Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors

                          10        20        30
                  ....*....|....*....|....*....|
gi 1786712910   1 MGKAKFERNKPHVNIGTIGHVDHGKTTLTA 30
Cdd:COG0050     1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTA 30

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. EF-Tu is one of the most abundant proteins in bacteria, as well as, one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation.

                          10        20
                  ....*....|....*....|
gi 1786712910  11 PHVNIGTIGHVDHGKTTLTA 30
Cdd:cd01884     1 PHVNVGTIGHVDHGKTTLTA 20

Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-Tu, a GTPase is part of the Pathway/BioSystem: Translation factors

                          10        20        30
                  ....*....|....*....|....*....|
gi 1786712910   1 MGKAKFERNKPHVNIGTIGHVDHGKTTLTA 30
Cdd:COG0050     1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTA 30

elongation factor Tu; Reviewed

                          10        20        30
                  ....*....|....*....|....*....|
gi 1786712910   1 MGKAKFERNKPHVNIGTIGHVDHGKTTLTA 30
Cdd:PRK12736    1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTA 30

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]

                          10        20        30
                  ....*....|....*....|....*....|
gi 1786712910   1 MGKAKFERNKPHVNIGTIGHVDHGKTTLTA 30
Cdd:TIGR00485   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTA 30

Elongation factor Tu; Provisional

                          10        20
                  ....*....|....*....|....*..
gi 1786712910   4 AKFERNKPHVNIGTIGHVDHGKTTLTA 30
Cdd:PLN03127   53 ATFTRTKPHVNVGTIGHVDHGKTTLTA 79

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.

                          10        20
                  ....*....|....*....|.
gi 1786712910  10 KPHVNIGTIGHVDHGKTTLTA 30
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTD 21

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors

                          10        20
                  ....*....|....*....|..
gi 1786712910   8 RNKPHVNIGTIGHVDHGKTTLT 29
Cdd:COG5257     1 KKQPEVNIGVVGHVDHGKTTLV 22

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.

                          10
                  ....*....|....*..
gi 1786712910  13 VNIGTIGHVDHGKTTLT 29
Cdd:cd01888     1 INIGTIGHVAHGKTTLV 17

Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1alpha (GTPase) is part of the Pathway/BioSystem: Translation factors

                          10        20
                  ....*....|....*....|..
gi 1786712910   8 RNKPHVNIGTIGHVDHGKTTLT 29
Cdd:COG5256     3 SEKPHLNLVVIGHVDHGKSTLV 24

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.

                          10
                  ....*....|....*.
gi 1786712910  14 NIGTIGHVDHGKTTLT 29
Cdd:cd01885     2 NICIIAHVDHGKTTLS 17

elongation factor EF-2; Reviewed

                          10
                  ....*....|....*.
gi 1786712910  14 NIGTIGHVDHGKTTLT 29
Cdd:PRK07560   22 NIGIIAHIDHGKTTLS 37

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];

                          10
                  ....*....|....*
gi 1786712910  14 NIGTIGHVDHGKTTL 28
Cdd:COG1217     8 NIAIIAHVDHGKTTL 22

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.

                          10
                  ....*....|....*.
gi 1786712910  13 VNIGTIGHVDHGKTTL 28
Cdd:cd01889     1 VNVGLLGHVDSGKTSL 16

selenocysteinyl-tRNA-specific translation factor; Provisional

                          10
                  ....*....|....
gi 1786712910  15 IGTIGHVDHGKTTL 28
Cdd:PRK10512    3 IATAGHVDHGKTTL 16

GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]

                          10
                  ....*....|....*
gi 1786712910  14 NIGTIGHVDHGKTTL 28
Cdd:TIGR01394   3 NIAIIAHVDHGKTTL 17

elongation factor 1- alpha; Provisional

                          10        20
                  ....*....|....*....|....*....
gi 1786712910   1 MGKakferNKPHVNIGTIGHVDHGKTTLT 29
Cdd:PTZ00141    1 MGK-----EKTHINLVVIGHVDSGKSTTT 24

selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]

                          10
                  ....*....|....*.
gi 1786712910  13 VNIGTIGHVDHGKTTL 28
Cdd:TIGR00475   1 MIIATAGHVDHGKTTL 16

elongation factor G-like protein;

                          10
                  ....*....|....*.
gi 1786712910  14 NIGTIGHVDHGKTTLT 29
Cdd:PRK13351   10 NIGILAHIDAGKTTLT 25

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors

                          10
                  ....*....|....*.
gi 1786712910  14 NIGTIGHVDHGKTTLT 29
Cdd:COG0480    11 NIGIVAHIDAGKTTLT 26

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.

                          10
                  ....*....|....*.
gi 1786712910  14 NIGTIGHVDHGKTTLT 29
Cdd:cd04168     1 NIGILAHVDAGKTTLT 16

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.

                          10
                  ....*....|....*.
gi 1786712910  14 NIGTIGHVDHGKTTLT 29
Cdd:cd01883     1 NLVVIGHVDAGKSTLT 16

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]

                          10        20
                  ....*....|....*....|....*
gi 1786712910   4 AKFERNKPHVNIgtIGHVDHGKTTL 28
Cdd:TIGR00487  81 DLLVERPPVVTI--MGHVDHGKTSL 103

elongation factor 1-alpha; Provisional

                          10        20        30
                  ....*....|....*....|....*....|
gi 1786712910   1 MGKAKFernkpHVNIGTIGHVDHGKTTLTA 30
Cdd:PLN00043    1 MGKEKV-----HINIVVIGHVDSGKSTTTG 25