O94489 · EF3_SCHPO
- ProteinElongation factor 3
- Genetef3
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids1047 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Ribosome-dependent ATPase that functions in cytoplasmic translation elongation (PubMed:29300771).
Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (By similarity).
Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied (By similarity).
Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis (By similarity).
Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied (By similarity).
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
Pathway
Protein biosynthesis; polypeptide chain elongation.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 467-474 | ATP 1 (UniProtKB | ChEBI) | |||
Binding site | 707-714 | ATP 2 (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | RNA binding | |
Molecular Function | translation elongation factor activity | |
Biological Process | cytoplasmic translation | |
Biological Process | cytoplasmic translational elongation |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameElongation factor 3
- EC number
- Short namesEF-3
Gene names
Organism names
- Strains
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Taphrinomycotina > Schizosaccharomycetes > Schizosaccharomycetales > Schizosaccharomycetaceae > Schizosaccharomyces
Accessions
- Primary accessionO94489
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Chain | PRO_0000093457 | 1-1047 | Elongation factor 3 | ||
Modified residue | 714 | Phosphoserine | |||
Modified residue | 768 | Phosphoserine | |||
Modified residue | 783 | Phosphoserine | |||
Modified residue | 1043 | Phosphoserine | |||
Keywords
- PTM
Proteomic databases
PTM databases
Structure
Family & Domains
Features
Showing features for repeat, domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Repeat | 48-85 | HEAT 1 | |||
Repeat | 91-128 | HEAT 2 | |||
Repeat | 130-167 | HEAT 3 | |||
Repeat | 171-208 | HEAT 4 | |||
Repeat | 210-246 | HEAT 5 | |||
Repeat | 247-284 | HEAT 6 | |||
Domain | 411-647 | ABC transporter 1 | |||
Domain | 673-1000 | ABC transporter 2 | |||
Region | 1022-1047 | Disordered | |||
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,047
- Mass (Da)115,802
- Last updated1999-05-01 v1
- Checksum10F5F10DB2E867F1
Features
Showing features for sequence conflict.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Sequence conflict | 770-771 | in Ref. 3; BAA11573 | |||
Sequence conflict | 777 | in Ref. 3; BAA11573 | |||
Sequence conflict | 800-802 | in Ref. 3; BAA11573 | |||
Sequence conflict | 950 | in Ref. 3; BAA11573 | |||
Sequence conflict | 959 | in Ref. 4; BAA33896 | |||
Sequence conflict | 962 | in Ref. 2; BAA13887 | |||
Sequence conflict | 972 | in Ref. 2; BAA13887 | |||
Sequence conflict | 977 | in Ref. 2; BAA13887 | |||
Sequence conflict | 982 | in Ref. 2; BAA13887 | |||
Sequence conflict | 988 | in Ref. 2; BAA13887 | |||
Sequence conflict | 1001-1002 | in Ref. 2; BAA13887 | |||
Sequence conflict | 1009-1014 | in Ref. 2; BAA13887 | |||
Sequence conflict | 1023 | in Ref. 2; BAA13887 | |||
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CU329672 EMBL· GenBank· DDBJ | CAA22654.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
D89226 EMBL· GenBank· DDBJ | BAA13887.1 EMBL· GenBank· DDBJ | mRNA | ||
D82575 EMBL· GenBank· DDBJ | BAA11573.1 EMBL· GenBank· DDBJ | mRNA | ||
AB018538 EMBL· GenBank· DDBJ | BAA33896.1 EMBL· GenBank· DDBJ | Genomic DNA |