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        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  91 AAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLW 170
Cdd:cd03181    1 EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 110625979 171 LYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAILGEVKLCEKM 213
Cdd:cd03181   81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123

cell envelope integrity inner membrane protein TolA; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625979 212 KMAQFDAKKFAESQPKKDTPRKEKGSREEKQKPQAERKEEKKAAAPAPEEEMDECEQALAAEPKAKD 278
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227

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        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  91 AAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLW 170
Cdd:cd03181    1 EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 110625979 171 LYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAILGEVKLCEKM 213
Cdd:cd03181   81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979   5 TLYTYPENWRAFKALIAAQYSGAQVRVLSAPPhfhFGQTNRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVsnEE- 83
Cdd:COG0625    3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDL---AKGEQKSPEFLALNPLGKVPVLV-DDGLVLTESLAILEYL--AEr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  84 -----LRGSTPEAAAQVVQWVSFADSDIVPPASTWVFPTLGimHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVT 158
Cdd:COG0625   77 ypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAP--EKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFS 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 110625979 159 LADITVVCTLLWLYKQVLEPSfrqAFPNTNRWFLTCINQPQFRAILGE 206
Cdd:COG0625  155 IADIALAPVLRRLDRLGLDLA---DYPNLAAWLARLAARPAFQRALAA 199

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  106 IVPPASTWVFPTLGIMHHNKQAT-ENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSfRQAF 184
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEvDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79

                          90
                  ....*....|....
gi 110625979  185 PNTNRWFLTCINQP 198
Cdd:pfam00043  80 PNLKAWFERVAARP 93

cell envelope integrity inner membrane protein TolA; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625979 212 KMAQFDAKKFAESQPKKDTPRKEKGSREEKQKPQAERKEEKKAAAPAPEEEMDECEQALAAEPKAKD 278
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227

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        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  91 AAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLW 170
Cdd:cd03181    1 EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 110625979 171 LYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAILGEVKLCEKM 213
Cdd:cd03181   81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123

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        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110625979   4 GTLYTYPENWRAFKALIAAQYSGAQVRVLSAPPHFhfgqTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYVSNE 82
Cdd:cd03044    1 GTLYTYPGNPRSLKILAAAKYNGLDVEIVDFQPGK----ENKTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYVANL 75

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979    2 AAGTLYTYPENWRAFKALIAAQYSGAQVRVlsAPPHFHFGQTNRtPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVSN 81
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEI--VPLDFGAGPEKS-PELLKLNPLGKVPALE-DGGKKLTESRAILEYIAR 76

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 110625979  95 VVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQ 174
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80

                         90
                 ....*....|....*..
gi 110625979 175 VLEPSFRQAFPNTNRWF 191
Cdd:cd00299   81 GPYYDLLDEYPRLKAWY 97

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 110625979   5 TLYTYPENWRAFKALIAAQYSGAQVRVLSAPPHfhfgqTNRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYV 79
Cdd:cd00570    2 KLYYFPGSPRSLRVRLALEEKGLPYELVPVDLG-----EGEQEEFLALNPLGKVPVLE-DGGLVLTESLAILEYL 70

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  89 PEAAAQVVQWVSFAdSDIVPPASTwvfptlgimhhnkqatenaKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTL 168
Cdd:cd10305    1 AEERAQVDQWLEYR-VTQVAPASD-------------------KADAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYGL 60

                         90       100
                 ....*....|....*....|...
gi 110625979 169 LWLYKQvLEPSFRQAFPNTNRWF 191
Cdd:cd10305   61 HPIMKD-LSPQEKEQYLNVSRWF 82

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  45 RTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVSNE------ELRGSTPEAAAQVVQWVS----FADSDIVPPASTWV 114
Cdd:PLN02473  41 KKPEHLLRQPFGQVPAIE-DGDLKLFESRAIARYYATKyadqgtDLLGKTLEHRAIVDQWVEvennYFYAVALPLVINLV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979 115 F-PTLGiMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSFRQAFPNTNRWFLT 193
Cdd:PLN02473 120 FkPRLG-EPCDVALVEELKVKFDKVLDVYENRLATNRYLGGDEFTLADLTHMPGMRYIMNETSLSGLVTSRENLNRWWNE 198

                        170
                 ....*....|.
gi 110625979 194 CINQPQFRAIL 204
Cdd:PLN02473 199 ISARPAWKKLM 209

Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS 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 GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 110625979 142 LDTHLKTRTFLVGERVTLADITVVCTllwLYKQVLEPSFRQAFPNTNRWF 191
Cdd:cd10309   29 LDKALSLRTYLVGNSLTLADFAVWAA---LRGNGEWLASKEKYVNVTRWF 75

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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 active site is located in a cleft between the N- and C-terminal 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  93 AQVVQWVSFADSDivppastwVFPTLGIMHH--------NKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITv 164
Cdd:cd03178    3 AEVLQWLFFQMSG--------LGPMFGQAGHflyfapekIPYAIERYTDEVKRLYGVLDKRLSDRPYLAGEEYSIADIA- 73

                         90       100
                 ....*....|....*....|....*....
gi 110625979 165 vcTLLWL--YKQVLEPSFrQAFPNTNRWF 191
Cdd:cd03178   74 --LYPWThyADLGGFADL-SEYPNVKRWL 99

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        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110625979  95 VVQWVSFADSDIVP-PASTWVFPTLGiMHHNKqatENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITV 164
Cdd:cd03206    1 VQRWLSFAAGEIAHgPAAARLIHLFG-APLDP---ERARAISHRLLRLLDQHLAGRDWLAGDRPTIADVAC 67

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
                 ....*....|....*....|....*....|....*..
gi 110625979  44 NRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVS 80
Cdd:cd03053   39 HKSPEHLARNPFGQIPALE-DGDLKLFESRAITRYLA 74

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 2; 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 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        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  93 AQVVQWVSFADSDIVPPastWVFPTLGIM-----HHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCT 167
Cdd:cd03180    4 ALADRWMDWQTSTLNPA---FRYAFWGLVrtppeQRDPAAIAASLAACNKLMAILDAQLARQAYLAGDRFTLADIALGCS 80

                         90       100
                 ....*....|....*....|....
gi 110625979 168 llwLYKQVLEPSFRQAFPNTNRWF 191
Cdd:cd03180   81 ---VYRWLELPIERPALPHLERWY 101

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625979   15 AFKALIAAQYSG--AQVRVLSAPPHfhfgqtNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYV 79
Cdd:pfam13409   5 SHRVRLALEEKGlpYEIELVDLDPK------DKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYL 65

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta 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 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  93 AQVVQWVSFADSDIVPPASTWVFPTL-GIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWL 171
Cdd:cd03188    4 ARLLEWLNFIASELHKAFGPLFYPARwADDALAEEVKAAARERLERRLAYLDAQLAGGPYLLGDQFSVADAYLFVVLRWA 83

                         90
                 ....*....|....*
gi 110625979 172 YKQVLEPSfrqAFPN 186
Cdd:cd03188   84 RAVGLDLS---DWPH 95

Glutathione S-transferase, N-terminal domain;

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625979   17 KALIAAQYSGAQVRVLSAPPHFHFgqtnrtPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVsnEELRGSTP 89
Cdd:pfam13417  12 RVRIALNEKGLPYEFVPIPPGDHP------PELLAKNPLGKVPVLE-DDGGILCESLAIIDYL--EELYPGPP 75

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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625979  17 KALIAAQYSGAQVR---VLSAPphfhfgqTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYV 79
Cdd:cd03049   14 KVRVAAHETGLGDDvelVLVNP-------WSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYL 72

GSH-dependent disulfide bond oxidoreductase; Provisional

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  47 PEFLRKFPAGKVPAF------EGDDGFCVFESNAIAYYVSNEE---LRGSTPEAAAqVVQWVSFADSDIvppastwvFPT 117
Cdd:PRK13972  41 PEFLRISPNNKIPAIvdhspaDGGEPLSLFESGAILLYLAEKTglfLSHETRERAA-TLQWLFWQVGGL--------GPM 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110625979 118 LGIMHHNKQAT--------ENAKEEVKRILGLLDTHLKTRTFLVGERVTLADI 162
Cdd:PRK13972 112 LGQNHHFNHAApqtipyaiERYQVETQRLYHVLNKRLENSPWLGGENYSIADI 164

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 110625979 152 LVGERVTLADITVVCTLLWLYKQVLEPSFRQAFPNTNRWFLTCINQPQFRA 202
Cdd:cd03205   56 LPGGRLTLGDIAVACALGYLDFRFPELDWRAGHPALAAWFARFEARPSFQA 106

Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA synthetase cofactor 1 and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase cofactor 1 (Arc1p)-like subfamily; Arc1p, also called GU4 nucleic binding protein 1 (G4p1) or p42, is a tRNA-aminoacylation and nuclear-export cofactor. It contains a domain in the N-terminal region with similarity to the C-terminal alpha helical domain of GSTs. This domain mediates the association of the aminoacyl tRNA synthetases (aaRSs), MetRS and GluRS, in yeast to form a stable stoichiometric ternany complex. The GST_C-like domain of Arc1p is a protein-protein interaction domain containing two binding sites which enable it to bind the two aaRSs simultaneously and independently. The MetRS-Arc1p-GluRS complex selectively recruits and aminoacylates its cognate tRNAs without additional cofactors. Arc1p also plays a role in the transport of tRNA from the nucleus to the cytoplasm. It may also control the subcellular distribution of GluRS in the cytoplasm, nucleoplasm, and the mitochondrial matrix.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625979  89 PEAAAQVVQWVSFADSdivppastwvfptlGIMHHNKQATenakeevkriLGLLDTHLKTRTFLVG-ERVTLADITVVCT 167
Cdd:cd10304    1 PEQSAEVAQWLSVAKS--------------GPVSKDVQET----------LGQLNLHLRTRTFLLGtGKPSVADVAVFEA 56

                         90       100
                 ....*....|....*....|....*.
gi 110625979 168 LLWLYKQvLEPSFR---QAFPNTNRW 190
Cdd:cd10304   57 VLPVVKE-WSDEVKtgyAKYRHILRW 81

GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. 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. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from aryl or alkyl sulfate esters.

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 110625979  45 RTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVSNE 82
Cdd:cd03050   39 LTPEFKKINPFGKVPAIV-DGDFTLAESVAILRYLARK 75

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing 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 N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 110625979  45 RTPEFLRKFPAGKVPAFEGDD--GFCVFESNAIAYY 78
Cdd:cd03048   39 KKPEFLKINPNGRIPAIVDHNgtPLTVFESGAILLY 74

C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU and related 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU does not contain a redox active cysteine residue, and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YghU reveals two GSH molecules bound in its active site.

                         10        20        30
                 ....*....|....*....|....*....|.
gi 110625979 134 EVKRILGLLDTHLKTRTFLVGERVTLADITV 164
Cdd:cd10292   44 EAKRQLDVLDRQLATHKYLAGDEYTIADMAI 74

30S ribosomal protein S16; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625979 211 EKMAQFDAKKFAESQPKKDTPRK----EKGSREEKQKPQAERK---EEKKAAAPAPEEEMDECEQALAAEPKAKD 278
Cdd:PRK14521 109 EKEGKVNAKKDKLSKAKKAAKKAaleaEKKVNEARAEAVAEKKaaeAAAVAAEEAAAAEEEEAEEAPAEEAPAEE 183

cell envelope integrity inner membrane protein TolA; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625979 212 KMAQFDAKKFAESQPKKDTPRKEKGSREEKQKPQAERKeeKKAAAPAPEEEMDECEQALAAEPKAK 277
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAA--KKAAAEAKKKAEAEAAAKAAAEAKKK 202

cell envelope integrity inner membrane protein TolA; Provisional

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110625979 211 EKMAQFDAKKFAESQPKKDTPRKEKGSREEKQKPQAERKEEKKAAAPAPEE---EMDECEQALAAEPKAKD 278
Cdd:PRK09510 168 KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKaaaEAKAAAAKAAAEAKAAA 238

GST_N family, Class Omega 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. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.

                         10        20        30
                 ....*....|....*....|....*....|...
gi 110625979  47 PE-FLRKFPAGKVPAFEGDDGFCVFESNAIAYY 78
Cdd:cd03055   55 PDwFLEKNPQGKVPALEIDEGKVVYESLIICEY 87