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Conserved domains on  [gi|15237931|ref|NP_197224|]
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glutathione S-transferase phi 12 [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02473 PLN02473
glutathione S-transferase
1-214 9.22e-169

glutathione S-transferase


:

Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 462.54  E-value: 9.22e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931    1 MVVKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFAD 80
Cdd:PLN02473   1 MVVKVYGQIKAANPQRVLLCFLEKGIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGDLKLFESRAIARYYATKYAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   81 QGTNLLGKSLEHRAIVDQWADVETYYFNVLAQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGE 160
Cdd:PLN02473  81 QGTDLLGKTLEHRAIVDQWVEVENNYFYAVALPLVINLVFKPRLGEPCDVALVEELKVKFDKVLDVYENRLATNRYLGGD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15237931  161 EFTMADLTHMPAMGYLMSITDINQMVKARGSFNRWWEEISDRPSWKKLMVLAGH 214
Cdd:PLN02473 161 EFTLADLTHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLMELAAY 214
 
Name Accession Description Interval E-value
PLN02473 PLN02473
glutathione S-transferase
1-214 9.22e-169

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 462.54  E-value: 9.22e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931    1 MVVKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFAD 80
Cdd:PLN02473   1 MVVKVYGQIKAANPQRVLLCFLEKGIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGDLKLFESRAIARYYATKYAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   81 QGTNLLGKSLEHRAIVDQWADVETYYFNVLAQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGE 160
Cdd:PLN02473  81 QGTDLLGKTLEHRAIVDQWVEVENNYFYAVALPLVINLVFKPRLGEPCDVALVEELKVKFDKVLDVYENRLATNRYLGGD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15237931  161 EFTMADLTHMPAMGYLMSITDINQMVKARGSFNRWWEEISDRPSWKKLMVLAGH 214
Cdd:PLN02473 161 EFTLADLTHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLMELAAY 214
GST_C_Phi cd03187
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione ...
91-209 2.79e-58

C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau 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: 198296 [Multi-domain]  Cd Length: 118  Bit Score: 179.35  E-value: 2.79e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  91 EHRAIVDQWADVETYYFNVLAQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLTHM 170
Cdd:cd03187   1 KERALVEQWLEVEAHQFDPPASKLVFELVFKPMLGLKTDEAVVEENEAKLKKVLDVYEARLSKSKYLAGDSFTLADLSHL 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15237931 171 PAMGYLMSiTDINQMVKARGSFNRWWEEISDRPSWKKLM 209
Cdd:cd03187  81 PNLHYLMA-TPSKKLFDSRPHVKAWWEDISARPAWKKVL 118
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-209 2.64e-41

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 139.26  E-value: 2.64e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   4 KLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFADQGt 83
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  84 nLLGKSLEHRAIVDQWADVETYYFNVLAQPLVInliikpRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFT 163
Cdd:COG0625  82 -LLPADPAARARVRQWLAWADGDLHPALRNLLE------RLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFS 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15237931 164 MADLTHMPAMGYLMSitdINQMVKARGSFNRWWEEISDRPSWKKLM 209
Cdd:COG0625 155 IADIALAPVLRRLDR---LGLDLADYPNLAAWLARLAARPAFQRAL 197
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
1-75 6.26e-20

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: 80.04  E-value: 6.26e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15237931     1 MVVKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYA 75
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIA 75
 
Name Accession Description Interval E-value
PLN02473 PLN02473
glutathione S-transferase
1-214 9.22e-169

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 462.54  E-value: 9.22e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931    1 MVVKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFAD 80
Cdd:PLN02473   1 MVVKVYGQIKAANPQRVLLCFLEKGIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGDLKLFESRAIARYYATKYAD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   81 QGTNLLGKSLEHRAIVDQWADVETYYFNVLAQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGE 160
Cdd:PLN02473  81 QGTDLLGKTLEHRAIVDQWVEVENNYFYAVALPLVINLVFKPRLGEPCDVALVEELKVKFDKVLDVYENRLATNRYLGGD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15237931  161 EFTMADLTHMPAMGYLMSITDINQMVKARGSFNRWWEEISDRPSWKKLMVLAGH 214
Cdd:PLN02473 161 EFTLADLTHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLMELAAY 214
PLN02395 PLN02395
glutathione S-transferase
1-211 3.34e-74

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 223.20  E-value: 3.34e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931    1 MVVKLYGQVTAaCPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFAD 80
Cdd:PLN02395   1 MVLKVYGPAFA-SPKRALVTLIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGDYKIFESRAIMRYYAEKYRS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   81 QGTNLLGKSLEHRAIVDQWADVE--TYYFNVLAqpLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLA 158
Cdd:PLN02395  80 QGPDLLGKTIEERGQVEQWLDVEatSYHPPLLN--LTLHILFASKMGFPADEKVIKESEEKLAKVLDVYEARLSKSKYLA 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15237931  159 GEEFTMADLTHMPAMGYLMSITDINQMVKARGSFNRWWEEISDRPSWKKLMVL 211
Cdd:PLN02395 158 GDFVSLADLAHLPFTEYLVGPIGKAYLIKDRKHVSAWWDDISSRPAWKEVLAK 210
GST_C_Phi cd03187
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione ...
91-209 2.79e-58

C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau 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: 198296 [Multi-domain]  Cd Length: 118  Bit Score: 179.35  E-value: 2.79e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  91 EHRAIVDQWADVETYYFNVLAQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLTHM 170
Cdd:cd03187   1 KERALVEQWLEVEAHQFDPPASKLVFELVFKPMLGLKTDEAVVEENEAKLKKVLDVYEARLSKSKYLAGDSFTLADLSHL 80
                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15237931 171 PAMGYLMSiTDINQMVKARGSFNRWWEEISDRPSWKKLM 209
Cdd:cd03187  81 PNLHYLMA-TPSKKLFDSRPHVKAWWEDISARPAWKKVL 118
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
2-77 1.32e-41

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: 135.47  E-value: 1.32e-41
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237931   2 VVKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATK 77
Cdd:cd03053   1 VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAEK 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
4-209 2.64e-41

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 139.26  E-value: 2.64e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   4 KLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFADQGt 83
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPEPP- 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  84 nLLGKSLEHRAIVDQWADVETYYFNVLAQPLVInliikpRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFT 163
Cdd:COG0625  82 -LLPADPAARARVRQWLAWADGDLHPALRNLLE------RLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGDRFS 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 15237931 164 MADLTHMPAMGYLMSitdINQMVKARGSFNRWWEEISDRPSWKKLM 209
Cdd:COG0625 155 IADIALAPVLRRLDR---LGLDLADYPNLAAWLARLAARPAFQRAL 197
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
3-73 2.59e-20

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: 80.69  E-value: 2.59e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15237931   3 VKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKkpEHLLRQPFGQVPAIEDGDFKLFESRAIARY 73
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQE--EFLALNPLGKVPVLEDGGLVLTESLAILEY 69
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
1-75 6.26e-20

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: 80.04  E-value: 6.26e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15237931     1 MVVKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYA 75
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIA 75
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
14-78 1.21e-17

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: 74.20  E-value: 1.21e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237931  14 PQRVLLCFLEK-GIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKF 78
Cdd:cd03050  11 PSRAVYIFLKLnKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGDFTLAESVAILRYLARKF 76
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
15-79 2.10e-15

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: 68.30  E-value: 2.10e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15237931  15 QRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFA 79
Cdd:cd03046  12 FRILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
4-73 7.47e-14

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: 64.24  E-value: 7.47e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15237931   4 KLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIE--DGDFkLFESRAIARY 73
Cdd:cd03051   2 KLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLEldDGTV-ITESVAICRY 72
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
4-78 1.07e-13

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: 63.72  E-value: 1.07e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15237931   4 KLYGQVTAaCPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIED---GDFKLFESRAIARYYATKF 78
Cdd:cd03048   3 TLYTHGTP-NGFKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDhngTPLTVFESGAILLYLAEKY 79
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
12-77 1.05e-11

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 58.03  E-value: 1.05e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15237931    12 ACP--QRVLLCFLEKGIEFEIIHIDLDTFeQKKPEHLLRQPFGQVPAIEDGD-FKLFESRAIARYYATK 77
Cdd:pfam13409   1 FSPfsHRVRLALEEKGLPYEIELVDLDPK-DKPPELLALNPLGTVPVLVLPDgTVLTDSLVILEYLEEL 68
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
5-80 3.51e-11

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 56.85  E-value: 3.51e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15237931     5 LYGqvTAACP--QRVLLCFLEKGIEFEIIHIDLDtfeQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFAD 80
Cdd:pfam13417   1 LYG--FPGSPyaRRVRIALNEKGLPYEFVPIPPG---DHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPG 73
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
16-75 1.20e-10

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: 55.66  E-value: 1.20e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  16 RVLLCFLekGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYA 75
Cdd:cd03056  16 RLLLALL--GIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYLA 73
PRK15113 PRK15113
glutathione transferase;
23-98 2.56e-10

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 57.66  E-value: 2.56e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15237931   23 EKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFADQGTN-LLGKSLEHRAIVDQ 98
Cdd:PRK15113  28 EKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAPPAWErIYPADLQARARARQ 104
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
4-75 7.86e-10

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: 53.47  E-value: 7.86e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15237931   4 KLYGQVTAACPQRVLLCFLEKGIEFEiiHID-------LDTfeqkkPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYA 75
Cdd:cd03047   2 TIWGRRSSINVQKVLWLLDELGLPYE--RIDaggqfggLDT-----PEFLAMNPNGRVPVLEDGDFVLWESNAILRYLA 73
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
4-73 1.35e-09

GST_N family, Class Zeta 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 Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid.


Pssm-ID: 239340 [Multi-domain]  Cd Length: 73  Bit Score: 52.57  E-value: 1.35e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   4 KLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARY 73
Cdd:cd03042   2 ILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEY 71
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
91-204 4.06e-09

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: 52.71  E-value: 4.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  91 EHRAIVDQW-ADVETYYFNVLAQPLV-INLIIKPRLgEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLT 168
Cdd:cd03182   3 LEKALIEMWqRRAELQGLAPVFQAFRhATPGLKPDR-EVQVPEWGERNKKRVIDFLPVLDKRLAESPYVAGDRFSIADIT 81
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15237931 169 hmpAMGYLMSITDINQMV-KARGSFNRWWEEISDRPS 204
Cdd:cd03182  82 ---AFVALDFAKNLKLPVpEELTALRRWYERMAARPS 115
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
5-78 9.47e-09

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 50.40  E-value: 9.47e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15237931   5 LYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDtfeqKKPEHLLR-QPFGQVPAIEDGDFKLFESRAIARYYATKF 78
Cdd:cd03059   3 LYSGPDDVYSHRVRIVLAEKGVSVEIIDVDPD----NPPEDLAElNPYGTVPTLVDRDLVLYESRIIMEYLDERF 73
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
15-214 9.62e-09

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 53.54  E-value: 9.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   15 QRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGD-------FKLFESRAIARYYATKfadqgTNL-L 86
Cdd:PRK13972  13 HKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAEK-----TGLfL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931   87 GKSLEHRAIVDQW----------ADVETYYFNvLAQPLVINLIIkprlgekcdvvlvEDLKVKLGVVLDIYNNRLSSNRF 156
Cdd:PRK13972  88 SHETRERAATLQWlfwqvgglgpMLGQNHHFN-HAAPQTIPYAI-------------ERYQVETQRLYHVLNKRLENSPW 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15237931  157 LAGEEFTMADLTHMPamgYLMSITDINQMVKARGSFNRWWEEISDRPSWKKLMVLAGH 214
Cdd:PRK13972 154 LGGENYSIADIACWP---WVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQL 208
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
17-73 1.13e-08

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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: 239343 [Multi-domain]  Cd Length: 74  Bit Score: 50.30  E-value: 1.13e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15237931  17 VLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARY 73
Cdd:cd03045  15 VLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIY 71
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
21-75 1.37e-08

GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. 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 members include the class II insect GSTs, S-crystallins from cephalopods 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. Also members are 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: 239337 [Multi-domain]  Cd Length: 72  Bit Score: 49.85  E-value: 1.37e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15237931  21 FLEKGIEFEIIHIDLDTFEQKKPEHLLrqPFGQVPAIEDGDFKLFESRAIARYYA 75
Cdd:cd03039  19 LADAGVEYEDVRITYEEWPELDLKPTL--PFGQLPVLEIDGKKLTQSNAILRYLA 71
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
13-73 2.08e-08

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: 50.04  E-value: 2.08e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15237931  13 CP--QRVLLCFLEKGIEFEIIHIDLDtfeqKKPEHLL-RQPFGQVPAIE-DGDFKLFESRAIARY 73
Cdd:cd03055  27 CPyaQRARLVLAAKNIPHEVININLK----DKPDWFLeKNPQGKVPALEiDEGKVVYESLIICEY 87
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
132-203 7.11e-08

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: 48.44  E-value: 7.11e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15237931   132 LVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLTHMPAMGYLMsITDINQMVKARGSFNRWWEEISDRP 203
Cdd:pfam00043  23 EVDEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLY-ELDPACLREKFPNLKAWFERVAARP 93
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
25-75 4.68e-07

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: 45.71  E-value: 4.68e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15237931  25 GIEFEIIHIDLdTFEQKKPEHLLRQPFGQVPAIEDGD-FKLFESRAIARYYA 75
Cdd:cd03044  23 GLDVEIVDFQP-GKENKTPEFLKKFPLGKVPAFEGADgFCLFESNAIAYYVA 73
GST_N_Pi cd03076
GST_N family, Class Pi subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
14-77 1.90e-06

GST_N family, Class Pi 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 Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumours.


Pssm-ID: 239374 [Multi-domain]  Cd Length: 73  Bit Score: 44.23  E-value: 1.90e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15237931  14 PQRVLLcfLEKGIEFEIIHIDLDTF-EQKKPEHLlrqpFGQVPAIEDGDFKLFESRAIARYYATK 77
Cdd:cd03076  15 AIRLLL--ADQGISWEEERVTYEEWqESLKPKML----FGQLPCFKDGDLTLVQSNAILRHLGRK 73
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
93-203 2.22e-06

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: 44.96  E-value: 2.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  93 RAIVDQWADVETYYFNVLAQPLVINLIIKPRlgEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMAD--LTHM 170
Cdd:cd03180   3 RALADRWMDWQTSTLNPAFRYAFWGLVRTPP--EQRDPAAIAASLAACNKLMAILDAQLARQAYLAGDRFTLADiaLGCS 80
                        90       100       110
                ....*....|....*....|....*....|...
gi 15237931 171 pAMGYLMsiTDINQmvKARGSFNRWWEEISDRP 203
Cdd:cd03180  81 -VYRWLE--LPIER--PALPHLERWYARLSQRP 108
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
22-78 4.13e-06

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: 43.29  E-value: 4.13e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15237931  22 LEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFK-LFESRAIARYYATKF 78
Cdd:cd03057  19 EELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALVLDDGEvLTESAAILQYLADLH 76
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
96-197 4.33e-06

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: 44.03  E-value: 4.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  96 VDQWADvetyYFNVLAQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLTHMPAMGY 175
Cdd:cd00299   1 VRALED----WADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLAR 76
                        90       100
                ....*....|....*....|..
gi 15237931 176 LMSITDINQMVKARGSFNRWWE 197
Cdd:cd00299  77 LEALGPYYDLLDEYPRLKAWYD 98
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
93-209 1.58e-05

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: 42.93  E-value: 1.58e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  93 RAIVDQWADvetyYFNvlaQPLVINL--IIKPRLG-EKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLTH 169
Cdd:cd03181   2 AAQVLQWIS----FAN---SELLPAAatWVLPLLGiAPYNKKAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLADIFV 74
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15237931 170 ----MPAMGYLMSitdiNQMVKARGSFNRWWEEISDRPSWKKLM 209
Cdd:cd03181  75 asalLRGFETVLD----PEFRKKYPNVTRWFNTVVNQPKFKAVF 114
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
143-207 3.27e-05

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: 41.46  E-value: 3.27e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15237931 143 VLDIYNNRLSSNRFLAGEEFTMADLTHMPAMGYLMSITDIN-QMVKArgsFNRWWEEISDRPSWKK 207
Cdd:cd03178  48 LYGVLDKRLSDRPYLAGEEYSIADIALYPWTHYADLGGFADlSEYPN---VKRWLERIAARPAVQK 110
GST_C_YghU_like cd10292
C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and ...
144-207 3.67e-05

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: 41.68  E-value: 3.67e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15237931 144 LDIYNNRLSSNRFLAGEEFTMADLTHMPAMGYLM--SITDINQM--VKARGSFNRWWEEISDRPSWKK 207
Cdd:cd10292  49 LDVLDRQLATHKYLAGDEYTIADMAIWPWYGGLAlgSLYDAAEFldVDEYKHVQRWAKDIAARPAVKR 116
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
105-204 4.17e-05

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: 41.13  E-value: 4.17e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931 105 YYFNVLaQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLThmpaMGYLMSITDINQ 184
Cdd:cd03207   7 FAAGTV-EPPLLNKALGRFFEPPWGEPAIAAAYGDLDERLAALEAALAGRPYLVGERFSAADLL----LASVLRWARAFG 81
                        90       100
                ....*....|....*....|
gi 15237931 185 MVKARGSFNRWWEEISDRPS 204
Cdd:cd03207  82 LLPEYPALRAYVARCTARPA 101
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
16-75 1.08e-04

GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, 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: 239341 [Multi-domain]  Cd Length: 73  Bit Score: 39.12  E-value: 1.08e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  16 RVLLCFLEKGIEFEIIHIDLDTFEQKkPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYA 75
Cdd:cd03043  15 RPWLLLKAAGIPFEEILVPLYTPDTR-ARILEFSPTGKVPVLVDGGIVVWDSLAICEYLA 73
PRK11752 PRK11752
putative S-transferase; Provisional
144-210 1.41e-04

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 41.45  E-value: 1.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15237931  144 LDIYNNRLSSNRFLAGEEFTMADLTHMPAMGYLMsitdINQMVKArGSF---------NRWWEEISDRPSWKK-LMV 210
Cdd:PRK11752 187 LDVLDKQLAEHEYIAGDEYTIADIAIWPWYGNLV----LGNLYDA-AEFldvgsykhvQRWAKEIAERPAVKRgRIV 258
sspA PRK09481
stringent starvation protein A; Provisional
16-78 3.16e-04

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 40.46  E-value: 3.16e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15237931   16 RVLLCflEKGIEFEIIHIDLDTFeqkkPEHLLR-QPFGQVPAIEDGDFKLFESRAIARYYATKF 78
Cdd:PRK09481  26 RIVLA--EKGVSVEIEQVEKDNL----PQDLIDlNPYQSVPTLVDRELTLYESRIIMEYLDERF 83
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
16-73 3.99e-04

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: 37.63  E-value: 3.99e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15237931  16 RVLLCFLEKGIEFEIIHIDldtfEQKKPEHLLRQ-PFGQVPA-IEDGDFKLFESRAIARY 73
Cdd:cd03049  16 RVAAHETGLGDDVELVLVN----PWSDDESLLAVnPLGKIPAlVLDDGEALFDSRVICEY 71
GST_N_Alpha cd03077
GST_N family, Class Alpha subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
25-78 5.69e-03

GST_N family, Class Alpha 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. The class Alpha subfamily is composed of eukaryotic GSTs which can form homodimer and heterodimers. There are at least six types of class Alpha GST subunits in rats, four of which have human counterparts, resulting in many possible isoenzymes with different activities, tissue distribution and substrate specificities. Human GSTA1-1 and GSTA2-2 show high GSH peroxidase activity. GSTA3-3 catalyzes the isomerization of intermediates in steroid hormone biosynthesis. GSTA4-4 preferentially catalyzes the GSH conjugation of alkenals.


Pssm-ID: 239375  Cd Length: 79  Bit Score: 34.81  E-value: 5.69e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15237931  25 GIEFEIIHIDL-DTFEQ-KKPEHLLrqpFGQVPAIEDGDFKLFESRAIARYYATKF 78
Cdd:cd03077  24 GVEFEEKFIESaEDLEKlKKDGSLM---FQQVPMVEIDGMKLVQTRAILNYIAGKY 76
 
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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