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 403063249  27 QAQVQQWISFADNEITPVSCAWVFPLLGIMPQQKNST--AKHDAEVVLQQLNKKLLDATYLAGERITLADIVVFCSLLHL 104
Cdd:cd03181    2 AAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVdkAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLRG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 403063249 105 YEHVLEPSVRSAYGNLNRWFVTILNQPQVKAVVKDFKLCEKA 146
Cdd:cd03181   82 FETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123

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 403063249  27 QAQVQQWISFADNEITPVSCAWVFPLLGIMPQQKNST--AKHDAEVVLQQLNKKLLDATYLAGERITLADIVVFCSLLHL 104
Cdd:cd03181    2 AAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVdkAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLRG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 403063249 105 YEHVLEPSVRSAYGNLNRWFVTILNQPQVKAVVKDFKLCEKA 146
Cdd:cd03181   82 FETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123

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

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063249   3 LSESNAIAYFLAneQLRGGKC-----PFVQAQVQQWISFADNEITPVSCAWVFPLLGIMPQQKNSTAKHDAEVVLQQLNK 77
Cdd:COG0625   63 LTESLAILEYLA--ERYPEPPllpadPAARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEA 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 403063249  78 KLLDATYLAGERITLADIVVFCSLLHLYEHVLEpsvRSAYGNLNRWFVTILNQPQVKAVVKD 139
Cdd:COG0625  141 RLAGGPYLAGDRFSIADIALAPVLRRLDRLGLD---LADYPNLAAWLARLAARPAFQRALAA 199

glutamate-tRNA ligase

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063249   6 SNAIAYFLANEQLR---GGKCPFVQAQVQQWISFAdNEITPVScawvfpllgimpqqknstakhDAEVVLQQLNKKLLDA 82
Cdd:PLN02907  52 TNVLLRYIARSASLpgfYGQDAFESSQVDEWLDYA-PTFSSGS---------------------EFENACEYVDGYLASR 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063249  83 TYLAGERITLADIVVFCSLL---HLYEhvlepSVRSA--YGNLNRWFVTILNQPQVKAvvkdfklcekalafdPKKYAEF 157
Cdd:PLN02907 110 TFLVGYSLTIADIAIWSGLAgsgQRWE-----SLRKSkkYQNLVRWFNSISAEYSDIL---------------NEVTAAY 169

                 ....*....
gi 403063249 158 VAKTGTGKP 166
Cdd:PLN02907 170 VGKRGAGKP 178

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 403063249  27 QAQVQQWISFADNEITPVSCAWVFPLLGIMPQQKNST--AKHDAEVVLQQLNKKLLDATYLAGERITLADIVVFCSLLHL 104
Cdd:cd03181    2 AAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVdkAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLRG 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 403063249 105 YEHVLEPSVRSAYGNLNRWFVTILNQPQVKAVVKDFKLCEKA 146
Cdd:cd03181   82 FETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123

Elongation factor 1 gamma, conserved domain;

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 403063249  207 KDPFDAMPKGTFNFDDFKRVYSNEEE-AKSIPYFFEKFDAENYSIWFGEYKYNSELTKTFMSCNLIGGM 274
Cdd:pfam00647   1 KHPLDALPKSSFNLDEWKRQYSNEDTrPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGF 69

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 403063249  26 VQAQVQQWISFADNEITPvscawvfpllgimpqqknSTAKHDAEVVLQQLNKKLLDATYLAGERITLADIVVFCSLLHLY 105
Cdd:cd10305    3 ERAQVDQWLEYRVTQVAP------------------ASDKADAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYGLHPIM 64

                         90       100
                 ....*....|....*....|....*....
gi 403063249 106 EHvLEPSVRSAYGNLNRWFVTILNQPQVK 134
Cdd:cd10305   65 KD-LSPQEKEQYLNVSRWFDHVQHLPGIR 92

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        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063249  27 QAQVQQWISFAdneitpvscawvfpLLGIMPQQKNSTAkhdaevvLQQLNKKLLDATYLAGERITLADIVVFCSLLHLYE 106
Cdd:cd10309    2 QTEVDHWISFS--------------AGRLSCDQDFSSA-------LSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGE 60

                         90       100
                 ....*....|....*....|....
gi 403063249 107 hvlEPSVRSAYGNLNRWFVTILNQ 130
Cdd:cd10309   61 ---WLASKEKYVNVTRWFKFISSQ 81

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 403063249  30 VQQWISFADNEITPVSCAWVFPLLGIMP--QQKNSTAKHDAEVVLQQLNKKLLDATYLAGERITLADIVVFCSLLHLYEH 107
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLEKVPLPkdEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80

                         90
                 ....*....|....*..
gi 403063249 108 VLEPSVRSAYGNLNRWF 124
Cdd:cd00299   81 GPYYDLLDEYPRLKAWY 97

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        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063249  30 VQQWISFADNEI-TPVSCAWVFPLLGiMPQQKNStAKHDAEVVLQQLNKKLLDATYLAGERITLADIVVFCSLLHLYEHV 108
Cdd:cd03206    1 VQRWLSFAAGEIaHGPAAARLIHLFG-APLDPER-ARAISHRLLRLLDQHLAGRDWLAGDRPTIADVACYPYIALAPEGG 78

                         90
                 ....*....|....*.
gi 403063249 109 LEpsvRSAYGNLNRWF 124
Cdd:cd03206   79 VS---LEPYPAIRAWL 91

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 403063249  27 QAQVQQWISFAdneitpvscawvfpllgimpqqKNSTAKHDAEVVLQQLNKKLLDATYLAG-ERITLADIVVFCSLLHLY 105
Cdd:cd10304    4 SAEVAQWLSVA----------------------KSGPVSKDVQETLGQLNLHLRTRTFLLGtGKPSVADVAVFEAVLPVV 61

                         90       100       110
                 ....*....|....*....|....*....|.
gi 403063249 106 EHvLEPSVRSAYG---NLNRWFVTILNQPQV 133
Cdd:cd10304   62 KE-WSDEVKTGYAkyrHILRWVDYVQNLLLF 91

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 403063249   72 LQQLNKKLLDA--TYLAGERITLADIVVFCSLLHLyEHVLEPSVRSAYGNLNRWFVTILNQPQVKA 135
Cdd:pfam14497  35 LGYFEKVLNKNggGYLVGDKLTYADLALFQVLDGL-LYPKAPDALDKYPKLKALHERVAARPNIKA 99

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 403063249  28 AQVQQWISFADNEITPVSCAWVFP-LLGIMPQQKNSTAKHDA--EVVLQQLNKKLLDATYLAGERITLADI--VVFCSLL 102
Cdd:cd03188    4 ARLLEWLNFIASELHKAFGPLFYPaRWADDALAEEVKAAARErlERRLAYLDAQLAGGPYLLGDQFSVADAylFVVLRWA 83

                         90       100       110
                 ....*....|....*....|....*....|....
gi 403063249 103 HLYEHVLepsvrSAYGNLNRWFVTILNQPQVKAV 136
Cdd:cd03188   84 RAVGLDL-----SDWPHLAAYLARVAARPAVQAA 112

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 403063249  27 QAQVQQWISFADNEITPVSCAWVFPLLgiMPQQKNSTA--KHDAEV--VLQQLNKKLLDATYLAGERITLADIVVFcSLL 102
Cdd:cd03178    2 RAEVLQWLFFQMSGLGPMFGQAGHFLY--FAPEKIPYAieRYTDEVkrLYGVLDKRLSDRPYLAGEEYSIADIALY-PWT 78

                         90       100       110
                 ....*....|....*....|....*....|..
gi 403063249 103 HLYEHVLEPSvRSAYGNLNRWFVTILNQPQVK 134
Cdd:cd03178   79 HYADLGGFAD-LSEYPNVKRWLERIAARPAVQ 109

Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 403063249   72 LQQLNKKLLDATYLAGERITLADIVVFCSL--LHLYEHVLEpsVRSAYGNLNRWF 124
Cdd:pfam13410  13 LDALEARLADGPGLLGDRPTLADIALAPVLarLDAAYPGLD--LREGYPRLRAWL 65

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 2 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. AIMP2, also called p38 or JTV-1, contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It plays an important role in the control of cell fate via antiproliferative (by enhancing the TGF-beta signal) and proapoptotic (activation of p53 and TNF-alpha) activities. Its roles in the control of cell proliferation and death suggest that it is a potent tumor suppressor. AIMP2 heterozygous mice with lower than normal expression of AIMP2 show high susceptibility to tumorigenesis. AIMP2 is also a substrate of Parkin, an E3 ubiquitin ligase that is involved in the ubiquitylation and proteasomal degradation of its substrates. Mutations in the Parkin gene is found in 50% of patients with autosomal-recessive early-onset parkinsonism. The accumulation of AIMP2, due to impaired Parkin function, may play a role in the pathogenesis of Parkinson's disease.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 403063249  58 QQKNSTAKHDAeVVLQQLNKKLLDATYLAGERITLADIVVFCSLLHLYEHVLEPSvrsaygNLNRWFVTILNQ 130
Cdd:cd03200   31 QLLEGSSKEKA-AVLRALNSALGRSPWLVGSEPTVADIALWSAVLQTGLASGAPA------NVQRWMKSCENL 96

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 403063249  75 LNKKLLDATYLAGERITLADIVVFCSLlhLYEHVLEPSVRSAYGNLNRWFVTILNQPQV 133
Cdd:cd03182   60 LDKRLAESPYVAGDRFSIADITAFVAL--DFAKNLKLPVPEELTALRRWYERMAARPSA 116

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS 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. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS 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. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 403063249  72 LQQLNKKLLDA-TYLAGERITLADIVVFCSLLHLYehVLEPSVRSAYGNLNRWFVTI 127
Cdd:cd10307   45 LVHLDQSLLKKsTPLLGDKLSSADVVVWSALYPLG--TDKSALPENLDNLRRWFQNV 99

putative S-transferase; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 403063249  75 LNKKLLDATYLAGERITLADIVV---FCSLL--HLYEHVLEPSVRSaYGNLNRWFVTILNQPQVK 134
Cdd:PRK11752 190 LDKQLAEHEYIAGDEYTIADIAIwpwYGNLVlgNLYDAAEFLDVGS-YKHVQRWAKEIAERPAVK 253