Elongation factor 1 gamma, conserved domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322769    253 HPLEALGKSTFVLDDWKRKYSNDDTRPVALPWFWEHYNPEEYSIWKVGYKYNDELTLTFMSNNLVGGFFNRLSASTKYMF 332
Cdd:pfam00647   2 HPLDALPKSSFNLDEWKRQYSNEDTRPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGFFQRLEASRKYAF 81

                          90       100
                  ....*....|....*....|....
gi 6322769    333 GCLVVYGENNNNGIVGAVMVRGQD 356
Cdd:pfam00647  82 GSVSVYGENNNSEISGVWLFRGQD 105

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 6322769    4 GTLYIN-RSPRNYASEALISYFKLDVKIVDLEQ-----SSEFASLFPLKQAPAFLGPKGLKLTEALAIQFYLANQ 72
Cdd:cd03044   1 GTLYTYpGNPRSLKILAAAKYNGLDVEIVDFQPgkenkTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYVANL 75

Elongation factor 1 gamma, conserved domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322769    253 HPLEALGKSTFVLDDWKRKYSNDDTRPVALPWFWEHYNPEEYSIWKVGYKYNDELTLTFMSNNLVGGFFNRLSASTKYMF 332
Cdd:pfam00647   2 HPLDALPKSSFNLDEWKRQYSNEDTRPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGFFQRLEASRKYAF 81

                          90       100
                  ....*....|....*....|....
gi 6322769    333 GCLVVYGENNNNGIVGAVMVRGQD 356
Cdd:pfam00647  82 GSVSVYGENNNSEISGVWLFRGQD 105

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 6322769    4 GTLYIN-RSPRNYASEALISYFKLDVKIVDLEQ-----SSEFASLFPLKQAPAFLGPKGLKLTEALAIQFYLANQ 72
Cdd:cd03044   1 GTLYTYpGNPRSLKILAAAKYNGLDVEIVDFQPgkenkTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYVANL 75

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 6322769    104 VMSNIARPFLSFKGLIPYNKK-DVDACFVKIDNLAAVFDARLRDYTFVATENISLGDLHAAGSWAFGLATILGPEwRAKH 182
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEpEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79

                          90
                  ....*....|....
gi 6322769    183 PHLMRWFNTVAASP 196
Cdd:pfam00043  80 PNLKAWFERVAARP 93

glutamate-tRNA ligase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322769    48 APAFLGPKGLKLTEALAIQFYlanqVADEKERARLLGSDVIEKSQILRWASLANSdvmsniarpFLSFKGLipynkkdvd 127
Cdd:PLN02907  38 APTLLFSSGEKLTGTNVLLRY----IARSASLPGFYGQDAFESSQVDEWLDYAPT---------FSSGSEF--------- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322769   128 acfvkiDNLAAVFDARLRDYTFVATENISLGDLhaaGSWAfGLATIlGPEW-----RAKHPHLMRWFNTVAASPivktpf 202
Cdd:PLN02907  96 ------ENACEYVDGYLASRTFLVGYSLTIADI---AIWS-GLAGS-GQRWeslrkSKKYQNLVRWFNSISAEY------ 158

                        170       180
                 ....*....|....*....|...
gi 6322769   203 aEVKLAEKALTYTPpkKQKAEKP 225
Cdd:PLN02907 159 -SDILNEVTAAYVG--KRGAGKP 178

Elongation factor 1 gamma, conserved domain;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322769    253 HPLEALGKSTFVLDDWKRKYSNDDTRPVALPWFWEHYNPEEYSIWKVGYKYNDELTLTFMSNNLVGGFFNRLSASTKYMF 332
Cdd:pfam00647   2 HPLDALPKSSFNLDEWKRQYSNEDTRPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGFFQRLEASRKYAF 81

                          90       100
                  ....*....|....*....|....
gi 6322769    333 GCLVVYGENNNNGIVGAVMVRGQD 356
Cdd:pfam00647  82 GSVSVYGENNNSEISGVWLFRGQD 105

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 6322769    4 GTLYIN-RSPRNYASEALISYFKLDVKIVDLEQ-----SSEFASLFPLKQAPAFLGPKGLKLTEALAIQFYLANQ 72
Cdd:cd03044   1 GTLYTYpGNPRSLKILAAAKYNGLDVEIVDFQPgkenkTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYVANL 75

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 6322769    104 VMSNIARPFLSFKGLIPYNKK-DVDACFVKIDNLAAVFDARLRDYTFVATENISLGDLHAAGSWAFGLATILGPEwRAKH 182
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEpEVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79

                          90
                  ....*....|....
gi 6322769    183 PHLMRWFNTVAASP 196
Cdd:pfam00043  80 PNLKAWFERVAARP 93

Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Valyl-tRNA synthetase (ValRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of human ValRS and its homologs from other vertebrates such as frog and zebrafish. 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. They typically form large stable complexes with other proteins. 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. The GST_C-like domain of ValRS 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. ValRSs from prokaryotes and lower eukaryotes, such as fungi and plants, do not appear to contain this GST_C-like domain.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322769   91 SQILRWASLANSDVMSNIARPFLSFKGLIPYNKKDVDACFVKIDNLAAVFDARLRDYTFVATENISLGDLHAAGSWAFGL 170
Cdd:cd10294   3 ALVWQWVSFADNELTPAACAAAFPLLGLSGSDKQNQQRSLAELQRVLKVLDCYLKLRTYLVGEAITLADIAVACALLLPF 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 6322769  171 ATILGPEWRAKHPHLMRWFNTVAASPIVKTPFAEVKLAEKA 211
Cdd:cd10294  83 KYVLDPARRESLLNVTRWFLTCVNQPEFLAVLGEVSLCEKA 123

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 6322769   95 RWASLANSDVMSNIARPFLSFKGLIPYNKKDVDACFVKIDNLAAVFDARLRDYTFVATENISLGDLHAAGSWAFGLATIL 174
Cdd:cd00299   3 ALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEALGP 82

                        90
                ....*....|....*...
gi 6322769  175 GPEWRAKHPHLMRWFNTV 192
Cdd:cd00299  83 YYDLLDEYPRLKAWYDRL 100

glutathione S-transferase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6322769    44 PLKQAPAfLGPKGLKLTEALAIQFYLANQVADEKerARLLGSDVIEKSQILRWASLANsDVMSNIARPFLSFKGLIPYNK 123
Cdd:PLN02473  50 PFGQVPA-IEDGDLKLFESRAIARYYATKYADQG--TDLLGKTLEHRAIVDQWVEVEN-NYFYAVALPLVINLVFKPRLG 125

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 6322769   124 KDVDACFV-----KIDNLAAVFDARLRDYTFVATENISLGDL-HAAGSWAFGLATILGPEWRAKHpHLMRWFNTVAASP 196
Cdd:PLN02473 126 EPCDVALVeelkvKFDKVLDVYENRLATNRYLGGDEFTLADLtHMPGMRYIMNETSLSGLVTSRE-NLNRWWNEISARP 203

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
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6322769  134 DNLAAVFDARLRDYTFVATENISLGDLhAAGSWAFGLATIlGPEWRAKHPHLMRWFNTVAASPIVK 199
Cdd:cd03178  46 KRLYGVLDKRLSDRPYLAGEEYSIADI-ALYPWTHYADLG-GFADLSEYPNVKRWLERIAARPAVQ 109

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces 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 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. 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
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 6322769  139 VFDARLRDYTFVATENISLGDLHAAGSWAFG-LATILGPEwraKHPHLMRWFNTVAASP 196
Cdd:cd03182  59 VLDKRLAESPYVAGDRFSIADITAFVALDFAkNLKLPVPE---ELTALRRWYERMAARP 114

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG 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. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG 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 YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6322769  136 LAAVFDARLRDYTFVATENISLGDLhAAGSWAFGLatilgpEWR----AKHPHLMRWFNTVAASPIVK 199
Cdd:cd10291  48 LYGVLDRRLAKSKYLAGDEYSIADI-AIWPWVARH------EWQgidlADFPNLKRWFERLAARPAVQ 108