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        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542762990   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGIT 62
Cdd:COG0050     1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGIT 62

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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1542762990  11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGIT 62
Cdd:cd01884     1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGIT 52

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        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542762990   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGIT 62
Cdd:COG0050     1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGIT 62

elongation factor Tu; Reviewed

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542762990   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGIT 62
Cdd:PRK12736    1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGIT 62

elongation factor Tu

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1542762990   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGIT 62
Cdd:CHL00071    1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGIT 62

Elongation factor Tu; Provisional

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1542762990   2 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQIDNAPEEKARGIT 62
Cdd:PLN03127   51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGIT 111

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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1542762990  10 KPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGSARAFDQ---IDNAPEEKARGIT 62
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGIT 56

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1542762990  13 VNVGTIGHVDHGKTTLTAAITTVLAktyggsarafdqiDNAPEEKARGIT 62
Cdd:COG3276     1 MIIGTAGHIDHGKTTLVKALTGIDT-------------DRLKEEKKRGIT 37

translation initiation factor IF-2 subunit gamma; Validated

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1542762990   7 ERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgsarafdqidnapEEKARGIT 62
Cdd:PRK04000    4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGIT 46

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        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1542762990   8 RTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgsarafdqidnapEEKARGIT 62
Cdd:COG5257     1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGIT 42

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        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1542762990  13 VNVGTIGHVDHGKTTLTAAITTVlaktyggsarafdQIDNAPEEKARGIT 62
Cdd:cd01888     1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNIT 37

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        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1542762990  13 VNVGTIGHVDHGKTTLTAAITTVLAktyggsarafdqiDNAPEEKARGIT 62
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMT 37

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        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1542762990  14 NVGTIGHVDHGKTTLTAA-------ITTVLAktygGSARAfdqIDNAPEEKARGIT 62
Cdd:cd01885     2 NICIIAHVDHGKTTLSDSllasagiISEKLA----GKARY---LDTREDEQERGIT 50

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        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1542762990   8 RTKPHVNVGTIGHVDHGKTTL-------TAAITTVLAKTYGGSARAFDQ--------IDNAPEEKARGIT 62
Cdd:COG5256     3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKKGKesfkfawvMDRLKEERERGVT 72

elongation factor 2; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1542762990  14 NVGTIGHVDHGKTTLTAAITT---VLAKTYGGSARAfdqIDNAPEEKARGIT 62
Cdd:PTZ00416   21 NMSVIAHVDHGKSTLTDSLVCkagIISSKNAGDARF---TDTRADEQERGIT 69

eukaryotic translation initiation factor 2 gamma subunit; Provisional

                          10        20
                  ....*....|....*....|...
gi 1542762990  13 VNVGTIGHVDHGKTTLTAAITTV 35
Cdd:PTZ00327   35 INIGTIGHVAHGKSTVVKALSGV 57

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1542762990  14 NVGTIGHVDHGKTTLTAAITtvlakTYGGSARAFDQI-----DNAPEEKARGIT 62
Cdd:cd01891     4 NIAIIAHVDHGKTTLVDALL-----KQSGTFRENEEVgervmDSNDLERERGIT 52

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        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1542762990  14 NVGTIGHVDHGKTTLTAAI---TTVLAKTYGGSARAFDQIDnapEEKARGIT 62
Cdd:TIGR01394   3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSND---LERERGIT 51

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

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1542762990  14 NVGTIGHVDHGKTTLTAAIttvL--AKTYGGSARAFDQI-DNAPEEKARGIT 62
Cdd:COG1217     8 NIAIIAHVDHGKTTLVDAL---LkqSGTFRENQEVAERVmDSNDLERERGIT 56

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1542762990  14 NVGTIGHVDHGKTTLTAAI------TTVLAKTYGGSArafdQIDNAPEEKARGIT 62
Cdd:cd01886     1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEVHGGGA----TMDWMEQERERGIT 51

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        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1542762990  14 NVGTIGHVDHGKTTLTAAITTVL--------------AKTYGGSARAFDQI-DNAPEEKARGIT 62
Cdd:cd01883     1 NLVVIGHVDAGKSTLTGHLLYKLggvdkrtiekyekeAKEMGKESFKYAWVlDKLKEERERGVT 64

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors

                          10        20
                  ....*....|....*....|....*....
gi 1542762990  17 TI-GHVDHGKTTLTAAI--TTVLAKTYGG 42
Cdd:COG0532     8 TVmGHVDHGKTSLLDAIrkTNVAAGEAGG 36

elongation factor 1- alpha; Provisional

                          10        20
                  ....*....|....*....|....*....
gi 1542762990   1 MSKEKfertkPHVNVGTIGHVDHGKTTLT 29
Cdd:PTZ00141    1 MGKEK-----THINLVVIGHVDSGKSTTT 24

translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]

                          10        20        30
                  ....*....|....*....|....*....|
gi 1542762990  15 VGTIGHVDHGKTTLTAAI--TTVLAKTYGG 42
Cdd:TIGR00491   7 VVVLGHVDHGKTTLLDKIrgTAVVKKEAGG 36

translation initiation factor 2; Provisional

                          10        20        30
                  ....*....|....*....|....*....|
gi 1542762990  15 VGTIGHVDHGKTTLTAAI--TTVLAKTYGG 42
Cdd:CHL00189  247 VTILGHVDHGKTTLLDKIrkTQIAQKEAGG 276