B4HFV9
Gene name |
eIF3d1 |
Protein name |
Eukaryotic translation initiation factor 3 subunit D-1 |
Names |
eIF3d-1, Eukaryotic translation initiation factor 3 subunit 7-1, Eukaryotic translation initiation factor 3 subunit p66 |
Species |
Drosophila sechellia (Fruit fly) |
KEGG Pathway |
dse:6607598 |
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 B4HFV9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B4HFV9-F1 | Predicted | AlphaFoldDB |
No variants for B4HFV9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B4HFV9 | |||||
No associated diseases with B4HFV9
No regional properties for B4HFV9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for B4HFV9 | |||
4 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| mRNA cap binding | Binding to a 7-methylguanosine (m7G) group or derivative located at the 5' end of an mRNA molecule. |
| translation initiation factor activity | Functions in the initiation of ribosome-mediated translation of mRNA into a polypeptide. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cap-dependent translational initiation | The process where the cap structure, composed of a 7- methylguanosine (m7G) group and associated cap-binding proteins, located at the 5' end of an mRNA molecule, which serves as a molecular tag that marks the spot where the 40S ribosomal subunit, is recruited and will then scan in a 5' to 3' direction until an AUG codon is encountered in an appropriate sequence context to initiate mRNA translation. |
| 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. |
| regulation of translational initiation | Any process that modulates the frequency, rate or extent of translational initiation. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSETINTAAQ | FPSFEKPTVQ | FNEKGWGPCE | LPDTFKDVPY | QPFSKNDRLG | KICDWTNTSN |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NDKKYQNKYA | SSFGTGNQYS | YYHEEDETTF | HLVDTARVQK | PPHQRGRFRN | MRNSRSGRGR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NARGGLNTHG | MTTLSGKNVK | ARDPRHGRGM | GKKFGHRGPP | PKMRESSVAV | RADWASIEEM |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DFPRLIKLSL | PNIKEGVDIV | TCGTLEYYDK | TYDRINVKNE | KPLQKIDRIV | HTVTTTDDPV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| IRRLSKTVGN | VFATDAILAT | IMCSTRSNYS | WDIVIEKVGD | KVFMDKRDHT | EFDLLTVNES |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SVEPPTDDDS | SCNSPRNLAI | EATFINHNFS | QQVLKTGDQE | PKYKFEESNP | FISEDEDIQV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ASVGYRYKKW | ELGSDIVLVA | RCEHDGVLQT | PSGEPQFMTI | KALNEWDSKL | ANGVEWRQKL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DTQRGAVLAN | ELRNNACKLA | KWTVQAVLAG | SDQLKLGYVS | RINPRDHSRH | VILGTQQFKP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| HEFATQINLS | MDNAWGILRC | IIDLVMKQKD | GKYLIMKDPN | KPIIRLYDIP | DNTFDSDDSD |
| 550 | |||||
| DGEGDDEGFQ | QVYNYAHNKI |