EuRBPDB

Macaca_mulattaFamily: GTP_EFTU_D2 Number of Genes: 21

Ensembl ID	Symbol	Entrez ID
ENSMMUG00000001210	-	-
ENSMMUG00000003303	TUFM	705462
ENSMMUG00000004089	-	-
ENSMMUG00000004802	HBS1L	706748
ENSMMUG00000004852	EEF1A1	716010
ENSMMUG00000004961	GFM1	706456
ENSMMUG00000006979	-	698763
ENSMMUG00000007369	-	-
ENSMMUG00000009270	GUF1	703333
ENSMMUG00000013118	EFTUD2	715512
ENSMMUG00000013388	-	-
ENSMMUG00000017420	-	-
ENSMMUG00000017625	-	-
ENSMMUG00000018946	EIF5B	714129
ENSMMUG00000019998	GFM2	704247
ENSMMUG00000022526	EEF1A2	-
ENSMMUG00000022767	EEF2	721806
ENSMMUG00000023178	GSPT1	716860
ENSMMUG00000029293	GSPT2	-
ENSMMUG00000040183	-	-
ENSMMUG00000043656	-	-

Introduction

Pfam

Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA [1]. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to PF03143 and in fact has weak sequence matches to this domain.

InterPro

Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome [PUBMED:12762045, PUBMED:15922593, PUBMED:12932732]. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution.

Reference

Nissen P, Kjeldgaard M, Thirup S, Polekhina G, Reshetnikova L, Clark BF, Nyborg J; , Science 1995;270:1464-1472.: Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog. PUBMED:7491491 EPMC:7491491.