C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.

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                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75313298   5 FSDLHTEEGVKSVEEHLAGKTYISGDQLSVDDVKVYAAVPVKPSDA-FPNASKWYESVAS 63
Cdd:cd10308  22 FADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATkFPHLARWYRHIAS 81

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75313298 133 SGKSSVLMDVKPWDDETDMKKLEEAVRGVEMPGLFWGASKLVPVGYGIKKLTIMFTIVDDLVSPDNLIEDFltsePNNEY 212
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAI----SEEDG 76

                        90
                ....*....|..
gi 75313298 213 IQSCDIVAFNKI 224
Cdd:cd00292  77 VQSVDVEAFNKL 88

Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.

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                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75313298   5 FSDLHTEEGVKSVEEHLAGKTYISGDQLSVDDVKVYAAVPVKPSDA-FPNASKWYESVAS 63
Cdd:cd10308  22 FADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATkFPHLARWYRHIAS 81

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.

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                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75313298 133 SGKSSVLMDVKPWDDETDMKKLEEAVRGVEMPGLFWGASKLVPVGYGIKKLTIMFTIVDDLVSPDNLIEDFltsePNNEY 212
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAI----SEEDG 76

                        90
                ....*....|..
gi 75313298 213 IQSCDIVAFNKI 224
Cdd:cd00292  77 VQSVDVEAFNKL 88

Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.

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                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75313298   5 FSDLHTEEGVKSVEEHLAGKTYISGDQLSVDDVKVYAAVPVKPSDA-FPNASKWYESVAS 63
Cdd:cd10308  22 FADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATkFPHLARWYRHIAS 81

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.

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                  ....*....|....*....|....*....|....*....|....*....|....*
gi 75313298    17 VEEHLAGKTYISGDQLSVDDVKVYAA-------VPVKPSDAFPNASKWYESVASQ 64
Cdd:pfam00043  38 LEEVLKGQTYLVGDKLTLADIALAPAllwlyelDPACLREKFPNLKAWFERVAAR 92

Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Cysteinyl-tRNA synthetase (CysRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of CysRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of CysRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. CysRSs from prokaryotes and lower eukaryotes do not appear to contain this GST_C-like domain.

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                ....*....|....*....|....*....|....*....|....*....|
gi 75313298  14 VKSVEEHLAGKTYISGDQLSVDDVKVYAAVPVKPSDAFPNASKWYESVAS 63
Cdd:cd10310  23 AEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPADRLVHVLRWYRHIEA 72

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds to membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.

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                ....*....|....*....|....*....|....*....|....*....|....*....
gi 75313298  14 VKSVEEHLAGKTYISGDQLSVDDVKV-------YAAVPVKP-SDAFPNASKWYESVASQ 64
Cdd:cd03181  49 LGVLEEHLLTRTYLVGERITLADIFVasallrgFETVLDPEfRKKYPNVTRWFNTVVNQ 107

C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 75313298  17 VEEHLAGKTYISGDQLSVDDVKVYAAVPVKPS-----DAFPNASKWYESVasqlaKSFPG 71
Cdd:cd03206  45 LDQHLAGRDWLAGDRPTIADVACYPYIALAPEggvslEPYPAIRAWLARV-----EALPG 99