A8WX15

PR
Gene name
eif-3.B
Protein name
Eukaryotic translation initiation factor 3 subunit B
Names
eIF3b, Eukaryotic translation initiation factor 3 subunit 9
Species
Caenorhabditis briggsae
KEGG Pathway
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-53 (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 A8WX15

Entry ID Method Resolution Chain Position Source
AF-A8WX15-F1 Predicted AlphaFoldDB

No variants for A8WX15

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A8WX15

No associated diseases with A8WX15

4 regional properties for A8WX15

Type Name Position InterPro Accession
domain Translation elongation factor P/YeiP, central 66 - 126 IPR001059
domain Translation elongation factor, KOW-like 4 - 60 IPR013185
conserved_site Translation elongation factor P/YeiP, conserved site 150 - 169 IPR013852
domain Elongation factor P, C-terminal 129 - 184 IPR015365

Functions

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

3 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.

3 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.
translation initiation factor binding Binding to a translation initiation factor, any polypeptide factor involved in the initiation of ribosome-mediated translation.

3 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.
regulation of translational initiation Any process that modulates the frequency, rate or extent of translational initiation.
translational initiation The process preceding formation of the peptide bond between the first two amino acids of a protein. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MVEIDFNKEN EEDYSDPADF VDDVTDDVLV PDVLYKKPTI DEFEGNVFIA GIPVVGAERI
70 80 90 100 110 120
ARLQSVLKKV LEKLEPGVKI FIPPSPEGGS LGVLLTEWPD SRSAAFAVKS LDGYSFDKNH
130 140 150 160 170 180
TFSARFFTDM KKLEAPSDAW TTPVKSEYSD VGDLWWWLQN ERCRDQFAIS HDKLGIPTVG
190 200 210 220 230 240
VFTNMKGNDP ELAGDPEKAE RANWTETVFT WSPHGSYLST IHKRGIILWG GKDYARAHRF
250 260 270 280 290 300
AHDNVQYIDF SPCETFLDTY LGRLEKKVPE SLGFRTGELK KAYSTFELTG RTQLPTWPFF
310 320 330 340 350 360
KWSIDEKYFA CLKAPEKDKL EREKKIDGIS IFESETFELV DKRAVTIENI KHFDWSPTAP
370 380 390 400 410 420
ILAYYSECTD AVPAEFGLLQ VPSMQRLRSA RVHNVADAQM FWQKSGKRLA FYTMRYKKKE
430 440 450 460 470 480
FRETGEVKYV GGCQYHVDIF EIDKKDVSLM NLPLAEPFIH FDWDPEGDKF CVLVGNTAKA
490 500 510 520 530 540
TPQVYKIEAN SHAPKLVSKL DAGVHFNEVQ FAPKGGWLAV LAKVSAGGNV YFIDTSLAEA
550 560 570 580 590 600
KRTNVIEHPL FNKGYWDPTG RYFVTCSTLG GRAGADLGYR IFTFQGRELC RKNLDRLAQF
610 620 630 640 650 660
KWRPRPPVKL SEQKQNEIRK NLKKTAAKFV KQDDDEKCRA SQEVVEKRRK IMAAFDVIRN
670 680 690 700 710
RNRECLENTR HLRIALRDGV DTEAQLDEDE FVDEEITIAL STSKTAAPLS EEDERD