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 P79083

Entry ID Method Resolution Chain Position Source
AF-P79083-F1 Predicted AlphaFoldDB

1 variants for P79083

Variant ID(s) Position Change Description Diseaes Association Provenance
I_5359746_T_C 127 V>A No Jeffares_SNPs

No associated diseases with P79083

5 regional properties for P79083

Type Name Position InterPro Accession
repeat WD40 repeat 1 - 89 IPR001680-1
repeat WD40 repeat 136 - 175 IPR001680-2
repeat WD40 repeat 178 - 219 IPR001680-3
repeat WD40 repeat 277 - 316 IPR001680-4
conserved_site WD40 repeat, conserved site 67 - 81 IPR019775

Functions

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

9 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
cytoplasmic stress granule A dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
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.
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.
nuclear periphery The portion of the nuclear lumen proximal to the inner nuclear membrane.

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
cytoplasmic translational initiation The process preceding formation of the peptide bond between the first two amino acids of a protein in the cytoplasm. This includes the formation of a complex of the ribosome, mRNA or circRNA, and an initiation complex that contains the first aminoacyl-tRNA.
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.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MRPIILQGHE RPLTQIKYNH DGDLLFSCAK DKVINVWFSH NGERLGTYEG HTGAIWTCDI
70 80 90 100 110 120
NKSSTLMVSG AADNTMRLWD VKTGKQLYKW EFPTAVKRVE FNEDDTRILA VTEERMGYAG
130 140 150 160 170 180
TVTVFRVPIS ESDAAAETPL YVITTRESKA TVAGWSYLSK FLFTGHEDGS VSRYDAITGE
190 200 210 220 230 240
FVESKQVHNS GSTITDLQFY PDRTYFITSC KDTTAKAIDV DSFEVIKTYL TDTPLNTSSF
250 260 270 280 290 300
TPVQDFVILG GGQEARDVTT TAARQGKFEA RFYHAILEEE LGRVKGHFGP INTIAVHPKG
310 320
TGYASGGEDG YVRVHFFDKN YFDFKYTL