C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453307 172 PPALQSKIDELNGWIYDNVNNGVYKAGFATSQQAYDEAVEKVFTALARLEQILGQHRYLTGDQLTEADIRLWTTLVRFDP 251
Cdd:cd03190    1 PEELRKEIDELNEWIYDNINNGVYKAGFATTQEAYDKAVKELFEALDKLEKRLSKQPYLLGDRLTEADIRLFTTLIRFDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453307 252 VYVTHFKCDKYRISDYLNLYGFLRDIYQIPGIAETVNLDHIRHHYFRSHKTINPTGIISIGP 313
Cdd:cd03190   81 VYHQHFKCNLKTIRDYPNLWRYLRRLYQNPGVFETTNFDHIKQHYYGSHFPINPNGIVPAGP 142

C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453307 172 PPALQSKIDELNGWIYDNVNNGVYKAGFATSQQAYDEAVEKVFTALARLEQILGQHRYLTGDQLTEADIRLWTTLVRFDP 251
Cdd:cd03190    1 PEELRKEIDELNEWIYDNINNGVYKAGFATTQEAYDKAVKELFEALDKLEKRLSKQPYLLGDRLTEADIRLFTTLIRFDP 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446453307 252 VYVTHFKCDKYRISDYLNLYGFLRDIYQIPGIAETVNLDHIRHHYFRSHKTINPTGIISIGP 313
Cdd:cd03190   81 VYHQHFKCNLKTIRDYPNLWRYLRRLYQNPGVFETTNFDHIKQHYYGSHFPINPNGIVPAGP 142

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.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453307 179 IDELNGWIYDNVNNGVYKAGFA------TSQQAYDEAVEKVFTALARLEQILGQHRYLTGDQLTEADIRLWTTLVRFDPV 252
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLekvplpKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80

                         90
                 ....*....|....*...
gi 446453307 253 YVTHFKCDKY-RISDYLN 269
Cdd:cd00299   81 GPYYDLLDEYpRLKAWYD 98

Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453307  57 LYVSLACPWAHRTLIFRKLKGLePF--IPVSVVnplmlengwtFDDTFPAatgdtlyqhEFLyqlylhadpHYSGRVTVP 134
Cdd:COG0625    4 LYGSPPSPNSRRVRIALEEKGL-PYelVPVDLA----------KGEQKSP---------EFL---------ALNPLGKVP 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453307 135 VLWDkkNHTIVSnESAEIIRMFNSAFDGLGAKAGDyypPALQSKIDELNGW----IYDNVNNGVYKAGFATSQQAYDEAV 210
Cdd:COG0625   55 VLVD--DGLVLT-ESLAILEYLAERYPEPPLLPAD---PAARARVRQWLAWadgdLHPALRNLLERLAPEKDPAAIARAR 128

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446453307 211 EKVFTALARLEQILGQHRYLTGDQLTEADIRLWTTLVRFDpvyvtHFKCDkyrISDYLNLYGFLRDIYQIPGIAETV 287
Cdd:COG0625  129 AELARLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLD-----RLGLD---LADYPNLAAWLARLAARPAFQRAL 197

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.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 446453307 203 QQAYDEAVEKVFTALARLEQILGQHRYLTGDQLTEADIRLWTTLVRF 249
Cdd:cd03181   35 KKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLRG 81

C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon subfamily; 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. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446453307 207 DEAVEKVFTALARLEQILGQHRYLTGDQLTEADIRLWTTLVRFD 250
Cdd:cd03177   37 EEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVSTLE 80

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. 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. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446453307 215 TALARLEQILGQHRYLTGDQLTEADIRLW---TTLVRFDPvyvthfkcdkyRISDYLNLYGFLRDIYQIP 281
Cdd:cd03189   65 RHLDFLEDHLAKHPYFAGDELTAADIMMSfplEAALARGP-----------LLEQYPNIAAYLERIEARP 123