EuRBPDB

Cercocebus_atysFamily: GTP_EFTU_D2 Number of Genes: 18

Ensembl ID	Symbol	Entrez ID
ENSCATG00000015798	-	-
ENSCATG00000021756	-	-
ENSCATG00000025774	GSPT1	105572228
ENSCATG00000029226	-	-
ENSCATG00000029600	-	-
ENSCATG00000032413	-	-
ENSCATG00000035809	EFTUD2	105585392
ENSCATG00000035822	TUFM	105598628
ENSCATG00000036349	EEF1A2	105592320
ENSCATG00000036394	GFM2	105599210
ENSCATG00000037374	-	105574615
ENSCATG00000037622	GFM1	105598056
ENSCATG00000038292	EIF5B	105583674
ENSCATG00000039727	-	105589208
ENSCATG00000039972	-	105591796
ENSCATG00000040932	GUF1	105571336
ENSCATG00000043042	HBS1L	105600418
ENSCATG00000044697	-	-

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.