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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573765318   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:cd01883    37 EAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNM 94

translation elongation factor EF-1 alpha; This model represents the counterpart of bacterial EF-Tu for the Archaea (aEF-1 alpha) and Eukaryotes (eEF-1 alpha). The trusted cutoff is set fairly high so that incomplete sequences will score between suggested and trusted cutoff levels. [Protein synthesis, Translation factors]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573765318   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:TIGR00483  45 EAQEKGKASFEFAWVMDRLKEERERGVTIDVAHWKFETDKYEVTIVDCPGHRDFIKNM 102

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
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573765318   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:cd01883    37 EAKEMGKESFKYAWVLDKLKEERERGVTIDVGLAKFETEKYRFTIIDAPGHRDFVKNM 94

elongation factor 1-alpha; Reviewed

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573765318   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:PRK12317   44 EAKEKGKESFKFAWVMDRLKEERERGVTIDLAHKKFETDKYYFTIVDCPGHRDFVKNM 101

elongation factor 1-alpha; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573765318   1 EAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:PLN00043   45 EAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNM 102

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1573765318  14 WVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:cd00881    35 TFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKET 79

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1573765318   6 GKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RYYVtVIDAPGHRDFIKNM 58
Cdd:COG2895    60 GTQEIDLALLTDGLQAEREQGITIDVAYRYFSTPkRKFI-IADTPGHEQYTRNM 112

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1573765318   8 GSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:TIGR02034  47 GEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIVADTPGHEQYTRNM 97

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1573765318   8 GSFKYAWVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:PRK05506   71 DEIDLALLVDGLAAEREQGITIDVAYRYFATPKRKFIVADTPGHEQYTRNM 121

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
                  ....*....|....*....|....*....|....*....|...
gi 1573765318  17 DKLKAERERGITIDIALWKFETPRYY-VTVIDAPGHRDFIKNM 58
Cdd:COG3276    26 DRLKEEKKRGITIDLGFAYLPLPDGRrLGFVDVPGHEKFIKNM 68

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 1573765318   3 AELGKGSFKYAWVLDKLKAERERGITIDIALWKFETP-RYYVTViDAPGHRDFIKNM 58
Cdd:cd01884    27 AKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETAnRHYAHV-DCPGHADYIKNM 82

sulfate adenylyltransferase subunit 1; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1573765318  12 YAWVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:PRK05124   78 LALLVDGLQAEREQGITIDVAYRYFSTEKRKFIIADTPGHEQYTRNM 124

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
                  ....*....|....*....|....*....|....*....|..
gi 1573765318  17 DKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:TIGR00475  26 DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67

elongation factor Tu

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1573765318   2 AAELGKGSFKYAWVlDKLKAERERGITIDIALWKFETP-RYYVTViDAPGHRDFIKNM 58
Cdd:CHL00071   37 AAKGGAKAKKYDEI-DSAPEEKARGITINTAHVEYETEnRHYAHV-DCPGHADYVKNM 92

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        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1573765318  16 LDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDFIKNM 58
Cdd:cd04168    39 TDSMELERQRGITIFSAVASFQWEDTKVNIIDTPGHMDFIAEV 81

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        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1573765318  16 LDKLKAERERGITIDIALWKFETP--------------RYYVTVIDAPGHRDFIK 56
Cdd:cd01889    29 FDKNPQSQERGITLDLGFSSFEVDkpkhlednenpqieNYQITLVDCPGHASLIR 83

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 1573765318  15 VLDKLKAERERGITID---IALwKFETPR-------YYVTVIDAPGHRDF 54
Cdd:cd01885    37 YLDTREDEQERGITIKssaISL-YFEYEEekmdgndYLINLIDSPGHVDF 85

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1573765318   6 GKGSFKYAwVLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDF 54
Cdd:cd04169    37 ARKSRKHA-TSDWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHEDF 84

selenocysteinyl-tRNA-specific translation factor; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1573765318  17 DKLKAERERGITIDI--ALWKFETPRYyVTVIDAPGHRDFIKNM 58
Cdd:PRK10512   26 DRLPEEKKRGMTIDLgyAYWPQPDGRV-LGFIDVPGHEKFLSNM 68

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
                  ....*....|....*....|....*....|....*....|...
gi 1573765318  15 VLDKLKAERERGITIdiaLWK---FETPRYYVTVIDAPGHRDF 54
Cdd:cd01891    39 VMDSNDLERERGITI---LAKntaITYKDTKINIIDTPGHADF 78

elongation factor G-like protein;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1573765318  15 VLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDF 54
Cdd:PRK13351   47 VTDWMPQEQERGITIESAATSCDWDNHRINLIDTPGHIDF 86

translational GTPase TypA;

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1573765318  15 VLDKLKAERERGITIDIALWKFETPRYYVTVIDAPGHRDF 54
Cdd:PRK10218   42 VMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADF 81

elongation factor 2; Provisional

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1573765318  22 ERERGITID---IALWkFETP--------RYYVTVIDAPGHRDF 54
Cdd:PTZ00416   63 EQERGITIKstgISLY-YEHDledgddkqPFLINLIDSPGHVDF 105