Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108598884 355 IAKSSILLDVKPWDDETDMAKLEECVRSVQMDGLLWGASKLVPVGYGIKKLQINCVVEDDKVGTDILEEEITKfEDYIQS 434
Cdd:cd00292     1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79

                  ....*....
gi 2108598884 435 VDVAAFNKI 443
Cdd:cd00292    80 VDVEAFNKL 88

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108598884 355 IAKSSILLDVKPWDDETDMAKLEECVRSVQMDGLLWGASKLVPVGYGIKKLQINCVVEDDKVGTDILEEEITKfEDYIQS 434
Cdd:cd00292     1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79

                  ....*....
gi 2108598884 435 VDVAAFNKI 443
Cdd:cd00292    80 VDVEAFNKL 88

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. 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. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108598884  357 KSSILLDVKPWDDETDMAKLEECVRS-VQMDGLLWGAS-KLVPVGYGIKKLQINCVVEDDKVGTDILEEEITKFEDyIQS 434
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSiLPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG-VQS 79

                   ....*....
gi 2108598884  435 VDVAAFNKI 443
Cdd:smart00888  80 VEVEAVSRL 88

elongation factor 1-beta; Validated

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108598884 362 LDVKPWDDETDMAKLEECVRSVqmdglLWGASKL-----VPVGYGIKKLQINCVVEDDKVGTDILEEEITKFEDyIQSVD 436
Cdd:PRK00435    8 LKVMPESPEVDLDELKEKIKEV-----LPEGYKIngieeEPIAFGLKALKLYVIMPDEEGGTEPVEEAFANVEG-VESVE 81

                  .
gi 2108598884 437 V 437
Cdd:PRK00435   82 V 82

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108598884 355 IAKSSILLDVKPWDDETDMAKLEECVRSVQMDGLLWGASKLVPVGYGIKKLQINCVVEDDKVGTDILEEEITKfEDYIQS 434
Cdd:cd00292     1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79

                  ....*....
gi 2108598884 435 VDVAAFNKI 443
Cdd:cd00292    80 VDVEAFNKL 88

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. 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. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108598884  357 KSSILLDVKPWDDETDMAKLEECVRS-VQMDGLLWGAS-KLVPVGYGIKKLQINCVVEDDKVGTDILEEEITKFEDyIQS 434
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSiLPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG-VQS 79

                   ....*....
gi 2108598884  435 VDVAAFNKI 443
Cdd:smart00888  80 VEVEAVSRL 88

elongation factor 1-beta; Validated

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2108598884 362 LDVKPWDDETDMAKLEECVRSVqmdglLWGASKL-----VPVGYGIKKLQINCVVEDDKVGTDILEEEITKFEDyIQSVD 436
Cdd:PRK00435    8 LKVMPESPEVDLDELKEKIKEV-----LPEGYKIngieeEPIAFGLKALKLYVIMPDEEGGTEPVEEAFANVEG-VESVE 81

                  .
gi 2108598884 437 V 437
Cdd:PRK00435   82 V 82