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Conserved domains on  [gi|21355779|ref|NP_648234|]
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glutathione S transferase O3 [Drosophila melanogaster]

Protein Classification

glutathione S-transferase omega( domain architecture ID 10221648)

class-omega glutathione S-transferase (GST) catalyzes the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins than GSTs

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 109-230 3.24e-55

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 172.89  E-value: 3.24e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779 109 LKRAQDKILLERFSSITSAFINILV----QGTGLEDYWTALDIFEEELTKRGTPYFGGNKPGFVDYMIWPWFERLSVIEL 184
Cdd:cd03184   1 YEKAQQKMLIERFSKVPSAFYKFLRsgedRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEALKL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21355779 185 KLqkEYNFNESRFPKITKWIALLKADSVVQSFYATPEQHNEFWRTR 230
Cdd:cd03184  81 LD--GYELCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 3-95 2.49e-38

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 cd03055:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 89  Bit Score: 128.63  E-value: 2.49e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   3 SGKHLAKGSPKPVLPDdGVLRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLVAEKgep 82
Cdd:cd03055   1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGK--- 76

                        90
                ....*....|...
gi 21355779  83 SLIESLIIAEYLD 95
Cdd:cd03055  77 VVYESLIICEYLD 89
 
Name Accession Description Interval E-value
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 109-230 3.24e-55

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 172.89  E-value: 3.24e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779 109 LKRAQDKILLERFSSITSAFINILV----QGTGLEDYWTALDIFEEELTKRGTPYFGGNKPGFVDYMIWPWFERLSVIEL 184
Cdd:cd03184   1 YEKAQQKMLIERFSKVPSAFYKFLRsgedRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEALKL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21355779 185 KLqkEYNFNESRFPKITKWIALLKADSVVQSFYATPEQHNEFWRTR 230
Cdd:cd03184  81 LD--GYELCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-95 2.49e-38

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: 128.63  E-value: 2.49e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   3 SGKHLAKGSPKPVLPDdGVLRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLVAEKgep 82
Cdd:cd03055   1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGK--- 76

                        90
                ....*....|...
gi 21355779  83 SLIESLIIAEYLD 95
Cdd:cd03055  77 VVYESLIICEYLD 89
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
22-223 9.47e-36

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 125.78  E-value: 9.47e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  22 LRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINL---TEKPEWLVEVSPLLKVPALqlvaEKGEPSLIESLIIAEYLDDKY 98
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLakgEQKSPEFLALNPLGKVPVL----VDDGLVLTESLAILEYLAERY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  99 PENPLLPKDPLKRAQDKILLERF-SSITSAFINILVQGTG----------LEDYWTALDIFEEELTKRgtPYFGGNKPGF 167
Cdd:COG0625  78 PEPPLLPADPAARARVRQWLAWAdGDLHPALRNLLERLAPekdpaaiaraRAELARLLAVLEARLAGG--PYLAGDRFSI 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21355779 168 VDYMIWPWFERLSVIELKLqkeynfneSRFPKITKWIALLKADSVVQSFYATPEQH 223
Cdd:COG0625 156 ADIALAPVLRRLDRLGLDL--------ADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
24-102 6.27e-22

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 85.74  E-value: 6.27e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355779    24 LYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLvaekGEPSLIESLIIAEYLDDKYPENP 102
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLED----DGGILCESLAIIDYLEELYPGPP 75
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 35-169 1.25e-15

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 72.74  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779    35 RAHLVLNAKNVPYHSVYINLTE-----KPEWLvEVSPLLKVPALQLvaekGEPSLIESLIIAEYLDDKYPENPLLPKDPL 109
Cdd:TIGR01262  13 RVRIALALKGIDYEYVPVNLLRdgeqrSPEFL-ALNPQGLVPTLDI----DGEVLTQSLAIIEYLEETYPDPPLLPADPI 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355779   110 KRAQDKILlerfSSITSAFI---------NILVQGTGLED----YWTA------LDIFEEELTKRGTPYFGGNKPGFVD 169
Cdd:TIGR01262  88 KRARVRAL----ALLIACDIhplnnlrvlQYLREKLGVEEearnRWYQhwiskgFAALEALLQPHAGRFCVGDTPTLAD 162
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 30-233 1.80e-15

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 73.49  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   30 CPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLvaekGEPSLIESLIIAEYLDDKYPENPLlpKDPL 109
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKL----DEKWVADSDVITQALEEKYPDPPL--ATPP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  110 KRAQDKillerfSSITSAFINILVQ---GTGLED-YWTALDIFEEELTKRGtPYFGGNKPGFVDYMIWPWFERLSvIELK 185
Cdd:PLN02817 147 EKASVG------SKIFSTFIGFLKSkdpGDGTEQaLLDELTSFDDYIKENG-PFINGEKISAADLSLGPKLYHLE-IALG 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 21355779  186 LQKEYNFNESrFPKITKWIA-LLKADSVVQSfYATPEQHNEFWRTRKAG 233
Cdd:PLN02817 219 HYKNWSVPDS-LPFVKSYMKnIFSMESFVKT-RALPEDVIAGWRPKVMG 265
PRK15113 PRK15113
glutathione transferase;
17-112 1.21e-10

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 59.20  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   17 PDDGVLRLYS--MRFCPYAQRAHLVLNAKNVPYHSVYINLTEK----PEWlVEVSPLLKVPALQLvaekGEPSLIESLII 90
Cdd:PRK15113   1 MSKPAITLYSdaHFFSPYVMSAFVALQEKGLPFELKTVDLDAGehlqPTY-QGYSLTRRVPTLQH----DDFELSESSAI 75

                         90       100
                 ....*....|....*....|....*
gi 21355779   91 AEYLDDKYPE---NPLLPKDPLKRA 112
Cdd:PRK15113  76 AEYLEERFAPpawERIYPADLQARA 100
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 138-205 5.03e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 40.38  E-value: 5.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355779   138 LEDYWTALDIFEEELtkRGTPYFGGNKPGFVDYMIWPWFERLSVIELKLqkeynFNESRFPKITKWIA 205
Cdd:pfam13410   6 REQLRAALDALEARL--ADGPGLLGDRPTLADIALAPVLARLDAAYPGL-----DLREGYPRLRAWLE 66
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
22-73 4.52e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.87  E-value: 4.52e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21355779  22 LRLYSMRFCPYAQRAHLVLNAKNVPYhsVYINLTEKPE---WLVEVSPLLKVPAL 73
Cdd:COG0695   2 VTLYTTPGCPYCARAKRLLDEKGIPY--EEIDVDEDPEareELRERSGRRTVPVI 54
 
Name Accession Description Interval E-value
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 109-230 3.24e-55

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 172.89  E-value: 3.24e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779 109 LKRAQDKILLERFSSITSAFINILV----QGTGLEDYWTALDIFEEELTKRGTPYFGGNKPGFVDYMIWPWFERLSVIEL 184
Cdd:cd03184   1 YEKAQQKMLIERFSKVPSAFYKFLRsgedRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEALKL 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 21355779 185 KLqkEYNFNESRFPKITKWIALLKADSVVQSFYATPEQHNEFWRTR 230
Cdd:cd03184  81 LD--GYELCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 3-95 2.49e-38

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: 128.63  E-value: 2.49e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   3 SGKHLAKGSPKPVLPDdGVLRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLVAEKgep 82
Cdd:cd03055   1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGK--- 76

                        90
                ....*....|...
gi 21355779  83 SLIESLIIAEYLD 95
Cdd:cd03055  77 VVYESLIICEYLD 89
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
22-223 9.47e-36

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 125.78  E-value: 9.47e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  22 LRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINL---TEKPEWLVEVSPLLKVPALqlvaEKGEPSLIESLIIAEYLDDKY 98
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLakgEQKSPEFLALNPLGKVPVL----VDDGLVLTESLAILEYLAERY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  99 PENPLLPKDPLKRAQDKILLERF-SSITSAFINILVQGTG----------LEDYWTALDIFEEELTKRgtPYFGGNKPGF 167
Cdd:COG0625  78 PEPPLLPADPAARARVRQWLAWAdGDLHPALRNLLERLAPekdpaaiaraRAELARLLAVLEARLAGG--PYLAGDRFSI 155

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21355779 168 VDYMIWPWFERLSVIELKLqkeynfneSRFPKITKWIALLKADSVVQSFYATPEQH 223
Cdd:COG0625 156 ADIALAPVLRRLDRLGLDL--------ADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
24-102 6.27e-22

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 85.74  E-value: 6.27e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355779    24 LYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLvaekGEPSLIESLIIAEYLDDKYPENP 102
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLED----DGGILCESLAIIDYLEELYPGPP 75
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 29-97 4.60e-16

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 70.35  E-value: 4.60e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 21355779    29 FCPYAQRAHLVLNAKNVPYHSVYINLT--EKPEWLVEVSPLLKVPALQLvaEKGEPsLIESLIIAEYLDDK 97
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLDpkDKPPELLALNPLGTVPVLVL--PDGTV-LTDSLVILEYLEEL 68
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 35-169 1.25e-15

maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and phenylalanine catabolism. It requires glutathione and belongs by homology to the zeta family of glutathione S-transferases. The enzyme (EC 5.2.1.2) is described as active also on maleylpyruvate, and the example from a Ralstonia sp. catabolic plasmid is described as a maleylpyruvate isomerase involved in gentisate catabolism. [Energy metabolism, Amino acids and amines]


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 72.74  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779    35 RAHLVLNAKNVPYHSVYINLTE-----KPEWLvEVSPLLKVPALQLvaekGEPSLIESLIIAEYLDDKYPENPLLPKDPL 109
Cdd:TIGR01262  13 RVRIALALKGIDYEYVPVNLLRdgeqrSPEFL-ALNPQGLVPTLDI----DGEVLTQSLAIIEYLEETYPDPPLLPADPI 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355779   110 KRAQDKILlerfSSITSAFI---------NILVQGTGLED----YWTA------LDIFEEELTKRGTPYFGGNKPGFVD 169
Cdd:TIGR01262  88 KRARVRAL----ALLIACDIhplnnlrvlQYLREKLGVEEearnRWYQhwiskgFAALEALLQPHAGRFCVGDTPTLAD 162
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 30-233 1.80e-15

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 73.49  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   30 CPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLvaekGEPSLIESLIIAEYLDDKYPENPLlpKDPL 109
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKL----DEKWVADSDVITQALEEKYPDPPL--ATPP 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  110 KRAQDKillerfSSITSAFINILVQ---GTGLED-YWTALDIFEEELTKRGtPYFGGNKPGFVDYMIWPWFERLSvIELK 185
Cdd:PLN02817 147 EKASVG------SKIFSTFIGFLKSkdpGDGTEQaLLDELTSFDDYIKENG-PFINGEKISAADLSLGPKLYHLE-IALG 218

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 21355779  186 LQKEYNFNESrFPKITKWIA-LLKADSVVQSfYATPEQHNEFWRTRKAG 233
Cdd:PLN02817 219 HYKNWSVPDS-LPFVKSYMKnIFSMESFVKT-RALPEDVIAGWRPKVMG 265
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 22-95 7.89e-14

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: 64.52  E-value: 7.89e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 21355779  22 LRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKP-EWLVEVSPLLKVPALQLvaekGEPSLIESLIIAEYLD 95
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEqEEFLALNPLGKVPVLED----GGLVLTESLAILEYLA 71
sspA PRK09481
stringent starvation protein A; Provisional
 21-184 1.58e-13

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 67.04  E-value: 1.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   21 VLRLYSMRFCPYAQRAHLVLNAKNVpyhSVYINLTEK---PEWLVEVSPLLKVPALQlvaeKGEPSLIESLIIAEYLDDK 97
Cdd:PRK09481  10 VMTLFSGPTDIYSHQVRIVLAEKGV---SVEIEQVEKdnlPQDLIDLNPYQSVPTLV----DRELTLYESRIIMEYLDER 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   98 YPENPLLPKDPLKRAQDKILLERFSSITSAFINILVQGTGlEDYWTALDIFEEELTKRG-----TPYFGGNKPGFVDYMI 172
Cdd:PRK09481  83 FPHPPLMPVYPVARGESRLMMHRIEKDWYSLMNKIVNGSA-SEADAARKQLREELLAIApvfgeKPYFMSEEFSLVDCYL 161

                        170
                 ....*....|....
gi 21355779  173 WPWFERLSV--IEL 184
Cdd:PRK09481 162 APLLWRLPVlgIEL 175
PLN02378 PLN02378
glutathione S-transferase DHAR1
 30-207 4.66e-11

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 60.50  E-value: 4.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   30 CPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLvaekGEPSLIESLIIAEYLDDKYPENPLlpKDPL 109
Cdd:PLN02378  20 CPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKI----DDKWVTDSDVIVGILEEKYPDPPL--KTPA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  110 KraqdkillerFSSITSAFINILvqGTGLED----------YWTALDIFEEELTKRGTPYFGGNKPGFVDYMIWPWFERL 179
Cdd:PLN02378  94 E----------FASVGSNIFGTF--GTFLKSkdsndgsehaLLVELEALENHLKSHDGPFIAGERVSAVDLSLAPKLYHL 161

                        170       180
                 ....*....|....*....|....*...
gi 21355779  180 SViELKLQKEYNFNESrFPKITKWIALL 207
Cdd:PLN02378 162 QV-ALGHFKSWSVPES-FPHVHNYMKTL 187
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 21-96 4.79e-11

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: 56.93  E-value: 4.79e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355779    21 VLRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLT---EKPEWLVEVSPLLKVPALqlvaEKGEPSLIESLIIAEYLDD 96
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPLGKVPAL----EDGGKKLTESRAILEYIAR 76
PRK15113 PRK15113
glutathione transferase;
17-112 1.21e-10

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 59.20  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   17 PDDGVLRLYS--MRFCPYAQRAHLVLNAKNVPYHSVYINLTEK----PEWlVEVSPLLKVPALQLvaekGEPSLIESLII 90
Cdd:PRK15113   1 MSKPAITLYSdaHFFSPYVMSAFVALQEKGLPFELKTVDLDAGehlqPTY-QGYSLTRRVPTLQH----DDFELSESSAI 75

                         90       100
                 ....*....|....*....|....*
gi 21355779   91 AEYLDDKYPE---NPLLPKDPLKRA 112
Cdd:PRK15113  76 AEYLEERFAPpawERIYPADLQARA 100
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 22-98 4.14e-10

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: 54.64  E-value: 4.14e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  22 LRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPAL---QLVaekgepsLIESLIIAEYLDDKY 98
Cdd:cd03059   1 MTLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYGTVPTLvdrDLV-------LYESRIIMEYLDERF 73
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 21-97 1.09e-08

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: 50.73  E-value: 1.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  21 VLRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLT---EKPEWLVEVSPLLKVPALqlvaEKGEPSLIESLIIAEYLDDK 97
Cdd:cd03053   1 VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNPFGQIPAL----EDGDLKLFESRAITRYLAEK 76
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 137-213 1.26e-07

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: 49.10  E-value: 1.26e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779 137 GLEDYWTALDIFEEELtKRGTPYFGGNKPGFVD---YMIWPWFERLS-VIELKLqkeynFNESRFPKITKWIALLKADSV 212
Cdd:cd03185  36 AVEEALEALKVLEEEL-KGGKPFFGGDTIGYLDialGSFLGWFKAIEeVGGVKL-----LDEEKFPLLAAWAERFLEREA 109


                .
gi 21355779 213 V 213
Cdd:cd03185 110 V 110
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 22-96 3.79e-07

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: 46.50  E-value: 3.79e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 21355779  22 LRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLL-KVPALQLVaekGEPsLIESLIIAEYLDD 96
Cdd:cd03058   1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHkKIPVLLHN---GKP-ICESLIIVEYIDE 72
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 29-99 6.53e-07

GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas paucimobilis beta etherase, LigE, a GST-like protein that catalyzes the cleavage of the beta-aryl ether linkages present in low-moleculer weight lignins using GSH as the hydrogen donor. This reaction is an essential step in the degradation of lignin, a complex phenolic polymer that is the most abundant aromatic material in the biosphere. The beta etherase activity of LigE is enantioselective and it complements the activity of the other GST family beta etherase, LigF.


Pssm-ID: 239336 [Multi-domain]  Cd Length: 84  Bit Score: 46.19  E-value: 6.53e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355779  29 FCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEV--SPLLKVPALQLVAEKgepSLIESLIIAEYLDDKYP 99
Cdd:cd03038  15 FSPNVWKTRLALNHKGLEYKTVPVEFPDIPPILGELtsGGFYTVPVIVDGSGE---VIGDSFAIAEYLEEAYP 84
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 31-109 7.22e-06

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 45.48  E-value: 7.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355779   31 PYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALqlVAEKGEpSLIESLIIAEYLDDKYPENPLLPKDPL 109
Cdd:PRK10357  10 PFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPAL--VTEEGE-CWFDSPIIAEYIELLNVAPAMLPRDPL 85
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 31-95 1.38e-05

GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239347 [Multi-domain]  Cd Length: 73  Bit Score: 41.86  E-value: 1.38e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 21355779  31 PYAQRAHLVL--NAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLvaEKGEpSLIESLIIAEYLD 95
Cdd:cd03049  10 PYVRKVRVAAheTGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVL--DDGE-ALFDSRVICEYLD 73
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 143-205 3.81e-05

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: 41.33  E-value: 3.81e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21355779 143 TALDIFEEELTKRgtPYFGGNKPGFVDYMIWPWFERLSVIelklqKEYNFNESRFPKITKWIA 205
Cdd:cd00299  43 ALLAALEQLLAGR--PYLAGDQFSLADVALAPVLARLEAL-----GPYYDLLDEYPRLKAWYD 98
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 138-205 5.03e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 40.38  E-value: 5.03e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 21355779   138 LEDYWTALDIFEEELtkRGTPYFGGNKPGFVDYMIWPWFERLSVIELKLqkeynFNESRFPKITKWIA 205
Cdd:pfam13410   6 REQLRAALDALEARL--ADGPGLLGDRPTLADIALAPVLARLDAAYPGL-----DLREGYPRLRAWLE 66
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 24-90 1.27e-04

GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega 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. 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. Like Omega enzymes, proteins in this subfamily 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.


Pssm-ID: 239358 [Multi-domain]  Cd Length: 71  Bit Score: 39.26  E-value: 1.27e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21355779  24 LYSMRFCPYAQRAH--LVLNAKNVPYHSVyiNLTEKPEWLVEVSPLLKVPALQLvaeKGEPSLIESLII 90
Cdd:cd03060   3 LYSFRRCPYAMRARmaLLLAGITVELREV--ELKNKPAEMLAASPKGTVPVLVL---GNGTVIEESLDI 66
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 30-95 4.15e-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: 37.93  E-value: 4.15e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  30 CPYaqRAHLVLNAKNVPYHSVYINLTE----KPEWLvEVSPLLKVPALQLvaekGEPSLIESLIIAEYLD 95
Cdd:cd03042  11 ASY--RVRIALNLKGLDYEYVPVNLLKgeqlSPAYR-ALNPQGLVPTLVI----DGLVLTQSLAIIEYLD 73
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
22-73 4.52e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.87  E-value: 4.52e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 21355779  22 LRLYSMRFCPYAQRAHLVLNAKNVPYhsVYINLTEKPE---WLVEVSPLLKVPAL 73
Cdd:COG0695   2 VTLYTTPGCPYCARAKRLLDEKGIPY--EEIDVDEDPEareELRERSGRRTVPVI 54
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 33-99 5.94e-04

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: 37.48  E-value: 5.94e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779  33 AQRAHLVLNAKNVPYHSVYINLTE---KPEWLVEVSPLLKVPALqlvaEKGEPSLIESLIIAEYLDDKYP 99
Cdd:cd03046  11 SFRILWLLEELGLPYELVLYDRGPgeqAPPEYLAINPLGKVPVL----VDGDLVLTESAAIILYLAEKYG 76
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 144-203 3.04e-03

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: 36.11  E-value: 3.04e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21355779   144 ALDIFEEELTKRGtpYFGGNKPGFVDYMIWPWFERLsvielkLQKEYNFNESRFPKITKW 203
Cdd:pfam00043  34 VLSALEEVLKGQT--YLVGDKLTLADIALAPALLWL------YELDPACLREKFPNLKAW 85
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
 35-94 6.19e-03

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: 34.49  E-value: 6.19e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21355779  35 RAHLVLNAKNVPYHSVYINLT--EKPEWLVEVSPLLKVPALQLvaekGEPSLIESLIIAEYL 94
Cdd:cd03043  15 RPWLLLKAAGIPFEEILVPLYtpDTRARILEFSPTGKVPVLVD----GGIVVWDSLAICEYL 72
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 21-73 8.57e-03

Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, as well as E. coli GRX1 and GRX3, which are members of this family. E. coli GRX2, however, is a 24-kDa protein that belongs to the GSH S-transferase (GST) family.


Pssm-ID: 239017 [Multi-domain]  Cd Length: 72  Bit Score: 33.98  E-value: 8.57e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 21355779  21 VLRLYSMRFCPYAQRAHLVLNAKNVPYhsVYINLTEKPE---WLVEVSPLLKVPAL 73
Cdd:cd02066   1 KVVVFSKSTCPYCKRAKRLLESLGIEF--EEIDILEDGElreELKELSGWPTVPQI 54
 
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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