 3 complex | A complex of several polypeptides that plays at least two important roles in protein synthesis: First, eIF3 binds to the 40S ribosome and facilitates loading of the Met-tRNA/eIF2.GTP ternary complex to form the 43S preinitiation complex. Subsequently, eIF3 apparently assists eIF4 in recruiting mRNAs to the 43S complex. The eIF3 complex contains five conserved core subunits, and may contain several additional proteins; the non-core subunits are thought to mediate association of the complex with specific sets of mRNAs. |
| incipient cellular bud site | The portion of the budding yeast plasma membrane where a daughter cell will emerge. The yeast marks this spot with bud-site selection proteins before bud emergence occurs. Actin is polarized to this spot just prior to and during bud emergence. |
| multi-eIF complex | A multifactor complex composed of multiple translation initiation factors and the initiatior tRNAiMet, which is ready to bind to the small (40S) ribosome to form the 43S preinitiation complex. In S. cerevisiae, this complex is composed of eIF1, eIF2, eIF3, and eIF5. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| RNA binding | Binding to an RNA molecule or a portion thereof. |
| translation initiation factor activity | Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| formation of cytoplasmic translation initiation complex | Joining of the large subunit, with release of IF2/eIF2 and IF3/eIF3. This leaves the functional ribosome at the AUG, with the methionyl/formyl-methionyl-tRNA positioned at the P site. |
| translation reinitiation | A gene-specific translational control mechanism where the small ribosomal subunit remains attached to the mRNA following termination of translation, then resumes scanning on the same mRNA molecule and initiates again at a downstream start site. Reinitiation depends on de novo recruitment of the ternary complex that is required to recognize the next AUG codon. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAPPPLRPEN | ALKRADELIS | VNEKPAALQS | LYEFITARRI | RYATPSQVEP | IVFKFLELGV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ELKKGKLIKD | ALYQYKKLVH | GSAEGLVSVG | AVLRKFIDYV | ETKLASEQAK | AEEKQKEEVS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DDLEGGVTPE | NLLSSVYEAD | HSVAGFNDEA | LNSWMRFSWE | SYRTALDLLR | NNSQLEITYS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| GVVSRTMQFC | LKHQRKNEFK | RLAEMLRQHL | DTANYHQSKF | GSNQVDLSDA | DTLQRYLDQR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| FQLVDASVKL | GLWHEAYKAA | EDVYHLMKMT | TRKPKSSTLA | NYFENLVQIF | LVSGDQILHT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LAWKKYFELY | STNPNATEEE | FKKIASTIFL | SALSIQLDDL | PNVRYNYQSR | SYRLLDVETK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PTRKEVIQSI | VEDDTIFSRV | DAETKTLYEI | MEVEFDGESF | KGKFEAILPK | LEGESYFANY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| SVSLRDVIIR | RMFVFASQKY | EDISLNDLYS | SVTFSSSFKL | SEWDIEKQLL | QAAVDDYVSF |
| 490 | 500 | 510 | 520 | 530 | 540 |
| QLDHEQNKVT | FVKDPLVNFA | AIKEEEVEEE | EEEEEEEEEE | EKEAEGAEGA | EGDTEEGQEA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| VAEPEPVIKR | NYYIRKRLSE | LYEKLLEDTD | YNTVSYLDKV | RIAREALIKH | TKDTIEDMKK |
| 610 | 620 | 630 | 640 | 650 | 660 |
| NSEERAKMHQ | ERRRQHMESA | AMNAEKDAEQ | RQKRIMEERA | SIEAKLEEEA | HRRLIEKKKR |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EFEEVKQREI | RKLVDELNAK | GNGTKVEYDE | VKDMDIPDIT | KYFVNRLSKN | KDELEERMNF |
| 730 | 740 | 750 | 760 | 770 | 780 |
| AVKRMDHLER | AYRKVELPLL | KKQADELRAT | DEVNFGNMKK | KIVDAAKAEY | EAKMEDYNRV |
| 790 | 800 | 810 | 820 | 830 | 840 |
| SSVFDDYKTL | RDRMLAAHNE | KFAAIRAENA | AKLEAAKKAR | IEEVRKQRYE | ELLARSEAEK |
| 850 | 860 | 870 | 880 | 890 | 900 |
| KAAEEAERRA | KLDEIARKQR | EMEEALERKS | AARTFTQPRA | PVVPNANLDE | IARKQREMEE |
| 910 | 920 | 930 | 940 | 950 | |
| AIERKLAGKS | AAPAPAPAPA | ASTPAASTPA | APGKMSFAER | MRLKRQQQQQ | K |