O49169 · EF1A_MANES
- ProteinElongation factor 1-alpha
- GeneEF1
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids449 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis.
Features
Showing features for binding site.
GO annotations
all annotations | all molecular function | nucleotide binding | molecular_function | nucleic acid binding | dna binding | chromatin binding | dna-binding transcription factor activity | rna binding | cytoskeletal motor activity | catalytic activity | nuclease activity | signaling receptor binding | structural molecule activity | transporter activity | binding | protein binding | translation factor activity, rna binding | lipid binding | kinase activity | transferase activity | hydrolase activity | oxygen binding | enzyme regulator activity | carbohydrate binding | signaling receptor activity | translation regulator activity | transcription regulator activity | other molecular function | all biological process | carbohydrate metabolic process | generation of precursor metabolites and energy | nucleobase-containing compound metabolic process | dna metabolic process | translation | lipid metabolic process | transport | response to stress | cell cycle | cell communication | signal transduction | cell-cell signaling | multicellular organism development | circadian rhythm | biological_process | metabolic process | catabolic process | biosynthetic process | response to light stimulus | response to external stimulus | tropism | response to biotic stimulus | response to abiotic stimulus | response to endogenous stimulus | embryo development | post-embryonic development | fruit ripening | abscission | pollination | flower development | cellular process | programmed cell death | photosynthesis | cellular component organization | cell growth | protein metabolic process | cellular homeostasis | secondary metabolic process | reproductive process | cell differentiation | protein modification process | growth | epigenetic regulation of gene expression | response to chemical | anatomical structure development | regulation of molecular function | other biological process | all cellular component | cellular_component | extracellular region | cell wall | intracellular anatomical structure | nucleus | nuclear envelope | nucleoplasm | nucleolus | cytoplasm | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | cytosol | ribosome | cytoskeleton | plasma membrane | chloroplast | plastid | thylakoid | membrane | external encapsulating structure | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | GTP binding | |
Molecular Function | GTPase activity | |
Molecular Function | translation elongation factor activity |
Keywords
- Molecular function
- Biological process
- Ligand
Names & Taxonomy
Protein names
- Recommended nameElongation factor 1-alpha
- Short namesEF-1-alpha
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Viridiplantae > Streptophyta > Embryophyta > Tracheophyta > Spermatophyta > Magnoliopsida > eudicotyledons > Gunneridae > Pentapetalae > rosids > fabids > Malpighiales > Euphorbiaceae > Crotonoideae > Manihoteae > Manihot
Accessions
- Primary accessionO49169
Subcellular Location
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000090940 | 1-449 | Elongation factor 1-alpha | |||
Sequence: MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQIQEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFGPTGLTTEVKSVEMHHEALQEALPGDNVGFNVKNVAVKDLKRGIVASNSKDDPAKEAANFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELEKEPKFLKNGDAGFVKMIPTKPMVVETFSAYPPLGRFAVRDMRQTVAVGVIKSVEKKDPSGAKVTKSAAKKGGK | ||||||
Modified residue | 55 | N6,N6-dimethyllysine | ||||
Sequence: K | ||||||
Modified residue | 79 | N6,N6,N6-trimethyllysine | ||||
Sequence: K | ||||||
Modified residue | 187 | N6,N6,N6-trimethyllysine | ||||
Sequence: K | ||||||
Modified residue | 261 | N6-methyllysine | ||||
Sequence: K | ||||||
Modified residue | 289 | 5-glutamyl glycerylphosphorylethanolamine | ||||
Sequence: E | ||||||
Modified residue | 306 | N6,N6,N6-trimethyllysine | ||||
Sequence: K | ||||||
Modified residue | 362 | 5-glutamyl glycerylphosphorylethanolamine | ||||
Sequence: E | ||||||
Modified residue | 396 | N6,N6,N6-trimethyllysine | ||||
Sequence: K |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-230 | tr-type G | ||||
Sequence: KVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQIQEPKRPS | ||||||
Region | 14-21 | G1 | ||||
Sequence: GHVDSGKS | ||||||
Region | 70-74 | G2 | ||||
Sequence: GITID | ||||||
Region | 91-94 | G3 | ||||
Sequence: DAPG | ||||||
Region | 153-156 | G4 | ||||
Sequence: NKMD | ||||||
Region | 194-196 | G5 | ||||
Sequence: SGF |
Sequence similarities
Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily.
Family and domain databases
Sequence
- Sequence statusComplete
- Length449
- Mass (Da)49,371
- Last updated1998-06-01 v1
- Checksum779E3858DBE16104