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Conserved domains on  [gi|51261278|gb|AAH79398|]
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Eukaryotic translation elongation factor 1 gamma [Rattus norvegicus]

Protein Classification

GST_C_EF1Bgamma_like and EF1G domain-containing protein( domain architecture ID 12930820)

protein containing domains GST_N_EF1Bgamma, GST_C_EF1Bgamma_like, and EF1G

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF1G pfam00647
Elongation factor 1 gamma, conserved domain;
277-381 1.21e-67

Elongation factor 1 gamma, conserved domain;


:

Pssm-ID: 459888  Cd Length: 105  Bit Score: 210.46  E-value: 1.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   277 KDPFAHLPKSTFVLDEFKRKYSNEDTLSVALPYFWEHFDKDGWSLWYAEYRFPEELTQTFMSCNLITGMFQRLDKLRKNA 356
Cdd:pfam00647   1 KHPLDALPKSSFNLDEWKRQYSNEDTRPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGFFQRLEASRKYA 80

                          90       100
                  ....*....|....*....|....*
gi 51261278   357 FASVILFGTNNSSSISGVWVFRGQD 381
Cdd:pfam00647  81 FGSVSVYGENNNSEISGVWLFRGQD 105
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 91-213 1.31e-67

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.


:

Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 210.88  E-value: 1.31e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  91 AAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLW 170
Cdd:cd03181   1 EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 51261278 171 LYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAILGEVKLCEKM 213
Cdd:cd03181  81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 4-82 9.15e-38

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.


:

Pssm-ID: 239342 [Multi-domain]  Cd Length: 75  Bit Score: 131.61  E-value: 9.15e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51261278   4 GTLYTYPENWRAFKALIAAQYSGAQIRVLSAPPHFhfgqTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYVSNE 82
Cdd:cd03044   1 GTLYTYPGNPRSLKILAAAKYNGLDVEIVDFQPGK----ENKTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYVANL 75
rpsP super family cl36390
30S ribosomal protein S16; Provisional
 211-278 7.36e-03

30S ribosomal protein S16; Provisional


The actual alignment was detected with superfamily member PRK14521:

Pssm-ID: 237744 [Multi-domain]  Cd Length: 186  Bit Score: 37.45  E-value: 7.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51261278  211 EKMAQFDAKKFAESQPKKDTPRK----EKGSREEKQKPQTERK---EEKKAAAPAPEEEMDECEQALAAEPKAKD 278
Cdd:PRK14521 109 EKEGKVNAKKDKLSKAKKAAKKAaleaEKKVNEARAEAVAEKKaaeAAAVAAEEAAAAEEEEAEEAPAEEAPAEE 183
 
Name Accession Description Interval E-value
EF1G pfam00647
Elongation factor 1 gamma, conserved domain;
277-381 1.21e-67

Elongation factor 1 gamma, conserved domain;


Pssm-ID: 459888  Cd Length: 105  Bit Score: 210.46  E-value: 1.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   277 KDPFAHLPKSTFVLDEFKRKYSNEDTLSVALPYFWEHFDKDGWSLWYAEYRFPEELTQTFMSCNLITGMFQRLDKLRKNA 356
Cdd:pfam00647   1 KHPLDALPKSSFNLDEWKRQYSNEDTRPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGFFQRLEASRKYA 80

                          90       100
                  ....*....|....*....|....*
gi 51261278   357 FASVILFGTNNSSSISGVWVFRGQD 381
Cdd:pfam00647  81 FGSVSVYGENNNSEISGVWLFRGQD 105
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 91-213 1.31e-67

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.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 210.88  E-value: 1.31e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  91 AAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLW 170
Cdd:cd03181   1 EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 51261278 171 LYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAILGEVKLCEKM 213
Cdd:cd03181  81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 4-82 9.15e-38

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.


Pssm-ID: 239342 [Multi-domain]  Cd Length: 75  Bit Score: 131.61  E-value: 9.15e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51261278   4 GTLYTYPENWRAFKALIAAQYSGAQIRVLSAPPHFhfgqTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYVSNE 82
Cdd:cd03044   1 GTLYTYPGNPRSLKILAAAKYNGLDVEIVDFQPGK----ENKTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYVANL 75
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
5-206 6.67e-34

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 125.78  E-value: 6.67e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   5 TLYTYPENWRAFKALIAAQYSGAQIRVLSAPPhfhFGQTNRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVsnEE- 83
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDL---AKGEQKSPEFLALNPLGKVPVLV-DDGLVLTESLAILEYL--AEr 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  84 -----LRGSTPEAAAQVVQWVSFADSDIVPPASTWVFPTLGimHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVT 158
Cdd:COG0625  77 ypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAP--EKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 51261278 159 LADITVVCTLLWLYKQVLEPSfrqAFPNTNRWFLTCINQPQFRAILGE 206
Cdd:COG0625 155 IADIALAPVLRRLDRLGLDLA---DYPNLAAWLARLAARPAFQRALAA 199
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 2-81 1.25e-19

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.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 82.74  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278     2 AAGTLYTYPENWRAFKALIAAQYSGAQIRVlsAPPHFHFGQTNRtPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVSN 81
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEI--VPLDFGAGPEKS-PELLKLNPLGKVPALE-DGGKKLTESRAILEYIAR 76
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 106-198 1.89e-18

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.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 80.02  E-value: 1.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   106 IVPPASTWVFPTLGIMHHNKQAT-ENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSfRQAF 184
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEvDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79

                          90
                  ....*....|....
gi 51261278   185 PNTNRWFLTCINQP 198
Cdd:pfam00043  80 PNLKAWFERVAARP 93
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 54-228 1.50e-11

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 63.20  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   54 PAGKVPAFEGDDGFCVFESNAIAYYVsneELRGSTP-------EAAAQVVQWVSFADSdIVPPASTWVFPTlgiMHHNKQ 126
Cdd:PRK10357  45 PLGKVPALVTEEGECWFDSPIIAEYI---ELLNVAPamlprdpLAALRVRQLEALADG-IMDAALVSVREQ---ARPAAQ 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  127 ATEN----AKEEVKRILGLLDTHLKTRTfLVGERVTLADITVVCTLLWLykqvlepSFRQAFPNtnrWfltCINQPQFra 202
Cdd:PRK10357 118 QSEDellrQREKINRSLDALEGYLVDGT-LKTDTVNLATIAIACAVGYL-------NFRRVAPG---W---CVDRPHL-- 181

                        170       180
                 ....*....|....*....|....*.
gi 51261278  203 ilgeVKLCEKMAQFDAkkFAESQPKK 228
Cdd:PRK10357 182 ----VKLVENLFQRES--FARTEPPK 201
rpsP PRK14521
30S ribosomal protein S16; Provisional
 211-278 7.36e-03

30S ribosomal protein S16; Provisional


Pssm-ID: 237744 [Multi-domain]  Cd Length: 186  Bit Score: 37.45  E-value: 7.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51261278  211 EKMAQFDAKKFAESQPKKDTPRK----EKGSREEKQKPQTERK---EEKKAAAPAPEEEMDECEQALAAEPKAKD 278
Cdd:PRK14521 109 EKEGKVNAKKDKLSKAKKAAKKAaleaEKKVNEARAEAVAEKKaaeAAAVAAEEAAAAEEEEAEEAPAEEAPAEE 183
 
Name Accession Description Interval E-value
EF1G pfam00647
Elongation factor 1 gamma, conserved domain;
277-381 1.21e-67

Elongation factor 1 gamma, conserved domain;


Pssm-ID: 459888  Cd Length: 105  Bit Score: 210.46  E-value: 1.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   277 KDPFAHLPKSTFVLDEFKRKYSNEDTLSVALPYFWEHFDKDGWSLWYAEYRFPEELTQTFMSCNLITGMFQRLDKLRKNA 356
Cdd:pfam00647   1 KHPLDALPKSSFNLDEWKRQYSNEDTRPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGFFQRLEASRKYA 80

                          90       100
                  ....*....|....*....|....*
gi 51261278   357 FASVILFGTNNSSSISGVWVFRGQD 381
Cdd:pfam00647  81 FGSVSVYGENNNSEISGVWLFRGQD 105
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 91-213 1.31e-67

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.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 210.88  E-value: 1.31e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  91 AAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLW 170
Cdd:cd03181   1 EAAQVLQWISFANSELLPAAATWVLPLLGIAPYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 51261278 171 LYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAILGEVKLCEKM 213
Cdd:cd03181  81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123
GST_C_ValRS_N cd10294
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ...
 91-213 1.95e-50

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.


Pssm-ID: 198327 [Multi-domain]  Cd Length: 123  Bit Score: 166.55  E-value: 1.95e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  91 AAAQVVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLW 170
Cdd:cd10294   1 ACALVWQWVSFADNELTPAACAAAFPLLGLSGSDKQNQQRSLAELQRVLKVLDCYLKLRTYLVGEAITLADIAVACALLL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 51261278 171 LYKQVLEPSFRQAFPNTNRWFLTCINQPQFRAILGEVKLCEKM 213
Cdd:cd10294  81 PFKYVLDPARRESLLNVTRWFLTCVNQPEFLAVLGEVSLCEKA 123
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 4-82 9.15e-38

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.


Pssm-ID: 239342 [Multi-domain]  Cd Length: 75  Bit Score: 131.61  E-value: 9.15e-38
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51261278   4 GTLYTYPENWRAFKALIAAQYSGAQIRVLSAPPHFhfgqTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYVSNE 82
Cdd:cd03044   1 GTLYTYPGNPRSLKILAAAKYNGLDVEIVDFQPGK----ENKTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYVANL 75
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
5-206 6.67e-34

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 125.78  E-value: 6.67e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   5 TLYTYPENWRAFKALIAAQYSGAQIRVLSAPPhfhFGQTNRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVsnEE- 83
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDL---AKGEQKSPEFLALNPLGKVPVLV-DDGLVLTESLAILEYL--AEr 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  84 -----LRGSTPEAAAQVVQWVSFADSDIVPPASTWVFPTLGimHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVT 158
Cdd:COG0625  77 ypeppLLPADPAARARVRQWLAWADGDLHPALRNLLERLAP--EKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFS 154

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 51261278 159 LADITVVCTLLWLYKQVLEPSfrqAFPNTNRWFLTCINQPQFRAILGE 206
Cdd:COG0625 155 IADIALAPVLRRLDRLGLDLA---DYPNLAAWLARLAARPAFQRALAA 199
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 2-81 1.25e-19

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.


Pssm-ID: 460698 [Multi-domain]  Cd Length: 76  Bit Score: 82.74  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278     2 AAGTLYTYPENWRAFKALIAAQYSGAQIRVlsAPPHFHFGQTNRtPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVSN 81
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEI--VPLDFGAGPEKS-PELLKLNPLGKVPALE-DGGKKLTESRAILEYIAR 76
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 106-198 1.89e-18

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.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 80.02  E-value: 1.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   106 IVPPASTWVFPTLGIMHHNKQAT-ENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSfRQAF 184
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEvDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79

                          90
                  ....*....|....
gi 51261278   185 PNTNRWFLTCINQP 198
Cdd:pfam00043  80 PNLKAWFERVAARP 93
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 95-191 2.09e-15

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.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 71.76  E-value: 2.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  95 VVQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQ 174
Cdd:cd00299   1 VRALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80

                        90
                ....*....|....*..
gi 51261278 175 VLEPSFRQAFPNTNRWF 191
Cdd:cd00299  81 GPYYDLLDEYPRLKAWY 97
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
 92-197 1.93e-13

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.


Pssm-ID: 198322 [Multi-domain]  Cd Length: 82  Bit Score: 65.41  E-value: 1.93e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  92 AAQVVQWVSFADSdivppastwvfptlgimhhnkqatENAKEEVKRILGLLDTHLKTRTFLVGERVTLADItVVCTLLWL 171
Cdd:cd10289   2 AAQVDQWLDLAGS------------------------LLKGKELEALLKSLNSYLASRTFLVGYSLTLADV-AVFSALYP 56

                        90       100
                ....*....|....*....|....*.
gi 51261278 172 YKQVLEPSFRQAFPNTNRWFLTCINQ 197
Cdd:cd10289  57 SGQKLSDKEKKKFPHVTRWFNHIQNL 82
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 5-79 7.47e-13

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.


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 63.36  E-value: 7.47e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51261278   5 TLYTYPENWRAFKALIAAQYSGAQIRVLSAPPHfhfgqTNRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYV 79
Cdd:cd00570   2 KLYYFPGSPRSLRVRLALEEKGLPYELVPVDLG-----EGEQEEFLALNPLGKVPVLE-DGGLVLTESLAILEYL 70
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 54-228 1.50e-11

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 63.20  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   54 PAGKVPAFEGDDGFCVFESNAIAYYVsneELRGSTP-------EAAAQVVQWVSFADSdIVPPASTWVFPTlgiMHHNKQ 126
Cdd:PRK10357  45 PLGKVPALVTEEGECWFDSPIIAEYI---ELLNVAPamlprdpLAALRVRQLEALADG-IMDAALVSVREQ---ARPAAQ 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  127 ATEN----AKEEVKRILGLLDTHLKTRTfLVGERVTLADITVVCTLLWLykqvlepSFRQAFPNtnrWfltCINQPQFra 202
Cdd:PRK10357 118 QSEDellrQREKINRSLDALEGYLVDGT-LKTDTVNLATIAIACAVGYL-------NFRRVAPG---W---CVDRPHL-- 181

                        170       180
                 ....*....|....*....|....*.
gi 51261278  203 ilgeVKLCEKMAQFDAkkFAESQPKK 228
Cdd:PRK10357 182 ----VKLVENLFQRES--FARTEPPK 201
GST_C_AIMP3 cd10305
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
 89-191 2.22e-11

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.


Pssm-ID: 198338 [Multi-domain]  Cd Length: 101  Bit Score: 60.00  E-value: 2.22e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  89 PEAAAQVVQWVSFAdSDIVPPASTwvfptlgimhhnkqatenaKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTL 168
Cdd:cd10305   1 AEERAQVDQWLEYR-VTQVAPASD-------------------KADAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYGL 60

                        90       100
                ....*....|....*....|...
gi 51261278 169 LWLYKQvLEPSFRQAFPNTNRWF 191
Cdd:cd10305  61 HPIMKD-LSPQEKEQYLNVSRWF 82
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 96-198 9.45e-11

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other 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. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 58.46  E-value: 9.45e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  96 VQWVSFADSDIVPPASTWVFPTLGIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQV 175
Cdd:cd03207   2 LRWLFFAAGTVEPPLLNKALGRFFEPPWGEPAIAAAYGDLDERLAALEAALAGRPYLVGERFSAADLLLASVLRWARAFG 81

                        90       100
                ....*....|....*....|...
gi 51261278 176 LEPsfrqAFPNTNRWFLTCINQP 198
Cdd:cd03207  82 LLP----EYPALRAYVARCTARP 100
PLN02473 PLN02473
glutathione S-transferase
 45-204 3.49e-10

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 59.62  E-value: 3.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   45 RTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVSNE------ELRGSTPEAAAQVVQWVS----FADSDIVPPASTWV 114
Cdd:PLN02473  41 KKPEHLLRQPFGQVPAIE-DGDLKLFESRAIARYYATKyadqgtDLLGKTLEHRAIVDQWVEvennYFYAVALPLVINLV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  115 F-PTLGiMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSFRQAFPNTNRWFLT 193
Cdd:PLN02473 120 FkPRLG-EPCDVALVEELKVKFDKVLDVYENRLATNRYLGGDEFTLADLTHMPGMRYIMNETSLSGLVTSRENLNRWWNE 198

                        170
                 ....*....|.
gi 51261278  194 CINQPQFRAIL 204
Cdd:PLN02473 199 ISARPAWKKLM 209
PLN02907 PLN02907
glutamate-tRNA ligase
 54-199 2.39e-09

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 59.35  E-value: 2.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   54 PAGKVPAFEGDDGFCVFESNAIAYYV----SNEELRGSTPEAAAQVVQWVSFAdSDIVPPAStwvFptlgimhhnkqatE 129
Cdd:PLN02907  34 KSGSAPTLLFSSGEKLTGTNVLLRYIarsaSLPGFYGQDAFESSQVDEWLDYA-PTFSSGSE---F-------------E 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51261278  130 NAKEEVkrilgllDTHLKTRTFLVGERVTLADITVVCTL-----LWlykqvlePSFRQA--FPNTNRWFLTCINQPQ 199
Cdd:PLN02907  97 NACEYV-------DGYLASRTFLVGYSLTIADIAIWSGLagsgqRW-------ESLRKSkkYQNLVRWFNSISAEYS 159
GST_C_GluProRS_N cd10309
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ...
 142-191 1.19e-08

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.


Pssm-ID: 198342 [Multi-domain]  Cd Length: 81  Bit Score: 51.94  E-value: 1.19e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 51261278 142 LDTHLKTRTFLVGERVTLADITVVCTllwLYKQVLEPSFRQAFPNTNRWF 191
Cdd:cd10309  29 LDKALSLRTYLVGNSLTLADFAVWAA---LRGNGEWLASKEKYVNVTRWF 75
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 127-191 1.50e-08

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 51.17  E-value: 1.50e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51261278   127 ATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSFRQAFPNTNRWF 191
Cdd:pfam13410   1 ALERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPVLARLDAAYPGLDLREGYPRLRAWL 65
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
 93-191 1.93e-08

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.


Pssm-ID: 198288 [Multi-domain]  Cd Length: 110  Bit Score: 51.86  E-value: 1.93e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  93 AQVVQWVSFADSDivppastwVFPTLGIMHH--------NKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITv 164
Cdd:cd03178   3 AEVLQWLFFQMSG--------LGPMFGQAGHflyfapekIPYAIERYTDEVKRLYGVLDKRLSDRPYLAGEEYSIADIA- 73

                        90       100
                ....*....|....*....|....*....
gi 51261278 165 vcTLLWL--YKQVLEPSFrQAFPNTNRWF 191
Cdd:cd03178  74 --LYPWThyADLGGFADL-SEYPNVKRWL 99
PLN02395 PLN02395
glutathione S-transferase
 44-163 3.33e-08

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 53.71  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   44 NRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVSNE------ELRGSTPEAAAQVVQWVSFADSDIVPPASTWVF-- 115
Cdd:PLN02395  39 HKQPEYLALQPFGVVPVIV-DGDYKIFESRAIMRYYAEKyrsqgpDLLGKTIEERGQVEQWLDVEATSYHPPLLNLTLhi 117

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 51261278  116 ---PTLGIMHHNKqATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADIT 163
Cdd:PLN02395 118 lfaSKMGFPADEK-VIKESEEKLAKVLDVYEARLSKSKYLAGDFVSLADLA 167
GST_C_7 cd03206
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ...
 95-164 5.24e-08

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.


Pssm-ID: 198315 [Multi-domain]  Cd Length: 100  Bit Score: 50.69  E-value: 5.24e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51261278  95 VVQWVSFADSDIVP-PASTWVFPTLGiMHHNKqatENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITV 164
Cdd:cd03206   1 VQRWLSFAAGEIAHgPAAARLIHLFG-APLDP---ERARAISHRLLRLLDQHLAGRDWLAGDRPTIADVAC 67
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 5-78 8.79e-08

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


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 49.04  E-value: 8.79e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51261278   5 TLYTYPENwRAFKALIAAQYSGA--QIRVLSAPPHFHfgqtnRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYY 78
Cdd:cd03046   2 TLYHLPRS-RSFRILWLLEELGLpyELVLYDRGPGEQ-----APPEYLAINPLGKVPVLV-DGDLVLTESAAIILY 70
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 44-80 1.95e-07

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.


Pssm-ID: 239351 [Multi-domain]  Cd Length: 76  Bit Score: 48.03  E-value: 1.95e-07
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 51261278  44 NRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVS 80
Cdd:cd03053  39 HKSPEHLARNPFGQIPALE-DGDLKLFESRAITRYLA 74
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 120-194 5.12e-07

C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Delta and Epsilon 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. 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. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.


Pssm-ID: 198287 [Multi-domain]  Cd Length: 117  Bit Score: 48.30  E-value: 5.12e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51261278 120 IMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWLYKQVLEPSfrqAFPNTNRWFLTC 194
Cdd:cd03177  28 ILFGGAEPPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVSTLEVVGFDLS---KYPNVAAWYERL 99
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 93-191 5.90e-07

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.


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 47.66  E-value: 5.90e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  93 AQVVQWVSFADSDIVPPastWVFPTLGIM-----HHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCT 167
Cdd:cd03180   4 ALADRWMDWQTSTLNPA---FRYAFWGLVrtppeQRDPAAIAASLAACNKLMAILDAQLARQAYLAGDRFTLADIALGCS 80

                        90       100
                ....*....|....*....|....
gi 51261278 168 llwLYKQVLEPSFRQAFPNTNRWF 191
Cdd:cd03180  81 ---VYRWLELPIERPALPHLERWY 101
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 15-79 1.51e-06

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 45.31  E-value: 1.51e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51261278    15 AFKALIAAQYSG--AQIRVLSAPPHfhfgqtNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYV 79
Cdd:pfam13409   5 SHRVRLALEEKGlpYEIELVDLDPK------DKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYL 65
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 5-80 2.87e-06

GST_N family, unknown subfamily 4; 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.


Pssm-ID: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 44.87  E-value: 2.87e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   5 TLYTYPENWRAFKALIAAQysgaqirVLSAPPHFHF-----GQTnRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYV 79
Cdd:cd03056   2 KLYGFPLSGNCYKVRLLLA-------LLGIPYEWVEvdilkGET-RTPEFLALNPNGEVPVLE-LDGRVLAESNAILVYL 72


                .
gi 51261278  80 S 80
Cdd:cd03056  73 A 73
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 93-186 6.25e-06

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.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 44.93  E-value: 6.25e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  93 AQVVQWVSFADSDIVPPASTWVFPTL-GIMHHNKQATENAKEEVKRILGLLDTHLKTRTFLVGERVTLADITVVCTLLWL 171
Cdd:cd03188   4 ARLLEWLNFIASELHKAFGPLFYPARwADDALAEEVKAAARERLERRLAYLDAQLAGGPYLLGDQFSVADAYLFVVLRWA 83

                        90
                ....*....|....*
gi 51261278 172 YKQVLEPSfrqAFPN 186
Cdd:cd03188  84 RAVGLDLS---DWPH 95
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
 116-193 6.30e-06

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.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 44.95  E-value: 6.30e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278 116 PTLGIMHHNKQAtenAKE-----------EVKRILGLLDTHLKTRTFLVGERVTLADITV---VCTLLWlYKQVLEPsfr 181
Cdd:cd10291  18 PMQGQAHHFKRY---APEkipyaikrytnETKRLYGVLDRRLAKSKYLAGDEYSIADIAIwpwVARHEW-QGIDLAD--- 90

                        90
                ....*....|..
gi 51261278 182 qaFPNTNRWFLT 193
Cdd:cd10291  91 --FPNLKRWFER 100
GST_C_GluRS_N cd10306
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ...
 93-191 1.37e-05

Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower 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 GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198339 [Multi-domain]  Cd Length: 87  Bit Score: 43.11  E-value: 1.37e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  93 AQVVQWVSFADSDIVPPAstwvFPTLgimhhnkqatenakeevKRILGLLDTHLKTRTFLVGERVTLADITVvctllWLY 172
Cdd:cd10306   5 EQVAEWIDFATTLLVLKD----FKAL-----------------SQALEELDSHLTLRTFIVGYSLSLADIAV-----WGA 58

                        90       100
                ....*....|....*....|...
gi 51261278 173 ----KQVLEPSFRQAFPNTNRWF 191
Cdd:cd10306  59 lrgnGVAGSLIKNKVYVNLSRWF 81
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 88-198 2.25e-05

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.


Pssm-ID: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 43.46  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  88 TPEAAAQVVQWVSFADSDIVPPASTWVFPTLGIM--HHNKQATENAKEEVKRI---LGLLDTHLKTRTFLVGERVTLADI 162
Cdd:cd03182   1 TPLEKALIEMWQRRAELQGLAPVFQAFRHATPGLkpDREVQVPEWGERNKKRVidfLPVLDKRLAESPYVAGDRFSIADI 80

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 51261278 163 TVVcTLLWLYKQVLEPSFRQAfPNTNRWFLTCINQP 198
Cdd:cd03182  81 TAF-VALDFAKNLKLPVPEEL-TALRRWYERMAARP 114
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 17-79 2.93e-05

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.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 41.86  E-value: 2.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 51261278  17 KALIAAQYSGAQIR---VLSAPphfhfgqTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYV 79
Cdd:cd03049  14 KVRVAAHETGLGDDvelVLVNP-------WSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYL 72
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
17-89 3.15e-05

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 41.83  E-value: 3.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 51261278    17 KALIAAQYSGAQIRVLSAPPHFHFgqtnrtPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVsnEELRGSTP 89
Cdd:pfam13417  12 RVRIALNEKGLPYEFVPIPPGDHP------PELLAKNPLGKVPVLE-DDGGILCESLAIIDYL--EELYPGPP 75
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 90-198 8.92e-05

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.


Pssm-ID: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 41.91  E-value: 8.92e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  90 EAAAQVVQWVSFADSDIVPP----------ASTWVFPTLGIMHHNKQATENA--KEEVKRILGLLDTHLKTRTFLVGERV 157
Cdd:cd03189   6 AEYADYLYWLHFAEGSLMPPlllklvfgkiGEAPPPFFRPISRKIADKPLQAfiNPELKRHLDFLEDHLAKHPYFAGDEL 85

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 51261278 158 TLADITVVCTLLWLYKQVlepSFRQAFPNTNRWFLTCINQP 198
Cdd:cd03189  86 TAADIMMSFPLEAALARG---PLLEQYPNIAAYLERIEARP 123
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
 47-162 1.02e-04

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 43.53  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278   47 PEFLRKFPAGKVPAF------EGDDGFCVFESNAIAYYVSNEE---LRGSTPEAAAqVVQWVSFADSDIvppastwvFPT 117
Cdd:PRK13972  41 PEFLRISPNNKIPAIvdhspaDGGEPLSLFESGAILLYLAEKTglfLSHETRERAA-TLQWLFWQVGGL--------GPM 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 51261278  118 LGIMHHNKQAT--------ENAKEEVKRILGLLDTHLKTRTFLVGERVTLADI 162
Cdd:PRK13972 112 LGQNHHFNHAApqtipyaiERYQVETQRLYHVLNKRLENSPWLGGENYSIADI 164
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
 44-80 1.13e-04

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions.


Pssm-ID: 239345 [Multi-domain]  Cd Length: 73  Bit Score: 40.38  E-value: 1.13e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 51261278  44 NRTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVS 80
Cdd:cd03047  38 LDTPEFLAMNPNGRVPVLE-DGDFVLWESNAILRYLA 73
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 112-168 1.65e-04

C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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 the 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 the aryl or alkyl sulfate esters.


Pssm-ID: 198292 [Multi-domain]  Cd Length: 126  Bit Score: 41.04  E-value: 1.65e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51261278 112 TWVFPTLGIMHHNKQATENAKEEVKRILGLLDTH-LKTRTFLVGERVTLADITVVCTL 168
Cdd:cd03183  27 KVLLPLFGGTPVSPEKVKKAEENLEESLDLLENKfLKDKPFLAGDEISIADLSAICEI 84
GST_C_6 cd03205
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ...
 152-202 1.69e-04

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.


Pssm-ID: 198314 [Multi-domain]  Cd Length: 109  Bit Score: 40.65  E-value: 1.69e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 51261278 152 LVGERVTLADITVVCTLLWLYKQVLEPSFRQAFPNTNRWFLTCINQPQFRA 202
Cdd:cd03205  56 LPGGRLTLGDIAVACALGYLDFRFPELDWRAGHPALAAWFARFEARPSFQA 106
GST_C_Arc1p_N_like cd10304
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ...
 89-190 1.69e-04

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.


Pssm-ID: 198337 [Multi-domain]  Cd Length: 100  Bit Score: 40.43  E-value: 1.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  89 PEAAAQVVQWVSFADSdivppastwvfptlGIMHHNKQATenakeevkriLGLLDTHLKTRTFLVG-ERVTLADITVVCT 167
Cdd:cd10304   1 PEQSAEVAQWLSVAKS--------------GPVSKDVQET----------LGQLNLHLRTRTFLLGtGKPSVADVAVFEA 56

                        90       100
                ....*....|....*....|....*.
gi 51261278 168 LLWLYKQvLEPSFR---QAFPNTNRW 190
Cdd:cd10304  57 VLPVVKE-WSDEVKtgyAKYRHILRW 81
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 44-79 1.91e-04

GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT2. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT2, a homodimer, exhibits GST activity with standard substrates. Strains with deleted GTT2 genes are viable but exhibit increased sensitivity to heat shock.


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 39.59  E-value: 1.91e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 51261278  44 NRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYV 79
Cdd:cd03051  38 QRSPEFLAKNPAGTVPVLELDDGTVITESVAICRYL 73
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
 45-82 2.55e-04

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.


Pssm-ID: 239348 [Multi-domain]  Cd Length: 76  Bit Score: 39.53  E-value: 2.55e-04
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 51261278  45 RTPEFLRKFPAGKVPAFEgDDGFCVFESNAIAYYVSNE 82
Cdd:cd03050  39 LTPEFKKINPFGKVPAIV-DGDFTLAESVAILRYLARK 75
GST_C_Ure2p cd10293
C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione ...
 92-190 3.02e-04

C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Ure2p subfamily; composed of the Saccharomyces cerevisiae Ure2p and related fungal 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. 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.


Pssm-ID: 198326 [Multi-domain]  Cd Length: 117  Bit Score: 40.10  E-value: 3.02e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51261278  92 AAQVVQWVSFADSDIVPPASTWVFPTlgIMHHNK--QATENAKEEVKRILGLLDTHLK--TRTFLVGERVTLADITVVC- 166
Cdd:cd10293   2 YYQAKQWLFFQASGQGPYWGQAGWFN--VFHAEKvpSAIERYTNEIRRVLGVLETALAerYRVWLVGDKFTIADLAFVPw 79

                        90       100
                ....*....|....*....|....*
gi 51261278 167 -TLLWLYKQVLEPSFRQAFPNTNRW 190
Cdd:cd10293  80 nNVVDMIFIDPELDIKKEFPHVYKW 104
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 45-78 3.89e-04

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.


Pssm-ID: 239346 [Multi-domain]  Cd Length: 81  Bit Score: 39.06  E-value: 3.89e-04
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 51261278  45 RTPEFLRKFPAGKVPAFEGDD--GFCVFESNAIAYY 78
Cdd:cd03048  39 KKPEFLKINPNGRIPAIVDHNgtPLTVFESGAILLY 74
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 125-168 7.23e-04

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 38.76  E-value: 7.23e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 51261278 125 KQATENAKEEVKRILGLLDTHLK--TRTFLVGERVTLADITVVCTL 168
Cdd:cd03192  34 EKKKEFLEEALPKFLGKFEKILKksGGGYFVGDKLTWADLALFDVL 79
GST_C_YghU_like cd10292
C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and ...
 134-164 1.35e-03

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.


Pssm-ID: 198325 [Multi-domain]  Cd Length: 118  Bit Score: 38.60  E-value: 1.35e-03
                        10        20        30
                ....*....|....*....|....*....|.
gi 51261278 134 EVKRILGLLDTHLKTRTFLVGERVTLADITV 164
Cdd:cd10292  44 EAKRQLDVLDRQLATHKYLAGDEYTIADMAI 74
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-81 1.87e-03

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.


Pssm-ID: 239355 [Multi-domain]  Cd Length: 77  Bit Score: 36.75  E-value: 1.87e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51261278   5 TLYTYPeNWRAFKALIAAQYSGAQIRVLSAPPHFHfgqTNRTPEFLRKFPAGKVPAFEGDDGFCVFESNAIAYYVSN 81
Cdd:cd03057   2 KLYYSP-GACSLAPHIALEELGLPFELVRVDLRTK---TQKGADYLAINPKGQVPALVLDDGEVLTESAAILQYLAD 74
PRK11752 PRK11752
putative S-transferase; Provisional
 134-164 4.70e-03

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 38.76  E-value: 4.70e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 51261278  134 EVKRILGLLDTHLKTRTFLVGERVTLADITV 164
Cdd:PRK11752 182 EAKRQLDVLDKQLAEHEYIAGDEYTIADIAI 212
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 47-78 6.32e-03

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.


Pssm-ID: 239353 [Multi-domain]  Cd Length: 89  Bit Score: 35.79  E-value: 6.32e-03
                        10        20        30
                ....*....|....*....|....*....|...
gi 51261278  47 PE-FLRKFPAGKVPAFEGDDGFCVFESNAIAYY 78
Cdd:cd03055  55 PDwFLEKNPQGKVPALEIDEGKVVYESLIICEY 87
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 125-186 6.69e-03

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 35.99  E-value: 6.69e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51261278   125 KQATENAKEEVKRILGLLDTHLKTR--TFLVGERVTLADItVVCTLLWLYKQVLEPSFRQAFPN 186
Cdd:pfam14497  21 KRRKEFREERLPKFLGYFEKVLNKNggGYLVGDKLTYADL-ALFQVLDGLLYPKAPDALDKYPK 83
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
 138-191 7.06e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component 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. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.


Pssm-ID: 198341  Cd Length: 82  Bit Score: 35.48  E-value: 7.06e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 51261278 138 ILGLLDTHLKTRTFLVGERVTLADITVvctllwlYKQVLEPSFRQAFPNTNRWF 191
Cdd:cd10308  30 GLEALNEYLADRSYISGYSPSQADVEV-------FDKLKKAPDATKFPHLARWY 76
rpsP PRK14521
30S ribosomal protein S16; Provisional
 211-278 7.36e-03

30S ribosomal protein S16; Provisional


Pssm-ID: 237744 [Multi-domain]  Cd Length: 186  Bit Score: 37.45  E-value: 7.36e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51261278  211 EKMAQFDAKKFAESQPKKDTPRK----EKGSREEKQKPQTERK---EEKKAAAPAPEEEMDECEQALAAEPKAKD 278
Cdd:PRK14521 109 EKEGKVNAKKDKLSKAKKAAKKAaleaEKKVNEARAEAVAEKKaaeAAAVAAEEAAAAEEEEAEEAPAEEAPAEE 183
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 212-278 9.37e-03

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 38.25  E-value: 9.37e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51261278  212 KMAQFDAKKFAESQPKKDTPRKEKGSREEKQKPQTERKEEKKAAAPAPEEEMDECEQALAAEPKAKD 278
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAA 227
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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