UniProt ID: Q6P3J5 |
FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step during translation elongation (By similarity). During this step, the ribosome changes from the pre-translocational (PRE) to the post- translocational (POST) state as the newly formed A-site-bound peptidyl- tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively (By similarity). Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome (By similarity). {ECO:0000250|UniProtKB:P13639}. CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P13639}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P13639}; SUBUNIT: Binds to 80S ribosomes (PubMed:36653451). Actively translating ribosomes show mutually exclusive binding of eIF5a (EIF5A or EIF5A2) and EEF2/eEF2 (By similarity). Interacts with serbp1; interaction sequesters eef2/eEF2 at the A-site of the ribosome, thereby blocking the interaction sites of the mRNA-tRNA complex, promoting ribosome stabilization and hibernation (By similarity). Interacts with habp4; interaction takes place at the A-site of hibernating ribosomes and promotes ribosome stabilization (PubMed:36653451). {ECO:0000250|UniProtKB:P13639, ECO:0000269|PubMed:36653451}. SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P13639}. Nucleus {ECO:0000250|UniProtKB:P13639}. SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}. |
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