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IID50184
 UniprotP20459
ProteinEukaryotic translation initiation factor 2 subunit alpha
GeneSUI2
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c)
Sequence LLPS PhaSepDB
PhaSePro
LLPSDB
DrLLPS Network xml rdf
Structure
Experiment
  :order   disorder   conflict   PDB cluster   ProS   Pfam Domain   SEG
304
 order/disorder by at least rule
     disorder by at least rule
     order by at least rule
 order/disorder by majority rule
Seq 2-176 Monomer :
 Evidence X-RAY 1q46 A Reference
       Region 1q46 A 2-2 disorder
       Region 1q46 A 3-176 order
Seq 4-176 Hetero tetramer : IID00443Complex
 Evidence X-RAY 2a1a A Reference
       Region 2a1a A 4-49 order
       Region 2a1a A 50-61 disorder
       Region 2a1a A 62-176 order
Seq 4-176 Hetero trimer : IID00443Complex
 Evidence X-RAY 2a19 A Reference
       Region 2a19 A 4-49 order
       Region 2a19 A 50-57 disorder
       Region 2a19 A 58-175 order
       Region 2a19 A 176-176 disorder
Seqphosphorylation
    292-292 Phosphoserine
    294-294 Phosphoserine
    52-52 Phosphoserine; by GCN2
 
Prediction
NeProc
Disorder 1-1,276-304
Order 2-275
ProS 276-290
AlphaFold
Disorder 1-5,155-162,214-216,273-275,279-279,290-304
Order 6-154,163-213,217-272,276-278,280-289
Pfam Hmmer
PF00575 13-88 7.6e-16
PF07541 125-237 1.4e-67
SEG 46-59 ,292-304
Function
Function in SwissProt
eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA. This complex binds to a 40S ribosomal subunit, followed by mRNA binding to form a 43S pre-initiation complex. Junction of the 60S ribosomal subunit to form the 80S initiation complex is preceded by hydrolysis of the GTP bound to eIF-2 and release of an eIF-2-GDP binary complex. In order for eIF-2 to recycle and catalyze another round of initiation, the GDP bound to eIF-2 must exchange with GTP by way of a reaction catalyzed by eIF-2B.