Q2U002

PR
Gene name
tif35 (AO090011000648)
Protein name
Eukaryotic translation initiation factor 3 subunit G
Names
eIF3g, Eukaryotic translation initiation factor 3 RNA-binding subunit, eIF-3 RNA-binding subunit, Translation initiation factor eIF3 p33 subunit homolog, eIF3 p33 homolog
Species
Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
KEGG Pathway
aor:AO090011000648
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-238 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q2U002

Entry ID Method Resolution Chain Position Source
AF-Q2U002-F1 Predicted AlphaFoldDB

No variants for Q2U002

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2U002

No associated diseases with Q2U002

3 regional properties for Q2U002

Type Name Position InterPro Accession
domain RNA recognition motif domain 207 - 285 IPR000504
domain Eukaryotic translation initiation factor 3 subunit G, N-terminal 25 - 152 IPR024675
domain eIF3G, RNA recognition motif 208 - 283 IPR034240

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

5 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, eIF3e An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3e.
eukaryotic translation initiation factor 3 complex, eIF3m An eukaryotic translation initiation factor 3 complex that contains the PCI-domain protein eIF3m.
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.

4 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.
positive regulation of ATP-dependent activity Any process that activates or increases the rate of an ATP-dependent activity.
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.
translational termination The process resulting in the release of a polypeptide chain from the ribosome, usually in response to a termination codon (UAA, UAG, or UGA in the universal genetic code).

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSKLANRADW ADDEEFDDPS ALPAQQVTTN KDGTKTVVSY RFNDEGKKVK VTRRIKTTVV
70 80 90 100 110 120
REHVNPQVAE RRSWAKFGLE KGHAPGPSFD TTSVGENIAF RPSINWKAQA AEAEKNGGEK
130 140 150 160 170 180
GSMKDQLKDK KVKCRICSGE HFTARCPFKD TMAPVDEPTA GGAGEDDEAA AGAVGTGSGS
190 200 210 220 230 240
YVPPHLRKGA AGGGERMGGK FEKDDLATLR VTNVSELAEE GELRDLFERF GRVTRVFLAR
250 260 270 280
DRETQRAKGF AFISFADRSD AARACEKMDG FGYRHLILRV EFAKRTT