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Conserved domains on  [gi|30697688|ref|NP_568954|]
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glutathione S-transferase tau 9 [Arabidopsis thaliana]

Protein Classification

glutathione S-transferase( domain architecture ID 10221649)

glutathione S-transferase (GST) catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress; similar to class-tau GSTs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 67-200 3.14e-45

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


:

Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 146.55  E-value: 3.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697688  67 PYRRSKVRFWANYIQLHLYDLVIKVVKSEGEEQKKALTEVKEKLSVIEKEGLkeifsdtDGEPTVTNETMSLVDIVMCTL 146
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELK-------GGKPFFGGDTIGYLDIALGSF 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30697688 147 LSPYKAHEEVLGLKIIDPEIVPGVYGWINAINETSVVKDLSPPYEQILEILRAF 200
Cdd:cd03185  74 LGWFKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 9-73 7.94e-28

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03058:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 74  Bit Score: 100.43  E-value: 7.94e-28
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30697688   9 VILHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVHKKIPVLVHNEDPYRRSKV 73
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLI 65
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 67-200 3.14e-45

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 146.55  E-value: 3.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697688  67 PYRRSKVRFWANYIQLHLYDLVIKVVKSEGEEQKKALTEVKEKLSVIEKEGLkeifsdtDGEPTVTNETMSLVDIVMCTL 146
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELK-------GGKPFFGGDTIGYLDIALGSF 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30697688 147 LSPYKAHEEVLGLKIIDPEIVPGVYGWINAINETSVVKDLSPPYEQILEILRAF 200
Cdd:cd03185  74 LGWFKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 9-73 7.94e-28

GST_N family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 100.43  E-value: 7.94e-28
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30697688   9 VILHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVHKKIPVLVHNEDPYRRSKV 73
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLI 65
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
10-179 5.15e-14

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 67.61  E-value: 5.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697688  10 ILHGSFASPYSKRIELALRLKSIPYQFVQEDL---QNKSQTLLRYNPVHkKIPVLVHN---------------------- 64
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLakgEQKSPEFLALNPLG-KVPVLVDDglvlteslaileylaerypepp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697688  65 ---EDPYRRSKVRFWANYIQLHLYDLVIKVVKSEGEEQ-----KKALTEVKEKLSVIEKEglkeiFSDTdgePTVTNETM 136
Cdd:COG0625  82 llpADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpaaiARARAELARLLAVLEAR-----LAGG---PYLAGDRF 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30697688 137 SLVDIVMCTLLSPYKAHEevlglkiIDPEIVPGVYGWINAINE 179
Cdd:COG0625 154 SIADIALAPVLRRLDRLG-------LDLADYPNLAAWLARLAA 189
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
11-71 1.22e-09

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 53.00  E-value: 1.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30697688    11 LHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVhKKIPVLVHNEDPYRRS 71
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPL-GKVPVLEDDGGILCES 60
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 11-83 7.03e-06

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 45.10  E-value: 7.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30697688   11 LHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVhKKIPVLVHNEDPYrrskvrfW------ANYIQLH 83
Cdd:PRK10357   3 LIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVTEEGEC-------WfdspiiAEYIELL 73
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 67-200 3.14e-45

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau 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. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 146.55  E-value: 3.14e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697688  67 PYRRSKVRFWANYIQLHLYDLVIKVVKSEGEEQKKALTEVKEKLSVIEKEGLkeifsdtDGEPTVTNETMSLVDIVMCTL 146
Cdd:cd03185   1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELK-------GGKPFFGGDTIGYLDIALGSF 73

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 30697688 147 LSPYKAHEEVLGLKIIDPEIVPGVYGWINAINETSVVKDLSPPYEQILEILRAF 200
Cdd:cd03185  74 LGWFKAIEEVGGVKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 9-73 7.94e-28

GST_N family, Class Tau 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 plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 239356 [Multi-domain]  Cd Length: 74  Bit Score: 100.43  E-value: 7.94e-28
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30697688   9 VILHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVHKKIPVLVHNEDPYRRSKV 73
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLI 65
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
10-179 5.15e-14

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 67.61  E-value: 5.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697688  10 ILHGSFASPYSKRIELALRLKSIPYQFVQEDL---QNKSQTLLRYNPVHkKIPVLVHN---------------------- 64
Cdd:COG0625   3 KLYGSPPSPNSRRVRIALEEKGLPYELVPVDLakgEQKSPEFLALNPLG-KVPVLVDDglvlteslaileylaerypepp 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30697688  65 ---EDPYRRSKVRFWANYIQLHLYDLVIKVVKSEGEEQ-----KKALTEVKEKLSVIEKEglkeiFSDTdgePTVTNETM 136
Cdd:COG0625  82 llpADPAARARVRQWLAWADGDLHPALRNLLERLAPEKdpaaiARARAELARLLAVLEAR-----LAGG---PYLAGDRF 153

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 30697688 137 SLVDIVMCTLLSPYKAHEevlglkiIDPEIVPGVYGWINAINE 179
Cdd:COG0625 154 SIADIALAPVLRRLDRLG-------LDLADYPNLAAWLARLAA 189
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
11-71 1.22e-09

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 53.00  E-value: 1.22e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30697688    11 LHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVhKKIPVLVHNEDPYRRS 71
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPL-GKVPVLEDDGGILCES 60
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 9-65 9.37e-09

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: 50.26  E-value: 9.37e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30697688   9 VILHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVHKKIPVLVHNE 65
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLALNPLGKVPVLEDGG 57
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 16-63 1.67e-06

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 44.16  E-value: 1.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 30697688    16 ASPYSKRIELALRLKSIPYQ--FVQEDLQNKSQTLLRYNPVHkKIPVLVH 63
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEieLVDLDPKDKPPELLALNPLG-TVPVLVL 49
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 11-83 7.03e-06

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 45.10  E-value: 7.03e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30697688   11 LHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVhKKIPVLVHNEDPYrrskvrfW------ANYIQLH 83
Cdd:PRK10357   3 LIGSYTSPFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPL-GKVPALVTEEGEC-------WfdspiiAEYIELL 73
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 9-80 1.35e-04

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: 39.21  E-value: 1.35e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30697688     9 VILHGSFASPYSKRIELALRLKSIPYQFVQEDL---QNKSQTLLRYNPVhKKIPVLVHNEDPYRRSkvRFWANYI 80
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFgagPEKSPELLKLNPL-GKVPALEDGGKKLTES--RAILEYI 74
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 8-65 1.43e-04

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: 39.17  E-value: 1.43e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30697688   8 KVILHGSFASPYSKRIELALRLKSIPYQFVQEDL---QNKSQTLLRYNPVhKKIPVLVHNE 65
Cdd:cd03053   1 VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLtkgEHKSPEHLARNPF-GQIPALEDGD 60
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 10-84 1.61e-04

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: 38.71  E-value: 1.61e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30697688  10 ILHGSFASPYSKRIELALRLKSIPYQFVQEDLQN---KSQTLLRYNPvHKKIPVLVHNEDPYRRSkvrfwaNYIQLHL 84
Cdd:cd03056   2 KLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKgetRTPEFLALNP-NGEVPVLELDGRVLAES------NAILVYL 72
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 10-65 4.60e-04

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: 37.55  E-value: 4.60e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30697688  10 ILHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRY---NPVhKKIPVLVHNE 65
Cdd:cd03042   2 ILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKGEQLSPAYralNPQ-GLVPTLVIDG 59
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 18-67 1.67e-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: 36.56  E-value: 1.67e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 30697688  18 PYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVhKKIPVLVHNEDP 67
Cdd:cd03055  28 PYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQ-GKVPALEIDEGK 76
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 11-65 5.03e-03

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: 34.61  E-value: 5.03e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 30697688  11 LHGSFASPYSKRIELALRLKSIPYQFVQEDLQNKSQTLLRYNPVHkKIPVLVHNE 65
Cdd:cd03059   3 LYSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYG-TVPTLVDRD 56
 
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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