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Conserved domains on  [gi|564334241|ref|XP_006231654|]
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glutathione S-transferase omega-2 isoform X1 [Rattus norvegicus]

Protein Classification

glutathione S-transferase omega family protein( domain architecture ID 10122750)

glutathione S-transferase (GST) omega family protein such as class-omega GSTs, which catalyze 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 ...
108-230 4.30e-51

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: 162.49  E-value: 4.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241 108 YERARQKMLLELFCKVPQLSKECLvalRCGRDCTDLKVALRQELCNLEEILEYQNTTFFGGDSISMIDYLVWPWFERLDV 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYKFL---RSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564334241 188 YGLA----DCVNHTPMLRLWISSMKQDPAVCALHIDKNIFLGFLNLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
7-94 4.15e-49

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: 156.36  E-value: 4.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241   7 RCLGKGSCPPGPVPeGVIRIYSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQCQLIYES 86
Cdd:cd03055    3 KHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVYES 81

                 ....*...
gi 564334241  87 VIACEYLD 94
Cdd:cd03055   82 LIICEYLD 89
 
Name Accession Description Interval E-value
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
108-230 4.30e-51

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: 162.49  E-value: 4.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241 108 YERARQKMLLELFCKVPQLSKECLvalRCGRDCTDLKVALRQELCNLEEILEYQNTTFFGGDSISMIDYLVWPWFERLDV 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYKFL---RSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564334241 188 YGLA----DCVNHTPMLRLWISSMKQDPAVCALHIDKNIFLGFLNLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
7-94 4.15e-49

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: 156.36  E-value: 4.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241   7 RCLGKGSCPPGPVPeGVIRIYSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQCQLIYES 86
Cdd:cd03055    3 KHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVYES 81

                 ....*...
gi 564334241  87 VIACEYLD 94
Cdd:cd03055   82 LIICEYLD 89
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
24-213 2.10e-31

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 114.61  E-value: 2.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  24 IRIYSMRFCPYSHRTRLVLKAKSIRHEIININLK---NKPDWYYTKHPFGQVPVLENSQcQLIYESVIACEYLDDVFPGR 100
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGKVPVLVDDG-LVLTESLAILEYLAERYPEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241 101 KLFPYDPYERARQKMLLELF-CKVPQLSKECLVALRCGRDcTDLKVALRQELCNLEEILEYQ--NTTFFGGDSISMIDYL 177
Cdd:COG0625   81 PLLPADPAARARVRQWLAWAdGDLHPALRNLLERLAPEKD-PAAIARARAELARLLAVLEARlaGGPYLAGDRFSIADIA 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564334241 178 VWPWFERLDVYGLAdcVNHTPMLRLWISSMKQDPAV 213
Cdd:COG0625  160 LAPVLRRLDRLGLD--LADYPNLAAWLARLAARPAF 193
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
31-95 4.52e-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: 4.52e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564334241   31 FCPYSHRTRLVLKAKSIRHEI--ININLKNKPDWYYTKHPFGQVPVLENSQCQLIYESVIACEYLDD 95
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIelVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEE 67
sspA PRK09481
stringent starvation protein A; Provisional
23-190 7.42e-11

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 59.72  E-value: 7.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  23 VIRIYSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQCQLiYESVIACEYLDDVFPGRKL 102
Cdd:PRK09481  10 VMTLFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTLVDRELTL-YESRIIMEYLDERFPHPPL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241 103 FPYDPYERARQKMLLE--------LFCKVPQLSKECLVALRcgrdctdlkVALRQELCNLEEIleYQNTTFFGGDSISMI 174
Cdd:PRK09481  89 MPVYPVARGESRLMMHriekdwysLMNKIVNGSASEADAAR---------KQLREELLAIAPV--FGEKPYFMSEEFSLV 157
                        170
                 ....*....|....*.
gi 564334241 175 DYLVWPWFERLDVYGL 190
Cdd:PRK09481 158 DCYLAPLLWRLPVLGI 173
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
32-119 4.40e-08

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 52.69  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  32 CPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQcQLIYESVIACEYLDDVFP------------- 98
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDE-KWVADSDVITQALEEKYPdpplatppekasv 151
                         90       100
                 ....*....|....*....|....*....
gi 564334241  99 GRKLFPY--------DPYERARQKMLLEL 119
Cdd:PLN02817 152 GSKIFSTfigflkskDPGDGTEQALLDEL 180
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
24-54 1.23e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 36.71  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 564334241  24 IRIYSMRFCPYSHRTRLVLKAKSIRHEIINI 54
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDV 32
 
Name Accession Description Interval E-value
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
108-230 4.30e-51

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: 162.49  E-value: 4.30e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241 108 YERARQKMLLELFCKVPQLSKECLvalRCGRDCTDLKVALRQELCNLEEILEYQNTTFFGGDSISMIDYLVWPWFERLDV 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYKFL---RSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 564334241 188 YGLA----DCVNHTPMLRLWISSMKQDPAVCALHIDKNIFLGFLNLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
7-94 4.15e-49

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: 156.36  E-value: 4.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241   7 RCLGKGSCPPGPVPeGVIRIYSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQCQLIYES 86
Cdd:cd03055    3 KHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVYES 81

                 ....*...
gi 564334241  87 VIACEYLD 94
Cdd:cd03055   82 LIICEYLD 89
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
24-213 2.10e-31

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 114.61  E-value: 2.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  24 IRIYSMRFCPYSHRTRLVLKAKSIRHEIININLK---NKPDWYYTKHPFGQVPVLENSQcQLIYESVIACEYLDDVFPGR 100
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGKVPVLVDDG-LVLTESLAILEYLAERYPEP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241 101 KLFPYDPYERARQKMLLELF-CKVPQLSKECLVALRCGRDcTDLKVALRQELCNLEEILEYQ--NTTFFGGDSISMIDYL 177
Cdd:COG0625   81 PLLPADPAARARVRQWLAWAdGDLHPALRNLLERLAPEKD-PAAIARARAELARLLAVLEARlaGGPYLAGDRFSIADIA 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564334241 178 VWPWFERLDVYGLAdcVNHTPMLRLWISSMKQDPAV 213
Cdd:COG0625  160 LAPVLRRLDRLGLD--LADYPNLAAWLARLAARPAF 193
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
31-95 4.52e-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: 4.52e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564334241   31 FCPYSHRTRLVLKAKSIRHEI--ININLKNKPDWYYTKHPFGQVPVLENSQCQLIYESVIACEYLDD 95
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIelVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEE 67
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
24-94 2.20e-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: 66.06  E-value: 2.20e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564334241  24 IRIYSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTK-HPFGQVPVLE-NSQCqlIYESVIACEYLD 94
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLAlNPLGKVPVLEdGGLV--LTESLAILEYLA 71
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
27-97 3.60e-14

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: 65.43  E-value: 3.60e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564334241  27 YSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQCQLiYESVIACEYLDDVF 97
Cdd:cd03059    4 YSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYGTVPTLVDRDLVL-YESRIIMEYLDERF 73
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
23-95 1.22e-12

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: 61.55  E-value: 1.22e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564334241   23 VIRIYSMRFCPYSHRTRLVLKAKSIRHEIININLK---NKPDWYYTKHPFGQVPVLE-NSQCqlIYESVIACEYLDD 95
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPLGKVPALEdGGKK--LTESRAILEYIAR 76
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
27-101 1.51e-12

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 61.09  E-value: 1.51e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564334241   27 YSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQcQLIYESVIACEYLDDVFPGRK 101
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDDG-GILCESLAIIDYLEELYPGPP 75
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
23-95 1.89e-12

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: 61.13  E-value: 1.89e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564334241  23 VIRIYSMRFCPYSHRTRLVLKAKSIRHEIININLK---NKPDWYYTKHPFGQVPVLENSQCQLiYESVIACEYLDD 95
Cdd:cd03053    1 VLKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNPFGQIPALEDGDLKL-FESRAITRYLAE 75
sspA PRK09481
stringent starvation protein A; Provisional
23-190 7.42e-11

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 59.72  E-value: 7.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  23 VIRIYSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQCQLiYESVIACEYLDDVFPGRKL 102
Cdd:PRK09481  10 VMTLFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTLVDRELTL-YESRIIMEYLDERFPHPPL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241 103 FPYDPYERARQKMLLE--------LFCKVPQLSKECLVALRcgrdctdlkVALRQELCNLEEIleYQNTTFFGGDSISMI 174
Cdd:PRK09481  89 MPVYPVARGESRLMMHriekdwysLMNKIVNGSASEADAAR---------KQLREELLAIAPV--FGEKPYFMSEEFSLV 157
                        170
                 ....*....|....*.
gi 564334241 175 DYLVWPWFERLDVYGL 190
Cdd:PRK09481 158 DCYLAPLLWRLPVLGI 173
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
25-94 6.69e-09

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: 51.14  E-value: 6.69e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564334241  25 RIYSMRFCPYSHRTRLVLKAKSIRHEIININL---KNKPDWYYTKHPFGQVPVLENSQCQLIYESVIACEYLD 94
Cdd:cd03051    2 KLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLaagEQRSPEFLAKNPAGTVPVLELDDGTVITESVAICRYLE 74
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
32-119 4.40e-08

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 52.69  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  32 CPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQcQLIYESVIACEYLDDVFP------------- 98
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDE-KWVADSDVITQALEEKYPdpplatppekasv 151
                         90       100
                 ....*....|....*....|....*....
gi 564334241  99 GRKLFPY--------DPYERARQKMLLEL 119
Cdd:PLN02817 152 GSKIFSTfigflkskDPGDGTEQALLDEL 180
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
26-87 5.25e-08

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: 48.89  E-value: 5.25e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564334241  26 IYSMRFCPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQCQLIYESV 87
Cdd:cd03060    3 LYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASPKGTVPVLVLGNGTVIEESL 64
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
33-97 1.67e-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: 47.27  E-value: 1.67e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564334241  33 PYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHP-FGQVPVLENSQCQlIYESVIACEYLDDVF 97
Cdd:cd03058   10 PFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPvHKKIPVLLHNGKP-ICESLIIVEYIDEAW 74
PLN02378 PLN02378
glutathione S-transferase DHAR1
32-187 7.87e-07

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 48.55  E-value: 7.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  32 CPYSHRTRLVLKAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQcQLIYESVIACEYLDDVFPGRKLfpYDPYERA 111
Cdd:PLN02378  20 CPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDD-KWVTDSDVIVGILEEKYPDPPL--KTPAEFA 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564334241 112 rqKMLLELFCKVPQLSKEclvalrcgRDCTD-LKVALRQELCNLEEILEYQNTTFFGGDSISMIDYLVWPWFERLDV 187
Cdd:PLN02378  97 --SVGSNIFGTFGTFLKS--------KDSNDgSEHALLVELEALENHLKSHDGPFIAGERVSAVDLSLAPKLYHLQV 163
PRK15113 PRK15113
glutathione transferase;
23-116 4.01e-06

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 46.49  E-value: 4.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  23 VIRIYS--MRFCPYSHRTRLVLKAKSIRHEIININLKNK----PDwYYTKHPFGQVPVLENSQCQLIYESVIaCEYLDDV 96
Cdd:PRK15113   5 AITLYSdaHFFSPYVMSAFVALQEKGLPFELKTVDLDAGehlqPT-YQGYSLTRRVPTLQHDDFELSESSAI-AEYLEER 82
                         90       100
                 ....*....|....*....|...
gi 564334241  97 FPG---RKLFPYDPYERARQKML 116
Cdd:PRK15113  83 FAPpawERIYPADLQARARARQI 105
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
146-207 2.25e-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: 42.10  E-value: 2.25e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564334241 146 ALRQELCNLEEILE--YQNTTFFGGDSISMIDYLVWPWFERLDVYGLADCVN-HTPMLRLWISSM 207
Cdd:cd00299   36 AAREELPALLAALEqlLAGRPYLAGDQFSLADVALAPVLARLEALGPYYDLLdEYPRLKAWYDRL 100
PLN02473 PLN02473
glutathione S-transferase
23-175 3.04e-05

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 43.82  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  23 VIRIYSMRFCPYSHRTRLVLKAKSIRHEIININL----KNKPDwYYTKHPFGQVPVLENSQCQLIYESVIACEY------ 92
Cdd:PLN02473   2 VVKVYGQIKAANPQRVLLCFLEKGIEFEVIHVDLdkleQKKPE-HLLRQPFGQVPAIEDGDLKLFESRAIARYYatkyad 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564334241  93 -----LDDVFPGRKLFPY------DPYERARQKMLLELFCKvPQLSKECLVALrcgrdCTDLKVALRQELCNLEEILeyQ 161
Cdd:PLN02473  81 qgtdlLGKTLEHRAIVDQwvevenNYFYAVALPLVINLVFK-PRLGEPCDVAL-----VEELKVKFDKVLDVYENRL--A 152
                        170
                 ....*....|....
gi 564334241 162 NTTFFGGDSISMID 175
Cdd:PLN02473 153 TNRYLGGDEFTLAD 166
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
35-94 8.02e-05

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: 39.86  E-value: 8.02e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564334241  35 SHRTRLVLKAKSIRHEIININL----KNKPDwyYTKH-PFGQVPVLENSQcQLIYESVIACEYLD 94
Cdd:cd03042   12 SYRVRIALNLKGLDYEYVPVNLlkgeQLSPA--YRALnPQGLVPTLVIDG-LVLTQSLAIIEYLD 73
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
33-94 2.59e-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: 38.40  E-value: 2.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564334241  33 PYSHRTRLVL--KAKSIRHEIININLKNKPDWYYTKHPFGQVPVLENSQCQLIYESVIACEYLD 94
Cdd:cd03049   10 PYVRKVRVAAheTGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYLD 73
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
24-93 5.76e-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: 37.55  E-value: 5.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564334241  24 IRIYSMRFCPYSHRTRLVLKAKSIRHEIININLKN---KPDWYYTKHPFGQVPVLENSQCQLiYESVIACEYL 93
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKgetRTPEFLALNPNGEVPVLELDGRVL-AESNAILVYL 72
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
35-98 9.23e-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: 37.10  E-value: 9.23e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564334241  35 SHRTRLVLKAKSIRHEIININLKN---KPDWYYTKHPFGQVPVLENSQcQLIYESVIACEYLDDVFP 98
Cdd:cd03046   11 SFRILWLLEELGLPYELVLYDRGPgeqAPPEYLAINPLGKVPVLVDGD-LVLTESAAIILYLAEKYG 76
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
24-54 1.23e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 36.71  E-value: 1.23e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 564334241  24 IRIYSMRFCPYSHRTRLVLKAKSIRHEIINI 54
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDV 32
Glutaredoxin pfam00462
Glutaredoxin;
24-54 1.23e-03

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 36.33  E-value: 1.23e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 564334241   24 IRIYSMRFCPYSHRTRLVLKAKSIRHEIINI 54
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDV 31
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
23-55 2.77e-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: 35.52  E-value: 2.77e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 564334241  23 VIRIYSMRFCPYSHRTRLVLKAKSIRHEIININ 55
Cdd:cd02066    1 KVVVFSKSTCPYCKRAKRLLESLGIEFEEIDIL 33
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
49-98 4.07e-03

GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.


Pssm-ID: 239355 [Multi-domain]  Cd Length: 77  Bit Score: 35.21  E-value: 4.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564334241  49 HEIININLKNK----PDwYYTKHPFGQVPVLENSQCQLIYESVIACEYLDDVFP 98
Cdd:cd03057   25 FELVRVDLRTKtqkgAD-YLAINPKGQVPALVLDDGEVLTESAAILQYLADLHP 77
 
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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