SMART: Pfam domain GTP_EFTU

The domain within your query sequence starts at position 572 and ends at position 681; the E-value for the GTP_EFTU_D3 domain shown below is 9.2e-34.

ACTRFRARILVFNIEVPITKGFPVLLHYQTVSEPAVIKRLISVLNKSTGEVTKKKPKLLT
KGQNALVELQTQRPVALELYKDFKELGRFMLRYGGSTVAAGVVTEIKE

GTP_EFTU_D3

PFAM accession number:	PF03143
Interpro abstract (IPR004160):	Elongation factor EF1A (also known as EF-1alpha or EF-Tu) promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. EF1A consists of three structural domains. Release factor eRF3, which governs translation termination, has a similar overall structure. RF3 has an N-terminal extension and a EF1A-like C-terminal region which comprises a GTP-binding domain (G domain) and two beta-barrel domains that are similar to the three respective domains of elongation factor EF-Tu/eEF1A [ (PUBMED:10676813) ]. Archaeal EF1A is both involved in translational elongation and termination, as well as in mRNA surveillance, which explains the lack of an eRF3 orthologue in archaea [ (PUBMED:20974926) ]. This entry represents the C-terminal domain of both EF1A and eRF3, which adopts a beta-barrel structure. In EF1A, this domain is involved in binding to both charged tRNA and to EF1B (or EF-Ts, IPR001816 ) [ (PUBMED:9253415) ].

PFAM accession number:

PF03143

Interpro abstract (IPR004160):

Elongation factor EF1A (also known as EF-1alpha or EF-Tu) promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. EF1A consists of three structural domains. Release factor eRF3, which governs translation termination, has a similar overall structure. RF3 has an N-terminal extension and a EF1A-like C-terminal region which comprises a GTP-binding domain (G domain) and two beta-barrel domains that are similar to the three respective domains of elongation factor EF-Tu/eEF1A [ (PUBMED:10676813) ]. Archaeal EF1A is both involved in translational elongation and termination, as well as in mRNA surveillance, which explains the lack of an eRF3 orthologue in archaea [ (PUBMED:20974926) ].

This entry represents the C-terminal domain of both EF1A and eRF3, which adopts a beta-barrel structure. In EF1A, this domain is involved in binding to both charged tRNA and to EF1B (or EF-Ts, IPR001816 ) [ (PUBMED:9253415) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry GTP_EFTU_D3