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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 466730     1 MKLVGSYTSPFVRKLSILLLEKGITFEFINELPYNADNGVAQF---NPLGKVPVLVtEEGECWFDSPIIAEYIELMNVAP 77
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFlalNPLGKVPVLV-DDGLVLTESLAILEYLAERYPEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 466730    78 AMLPRDPLESLRVRKIEALADGIMDAGLVSVREQARPAaqQSEDELLRQREKINRSLDVLEGYLVDGT-LKTDTVNLATI 156
Cdd:COG0625  81 PLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPE--KDPAAIARARAELARLLAVLEARLAGGPyLAGDRFSIADI 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 466730   157 AIACAVGYLNFRRVAPGwcvDRPHLVKLVENLFSRESFARTEPP 200
Cdd:COG0625 159 ALAPVLRRLDRLGLDLA---DYPNLAAWLARLAARPAFQRALAA 199

Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 466730       8 TSPFVRKLSILLLEKGITFE--FINELPYNADNGVAQFNPLGKVPVLVTEEGECWFDSPIIAEYIE 71
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEieLVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLE 66

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

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 466730     1 MKLVGSYTSPFVRKLSILLLEKGITFEFINELPYNADNGVAQF---NPLGKVPVLVtEEGECWFDSPIIAEYIELMNVAP 77
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFlalNPLGKVPVLV-DDGLVLTESLAILEYLAERYPEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 466730    78 AMLPRDPLESLRVRKIEALADGIMDAGLVSVREQARPAaqQSEDELLRQREKINRSLDVLEGYLVDGT-LKTDTVNLATI 156
Cdd:COG0625  81 PLLPADPAARARVRQWLAWADGDLHPALRNLLERLAPE--KDPAAIARARAELARLLAVLEARLAGGPyLAGDRFSIADI 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 466730   157 AIACAVGYLNFRRVAPGwcvDRPHLVKLVENLFSRESFARTEPP 200
Cdd:COG0625 159 ALAPVLRRLDRLGLDLA---DYPNLAAWLARLAARPAFQRALAA 199

GST_N family, unknown subfamily 3; composed of uncharacterized bacterial 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 466730     1 MKLVGSYTSPFVRKLSILLLEKG--ITFEFINELPYNADNGVAQFNPLGKVPVLVTEEGECWFDSPIIAEYIE 71
Cdd:cd03049   1 MKLLYSPTSPYVRKVRVAAHETGlgDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYLD 73

Glutathione S-transferase (GST) family, N-terminal 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 subfamily, a member of the DsbA family). 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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, metaxin 2 and stringent starvation protein A.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 466730     1 MKLVGSYTSPFVRKLSILLLEKGITFEFIN-ELPYNADNGVAQFNPLGKVPVLVTeEGECWFDSPIIAEYIE 71
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPvDLGEGEQEEFLALNPLGKVPVLED-GGLVLTESLAILEYLA 71

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 466730     1 MKLVGSYTSPFVRKLSILLLEKGITFEFINELPYNADNGVAQF---NPLGKVPVLVTEEGECWFDSPIIAEYIE 71
Cdd:cd03051   1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFlakNPAGTVPVLELDDGTVITESVAICRYLE 74

GST_N family, Class Tau 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. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 466730     1 MKLVGSYTSPFVRKLSILLLEKGITFEFINELPYNADNGVAQFNPL-GKVPVLVtEEGECWFDSPIIAEYIE 71
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVhKKIPVLL-HNGKPICESLIIVEYID 71

Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain.

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 466730       1 MKLVGSYTSPFVRKLSILLLEKGITFEFINELPYNADNGVAQF---NPLGKVPVLVTeEGECWFDSPIIAEYI 70
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELlklNPLGKVPALED-GGKKLTESRAILEYI 74

GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) 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 TRX-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 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.

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 466730    29 INELPYNADNGVAQF---NPLGKVPVLVTEEGECWFDSPIIAEYI 70
Cdd:cd03044  28 IVDFQPGKENKTPEFlkkFPLGKVPAFEGADGFCLFESNAIAYYV 72

GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. 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. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 466730     1 MKLVGSYTSPFVRKLSILLLEKGITFEFINELPYNADNGVAQF---NPLGKVPVLVtEEGECWFDSPIIAEYI 70
Cdd:cd03053   2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHlarNPFGQIPALE-DGDLKLFESRAITRYL 73

GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 466730    18 LLLEK-GITFEFINELPYNADNG--VAQFNPLGKVPVLVTEEGECWfDSPIIAEYI 70
Cdd:cd03043  18 LLLKAaGIPFEEILVPLYTPDTRarILEFSPTGKVPVLVDGGIVVW-DSLAICEYL 72

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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 466730     7 YTSPFVRKLSI--LLLEKGITFEFInelPYNADNGVA------QFNPLGKVPVLVtEEGECWFDSPIIAEYI 70
Cdd:cd03046   4 YHLPRSRSFRIlwLLEELGLPYELV---LYDRGPGEQappeylAINPLGKVPVLV-DGDLVLTESAAIILYL 71

glutathione transferase;

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 466730      7 YTSPFVRKLSILLLEKGITFEfINELPYNAD----NGVAQFNPLGKVPVLvtEEGECWF-DSPIIAEYIELMNVAP---A 78
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFE-LKTVDLDAGehlqPTYQGYSLTRRVPTL--QHDDFELsESSAIAEYLEERFAPPaweR 90

                         90
                 ....*....|....*..
gi 466730     79 MLPRDPLESLRVRKIEA 95
Cdd:PRK15113  91 IYPADLQARARARQIQA 107