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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488398925 233 ARFLFSLLG-AKHNTVAATLIDSWVDTALFQLQGGSNKEKAAVLRGMNATLGKTSWLVGNELTVADVVTWCALQQAGGTE 311
Cdd:cd03200     1 ARFLFRLLGdESDDPVNATLIDSWVDTAIFQLLEGSSKEKAAVLRALNSALGRSPWLVGSEPTVADIALWSAVLQTGLAS 80

                          90
                  ....*....|....*.
gi 1488398925 312 AVPANVQKWLRSCENL 327
Cdd:cd03200    81 GAPANVQRWMKSCENL 96

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488398925 233 ARFLFSLLG-AKHNTVAATLIDSWVDTALFQLQGGSNKEKAAVLRGMNATLGKTSWLVGNELTVADVVTWCALQQAGGTE 311
Cdd:cd03200     1 ARFLFRLLGdESDDPVNATLIDSWVDTAIFQLLEGSSKEKAAVLRALNSALGRSPWLVGSEPTVADIALWSAVLQTGLAS 80

                          90
                  ....*....|....*.
gi 1488398925 312 AVPANVQKWLRSCENL 327
Cdd:cd03200    81 GAPANVQRWMKSCENL 96

glutamate-tRNA ligase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488398925 212 PKPQMKFSIQTmcPIEGEGNIARF------LFSLLGakHNTVAATLIDSWVDTALfQLQGGSNKEKAAVlrGMNATLGKT 285
Cdd:PLN02907   37 SAPTLLFSSGE--KLTGTNVLLRYiarsasLPGFYG--QDAFESSQVDEWLDYAP-TFSSGSEFENACE--YVDGYLASR 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1488398925 286 SWLVGNELTVADVVTWCALQQAG-------GTEAVPaNVQKWLRSC 324
Cdd:PLN02907  110 TFLVGYSLTIADIAIWSGLAGSGqrweslrKSKKYQ-NLVRWFNSI 154

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1488398925 269 KEKAAVLRGMNATLGKTSWLVGNELTVADVVTWCALQQAG------GTEAVPaNVQKWLRSCENL 327
Cdd:pfam00043  29 EKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYeldpacLREKFP-NLKAWFERVAAR 92

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        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488398925 233 ARFLFSLLG-AKHNTVAATLIDSWVDTALFQLQGGSNKEKAAVLRGMNATLGKTSWLVGNELTVADVVTWCALQQAGGTE 311
Cdd:cd03200     1 ARFLFRLLGdESDDPVNATLIDSWVDTAIFQLLEGSSKEKAAVLRALNSALGRSPWLVGSEPTVADIALWSAVLQTGLAS 80

                          90
                  ....*....|....*.
gi 1488398925 312 AVPANVQKWLRSCENL 327
Cdd:cd03200    81 GAPANVQRWMKSCENL 96

Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). 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. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs 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 1488398925 249 ATLIDSWVDTALFQLqggSNKEKAAVLRGMNATLGKTSWLVGNELTVADVVTWCALQQAGGTEAV-----PANVQKWLRS 323
Cdd:cd10289     2 AAQVDQWLDLAGSLL---KGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKLSDkekkkFPHVTRWFNH 78

                  ....
gi 1488398925 324 CENL 327
Cdd:cd10289    79 IQNL 82

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1488398925 263 LQGGSNKEKAAVLRGMNATLGKTSWLVGNELTVADVVTW----CALQQAGGTEAVPaNVQKWLRSCEN 326
Cdd:cd03189    55 LQAFINPELKRHLDFLEDHLAKHPYFAGDELTAADIMMSfpleAALARGPLLEQYP-NIAAYLERIEA 121

glutamate-tRNA ligase

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1488398925 212 PKPQMKFSIQTmcPIEGEGNIARF------LFSLLGakHNTVAATLIDSWVDTALfQLQGGSNKEKAAVlrGMNATLGKT 285
Cdd:PLN02907   37 SAPTLLFSSGE--KLTGTNVLLRYiarsasLPGFYG--QDAFESSQVDEWLDYAP-TFSSGSEFENACE--YVDGYLASR 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1488398925 286 SWLVGNELTVADVVTWCALQQAG-------GTEAVPaNVQKWLRSC 324
Cdd:PLN02907  110 TFLVGYSLTIADIAIWSGLAGSGqrweslrKSKKYQ-NLVRWFNSI 154

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

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1488398925 272 AAVLRGMNATLGKTSWLVGNELTVADVVTWCALQQAGGTE---AVPANVQKWLRSCENLAPFNAAL 334
Cdd:COG0625   132 ARLLAVLEARLAGGPYLAGDRFSIADIALAPVLRRLDRLGldlADYPNLAAWLARLAARPAFQRAL 197

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
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1488398925 269 KEKAAVLRGMNATLGKTSWLVGNELTVADVVTWCALQQAG------GTEAVPaNVQKWLRSCENL 327
Cdd:pfam00043  29 EKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYeldpacLREKFP-NLKAWFERVAAR 92

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 1488398925 232 IARFLFsllgakhntVAATLIDSWVDTA-LFQLQG-GSNKEKA-----AVLRGMNATLGKTSWLVGNELTVADVV--TWC 302
Cdd:cd03206     1 VQRWLS---------FAAGEIAHGPAAArLIHLFGaPLDPERAraishRLLRLLDQHLAGRDWLAGDRPTIADVAcyPYI 71

                          90       100
                  ....*....|....*....|....*....
gi 1488398925 303 ALQQAGGTEAVP-ANVQKWLRSCENLAPF 330
Cdd:cd03206    72 ALAPEGGVSLEPyPAIRAWLARVEALPGF 100