This family represents domain IV of archaeal and eukaryotic elongation factor 2 (aeEF-2) and of an evolutionarily conserved U5 snRNP-specific protein. U5 snRNP is a GTP-binding factor closely related to the ribosomal translocase EF-2. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site of the small subunit of ribosome and the mRNA is shifted one codon relative to the ribosome. It has been shown that EF-2_IV domain mimics the shape of anticodon arm of the tRNA in the structurally homologous ternary complex of Phe-tRNA, EF-1 (another transcriptional elongation factor) and GTP analog. The tip portion of this domain is found in a position that overlaps the anticodon arm of the A-site tRNA, implying that EF-2 displaces the A-site tRNA to the P-site by physical interaction with the anticodon arm.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480546651   1 HNRIYVKAQRLDEEVSQDIESGVINP*DDFKARARVLADKHGWDVTDARKIWCFGPDGRGPNVVVDQTKAVQY----LNE 76
Cdd:cd01681   26 HNRLYMRAEPLPEELIEDIEKGKITLKDDKKKRARILLDKYGWDKLAARKIWAFGPDRTGPNILVDDTKGVQYdkslLNE 105

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480546651  77 IKDSVVAAFQWATKEGPIFGEDVRSVRINILDVTMHADAIHRGGGQIIPTMRRVTYASMLLAEPAIQEPVFL 148
Cdd:cd01681  106 IKDSIVAGFQWATKEGPLCEEPMRGVKFKLEDATLHADAIHRGGGQIIPAARRACYAAFLLASPRLMEPMYL 177

Elongation factor G, domain IV; 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 EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome. EF2 has five domains. This entry represents domain IV found in EF2 (or EF-G) of both prokaryotes and eukaryotes. The EF2-GTP-ribosome complex undergoes extensive structural rearrangement for tRNA-mRNA movement to occur. Domain IV, which extends from the 'body' of the EF2 molecule much like a lever arm, appears to be essential for the structural transition to take place.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480546651    26 P*DDFKARARVLADKHGWDVTDARKIWCFGPDGRGPNVVVDQTK--AVQYLnEIKDSVVAAFQWATKEGPIFGEDVRSVR 103
Cdd:smart00889   8 ITKPVKEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDTIvgGVIPK-EYIPAVEKGFREALEEGPLAGYPVVDVK 86

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 480546651   104 INILDVTMHADaIHRGGGqIIPTMRRVTYASMLLAE 139
Cdd:smart00889  87 VTLLDGSYHEV-DSSEMA-FKPAARRAFKEALLKAG 120

translation elongation factor EF-2 subunit; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480546651   1 HNRIYVKAQRLDEEVSQDIESGVINP*DDFKARARVLADKHGWDVTDARKIWCFGPDGRGPNVVVDQTKAVQYLNEIKDS 80
Cdd:PLN00116 584 HNRLYMEARPLEEGLAEAIDDGRIGPRDDPKIRSKILAEEFGWDKDLAKKIWCFGPETTGPNMVVDMCKGVQYLNEIKDS 663

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480546651  81 VVAAFQWATKEGPIFGEDVRSVRINILDVTMHADAIHRGGGQIIPTMRRVTYASMLLAEPAIQEPVFLVEIQCPENAIGG 160
Cdd:PLN00116 664 VVAGFQWATKEGALAEENMRGICFEVCDVVLHADAIHRGGGQIIPTARRVIYASQLTAKPRLLEPVYLVEIQAPEQALGG 743

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 480546651 161 IYSVLNKKRGQVISEEQRPGTPLFTVKAYMPVNESFGFSGELRQATGGQ 209
Cdd:PLN00116 744 IYSVLNQKRGHVFEEMQRPGTPLYNIKAYLPVIESFGFSGTLRAATSGQ 792

elongation factor EF-2; Reviewed

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480546651   1 HNRIYVKAQRLDEEVSQDIESGVINP*DDFKARaRVLAD---KHGWDVTDARKIWCFgpdgRGPNVVVDQTKAVQYLNEI 77
Cdd:PRK07560 484 HNRFYISVEPLEEEVIEAIKEGEISEDMDKKEA-KILREkliEAGMDKDEAKRVWAI----YNGNVFIDMTKGIQYLNEV 558

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480546651  78 KDSVVAAFQWATKEGPIFGEDVRSVRINILDVTMHADAIHRGGGQIIPTMRRVTYASMLLAEPAIQEPVFLVEIQCPENA 157
Cdd:PRK07560 559 MELIIEGFREAMKEGPLAAEPVRGVKVRLHDAKLHEDAIHRGPAQVIPAVRNAIFAAMLTAKPTLLEPIQKVDINVPQDY 638

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 480546651 158 IGGIYSVLNKKRGQVISEEQRPGtpLFTVKAYMPVNESFGFSGELRQATGG 208
Cdd:PRK07560 639 MGAVTREIQGRRGKILDMEQEGD--MAIIEAEAPVAEMFGFAGEIRSATEG 687

eEF2_snRNP_like_C: this family represents a C-terminal domain of eukaryotic elongation factor 2 (eEF-2) and a homologous domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480546651 144 EPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTPLFTVKAYMPVNESFGFSGELRQATGGQ 209
Cdd:cd04096    1 EPIYLVEIQCPEDALGKVYSVLSKRRGHVLSEEPKEGTPLFEIKAYLPVIESFGFETDLRSATSGQ 66

Elongation factor G, domain IV; 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 EF2 (EF-G) is a G-protein. It brings about the translocation of peptidyl-tRNA and mRNA through a ratchet-like mechanism: the binding of GTP-EF2 to the ribosome causes a counter-clockwise rotation in the small ribosomal subunit; the hydrolysis of GTP to GDP by EF2 and the subsequent release of EF2 causes a clockwise rotation of the small subunit back to the starting position. This twisting action destabilises tRNA-ribosome interactions, freeing the tRNA to translocate along the ribosome upon GTP-hydrolysis by EF2. EF2 binding also affects the entry and exit channel openings for the mRNA, widening it when bound to enable the mRNA to translocate along the ribosome. EF2 has five domains. This entry represents domain IV found in EF2 (or EF-G) of both prokaryotes and eukaryotes. The EF2-GTP-ribosome complex undergoes extensive structural rearrangement for tRNA-mRNA movement to occur. Domain IV, which extends from the 'body' of the EF2 molecule much like a lever arm, appears to be essential for the structural transition to take place.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480546651    26 P*DDFKARARVLADKHGWDVTDARKIWCFGPDGRGPNVVVDQTK--AVQYLnEIKDSVVAAFQWATKEGPIFGEDVRSVR 103
Cdd:smart00889   8 ITKPVKEAEGKHKKQSGGDGQYARVILEVEPLERGSGFEFDDTIvgGVIPK-EYIPAVEKGFREALEEGPLAGYPVVDVK 86

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 480546651   104 INILDVTMHADaIHRGGGqIIPTMRRVTYASMLLAE 139
Cdd:smart00889  87 VTLLDGSYHEV-DSSEMA-FKPAARRAFKEALLKAG 120

eEF2_C_snRNP: This family includes a C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and, its yeast counterpart Snu114p. This domain is homologous to the C-terminal domain of the eukaryotic translational elongation factor EF-2. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of the U5-116 kD/Snu114p. In complex with GTP, EF-2 promotes the translocation step of translation. During translocation the peptidyl-tRNA is moved from the A site to the P site, the uncharged tRNA from the P site to the E-site and, the mRNA is shifted one codon relative to the ribosome.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480546651 144 EPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTPLFTVKAYMPVNESFGFSGELRQATGGQ 209
Cdd:cd04098    1 EPIYEVEITCPADAVSAVYEVLSRRRGHVIYDTPIPGTPLYEVKAFIPVIESFGFETDLRVHTQGQ 66

Elongation factor G C-terminus; This domain includes the carboxyl terminal regions of Elongation factor G, elongation factor 2 and some tetracycline resistance proteins and adopt a ferredoxin-like fold.

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480546651   144 EPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGtpLFTVKAYMPVNESFGFSGELRQATGG 208
Cdd:smart00838   3 EPIMKVEVTVPEEYMGDVIGDLNSRRGKIEGMEQRGG--AQVIKAKVPLSEMFGYATDLRSATQG 65

EFG_mtEFG_C: domains similar to the C-terminal domain of the bacterial translational elongation factor (EF) EF-G. Included in this group is the C-terminus of mitochondrial Elongation factor G1 (mtEFG1) and G2 (mtEFG2) proteins. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. In bacteria this translocation step is catalyzed by EF-G_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. No clear phenotype has been found for mutants in the yeast homologue of mtEFG2, MEF2.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480546651 144 EPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTplFTVKAYMPVNESFGFSGELRQATGGQ 209
Cdd:cd03713    1 EPIMKVEVTVPEEYMGDVIGDLSSRRGQILGTESRGGW--KVIKAEVPLAEMFGYSTDLRSLTQGR 64

elongation factor G-like protein EF-G2;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480546651  80 SVVAAFQWATKEGPIFGEDVRSVRINILDVTMHA----DAIHRGGGQIipTMRrvtyASMLLAEPAIQEPVFLVEIQCPE 155
Cdd:PRK12740 520 AVEKGVREALEKGVLAGYPVVDVKVTLTDGSYHSvdssEMAFKIAARL--AFR----EALPKAKPVLLEPIMKVEVSVPE 593

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 480546651 156 NAIGGIYSVLNKKRGQVISEEQRPGTplFTVKAYMPVNESFGFSGELRQATGGQ 209
Cdd:PRK12740 594 EFVGDVIGDLSSRRGRILGMESRGGG--DVVRAEVPLAEMFGYATDLRSLTQGR 645

mtEFG1_C: C-terminus of mitochondrial Elongation factor G1 (mtEFG1)-like proteins found in eukaryotes. Eukaryotic cells harbor 2 protein synthesis systems: one localized in the cytoplasm, the other in the mitochondria. Most factors regulating mitochondrial protein synthesis are encoded by nuclear genes, translated in the cytoplasm, and then transported to the mitochondria. The eukaryotic system of elongation factor (EF) components is more complex than that in prokaryotes, with both cytoplasmic and mitochondrial elongation factors and multiple isoforms being expressed in certain species. Eukaryotic EF-2 operates in the cytosolic protein synthesis machinery of eukaryotes, EF-Gs in protein synthesis in bacteria. Eukaryotic mtEFG1 proteins show significant homology to bacterial EF-Gs. Mutants in yeast mtEFG1 have impaired mitochondrial protein synthesis, respiratory defects and a tendency to lose mitochondrial DNA. There are two forms of mtEFG present in mammals (designated mtEFG1s and mtEFG2s) mtEFG2s are not present in this group.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480546651 144 EPVFLVEIQCPENAIGGIYSVLNKKRGQVISEEQRPGTplFTVKAYMPVNESFGFSGELRQATGG 208
Cdd:cd04097    1 EPIMKVEVTAPTEFQGNVIGLLNKRKGTIVDTDTGEDE--FTLEAEVPLNDMFGYSTELRSMTQG 63