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Conserved domains on  [gi|1393763089|ref|WP_109912176|]
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MULTISPECIES: glutaredoxin 2 [Providencia]

Protein Classification

glutaredoxin 2( domain architecture ID 11459498)

glutaredoxin 2 is an aytpical glutaredoxin that catalyzes the glutathione dependent protein disulfide reduction of certain substrates, primarily proteins involved in cellular redox regulation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
1-210 1.13e-105

Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 302.92  E-value: 1.13e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVDSINEPKYAKG 80
Cdd:COG2999     1 MKLYIYDHCPFCVRARMIFGLKNIPVELIVLLNDDEETPIRMIGKKMVPILEKDDGSYMPESLDIVHYIDELDGKPILTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  81 SIAPEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLET 160
Cdd:COG2999    81 PVRPEIAAWLKKVSSYVNRLLYPRWAKAPLPEFATPSARAYFINKKEASIGDFEELLANTPELIAELNQDLEELEPLIKS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393763089 161 RSED---IDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLLFDK 210
Cdd:COG2999   161 PSAVngeLSLDDIILFPLLRSLTIVKGIQFPPKVRAYRDRMSKKTGVPLLDDV 213
 
Name Accession Description Interval E-value
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
1-210 1.13e-105

Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 302.92  E-value: 1.13e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVDSINEPKYAKG 80
Cdd:COG2999     1 MKLYIYDHCPFCVRARMIFGLKNIPVELIVLLNDDEETPIRMIGKKMVPILEKDDGSYMPESLDIVHYIDELDGKPILTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  81 SIAPEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLET 160
Cdd:COG2999    81 PVRPEIAAWLKKVSSYVNRLLYPRWAKAPLPEFATPSARAYFINKKEASIGDFEELLANTPELIAELNQDLEELEPLIKS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393763089 161 RSED---IDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLLFDK 210
Cdd:COG2999   161 PSAVngeLSLDDIILFPLLRSLTIVKGIQFPPKVRAYRDRMSKKTGVPLLDDV 213
PRK10387 PRK10387
glutaredoxin 2; Provisional
 1-207 5.13e-96

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 278.30  E-value: 5.13e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVDSINEPKYAKG 80
Cdd:PRK10387    1 MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYIDELDGKPLLTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  81 SIAPEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLET 160
Cdd:PRK10387   81 KRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHTPGLIKEINADLRALDPLIVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1393763089 161 RSED---IDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLL 207
Cdd:PRK10387  161 PNAVngeLSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL 210
GRXB TIGR02182
Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 2-207 2.80e-69

Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase, and may have more to do with resistance to redox stress. [Energy metabolism, Electron transport]


Pssm-ID: 274018 [Multi-domain]  Cd Length: 209  Bit Score: 210.40  E-value: 2.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   2 KLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVDSINEPKYAKGS 81
Cdd:TIGR02182   1 KLYIYDHCPFCVRARMIFGLKNIPVEKHVLLNDDEETPIRMIGAKQVPILQKDDGRAMPESLDIVAYFDKLDGEPLLTGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  82 IAPEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLETR 161
Cdd:TIGR02182  81 VSPEIEAWLRKVTGYANKLLLPRFAKSDLPEFATQSARKYFTDKKEASAGNFSALLNHTPGLLEEINADLEELDKLIDGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1393763089 162 SE---DIDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLL 207
Cdd:TIGR02182 161 NAvngELSEDDILVFPLLRNLTLVAGINWPSRVADYLDNMSKKSKVPLL 209
GST_C_GRX2 cd03199
C-terminal, alpha helical domain of Glutaredoxin 2; Glutathione S-transferase (GST) C-terminal ...
 84-207 1.77e-40

C-terminal, alpha helical domain of Glutaredoxin 2; Glutathione S-transferase (GST) C-terminal domain family, Glutaredoxin 2 (GRX2) subfamily; composed of Escherichia coli GRX2 and similar proteins. Escherichia coli GRX2 is an atypical GRX with a molecular mass of about 24kD (most GRXs range from 9-12kD). It adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain, but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.


Pssm-ID: 198308  Cd Length: 128  Bit Score: 134.21  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  84 PEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLETrSE 163
Cdd:cd03199     2 PEIAAWLKQVGPYYNRLLLPRFAKADLPEFATPSARAYFIRKKEASIGSFEELLAKTPELIAELNADLEALDPLILS-SD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1393763089 164 DID----INDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLL 207
Cdd:cd03199    81 AVNgelsYDDIILFPLLRNLTIVKGLEFPPKVRAYIDNMSALSDVPLY 128
Glutaredoxin2_C pfam04399
Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of ...
 85-210 4.20e-32

Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of glutathione-dependent disulphide oxidoreductases. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide reductase. Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxins. The active site residues (Cys9-Pro10-Tyr11-Cys12, in Escherichia coli Grx2, Swiss:P39811), which are found at the interface between the N- and C-terminal domains are identical to other glutaredoxins, but there is no other similarity between glutaredoxin 2 and other glutaredoxins. Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity. The inter-domain contacts are mainly hydrophobic, suggesting that the two domains are unlikely to be stable on their own. Both domains are needed for correct folding and activity of Grx2. It is thought that the primary function of Grx2 is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress.


Pssm-ID: 461291  Cd Length: 130  Bit Score: 113.06  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  85 EIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLETRSED 164
Cdd:pfam04399   1 EIAAWLKRVFPYLNRLLLPRFAAAPLPEFATQSAREYFRNKKEASIGSFEELLAKSPELIAQLNADLEALEPLILSSHAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1393763089 165 ---IDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLLFDK 210
Cdd:pfam04399  81 ngqLSYDDILLFPILRSLTIVKGLQWPPEVRAYLDRMSAATGVPLLDDI 129
 
Name Accession Description Interval E-value
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
1-210 1.13e-105

Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 302.92  E-value: 1.13e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVDSINEPKYAKG 80
Cdd:COG2999     1 MKLYIYDHCPFCVRARMIFGLKNIPVELIVLLNDDEETPIRMIGKKMVPILEKDDGSYMPESLDIVHYIDELDGKPILTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  81 SIAPEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLET 160
Cdd:COG2999    81 PVRPEIAAWLKKVSSYVNRLLYPRWAKAPLPEFATPSARAYFINKKEASIGDFEELLANTPELIAELNQDLEELEPLIKS 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1393763089 161 RSED---IDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLLFDK 210
Cdd:COG2999   161 PSAVngeLSLDDIILFPLLRSLTIVKGIQFPPKVRAYRDRMSKKTGVPLLDDV 213
PRK10387 PRK10387
glutaredoxin 2; Provisional
 1-207 5.13e-96

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 278.30  E-value: 5.13e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVDSINEPKYAKG 80
Cdd:PRK10387    1 MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYIDELDGKPLLTG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  81 SIAPEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLET 160
Cdd:PRK10387   81 KRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHTPGLIKEINADLRALDPLIVK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1393763089 161 RSED---IDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLL 207
Cdd:PRK10387  161 PNAVngeLSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL 210
GRXB TIGR02182
Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 2-207 2.80e-69

Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This model includes the highly abundant E. coli GrxB (Grx2) glutaredoxin which is notably longer than either GrxA or GrxC. Unlike the other two E. coli glutaredoxins, GrxB appears to be unable to reduce ribonucleotide reductase, and may have more to do with resistance to redox stress. [Energy metabolism, Electron transport]


Pssm-ID: 274018 [Multi-domain]  Cd Length: 209  Bit Score: 210.40  E-value: 2.80e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   2 KLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVDSINEPKYAKGS 81
Cdd:TIGR02182   1 KLYIYDHCPFCVRARMIFGLKNIPVEKHVLLNDDEETPIRMIGAKQVPILQKDDGRAMPESLDIVAYFDKLDGEPLLTGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  82 IAPEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLETR 161
Cdd:TIGR02182  81 VSPEIEAWLRKVTGYANKLLLPRFAKSDLPEFATQSARKYFTDKKEASAGNFSALLNHTPGLLEEINADLEELDKLIDGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1393763089 162 SE---DIDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLL 207
Cdd:TIGR02182 161 NAvngELSEDDILVFPLLRNLTLVAGINWPSRVADYLDNMSKKSKVPLL 209
GST_C_GRX2 cd03199
C-terminal, alpha helical domain of Glutaredoxin 2; Glutathione S-transferase (GST) C-terminal ...
 84-207 1.77e-40

C-terminal, alpha helical domain of Glutaredoxin 2; Glutathione S-transferase (GST) C-terminal domain family, Glutaredoxin 2 (GRX2) subfamily; composed of Escherichia coli GRX2 and similar proteins. Escherichia coli GRX2 is an atypical GRX with a molecular mass of about 24kD (most GRXs range from 9-12kD). It adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain, but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.


Pssm-ID: 198308  Cd Length: 128  Bit Score: 134.21  E-value: 1.77e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  84 PEIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLETrSE 163
Cdd:cd03199     2 PEIAAWLKQVGPYYNRLLLPRFAKADLPEFATPSARAYFIRKKEASIGSFEELLAKTPELIAELNADLEALDPLILS-SD 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1393763089 164 DID----INDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLL 207
Cdd:cd03199    81 AVNgelsYDDIILFPLLRNLTIVKGLEFPPKVRAYIDNMSALSDVPLY 128
GST_N_GRX2 cd03037
GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. ...
 1-70 5.79e-40

GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. coli GRX2, an atypical GRX with a molecular mass of about 24kD, compared with other GRXs which are 9-12kD in size. GRX2 adopts a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. It contains a redox active CXXC motif located in the N-terminal domain but is not able to reduce ribonucleotide reductase like other GRXs. However, it catalyzes GSH-dependent protein disulfide reduction of other substrates efficiently. GRX2 is thought to function primarily in catalyzing the reversible glutathionylation of proteins in cellular redox regulation including stress responses.


Pssm-ID: 239335 [Multi-domain]  Cd Length: 71  Bit Score: 131.36  E-value: 5.79e-40
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVD 70
Cdd:cd03037     1 MKLYIYEHCPFCVKARMIAGLKNIPVEQIILQNDDEATPIRMIGAKQVPILEKDDGSFMAESLDIVAFID 70
Glutaredoxin2_C pfam04399
Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of ...
 85-210 4.20e-32

Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of glutathione-dependent disulphide oxidoreductases. Unlike other glutaredoxins, glutaredoxin 2 (Grx2) cannot reduce ribonucleotide reductase. Grx2 has significantly higher catalytic activity in the reduction of mixed disulphides with glutathione (GSH) compared with other glutaredoxins. The active site residues (Cys9-Pro10-Tyr11-Cys12, in Escherichia coli Grx2, Swiss:P39811), which are found at the interface between the N- and C-terminal domains are identical to other glutaredoxins, but there is no other similarity between glutaredoxin 2 and other glutaredoxins. Grx2 is structurally similar to glutathione-S-transferases (GST), but there is no obvious sequence similarity. The inter-domain contacts are mainly hydrophobic, suggesting that the two domains are unlikely to be stable on their own. Both domains are needed for correct folding and activity of Grx2. It is thought that the primary function of Grx2 is to catalyze reversible glutathionylation of proteins with GSH in cellular redox regulation including the response to oxidative stress.


Pssm-ID: 461291  Cd Length: 130  Bit Score: 113.06  E-value: 4.20e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  85 EIETWSKTVSAVVYKLVTPRFTQTDFPEISTAEARAAYISRTSKSYGDLNELKKETHTLLVELEPQLSLLDAWLETRSED 164
Cdd:pfam04399   1 EIAAWLKRVFPYLNRLLLPRFAAAPLPEFATQSAREYFRNKKEASIGSFEELLAKSPELIAQLNADLEALEPLILSSHAV 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1393763089 165 ---IDINDFIIFPTLRSLSIVEHLSFSTNIRNYMERIAKSTNINLLFDK 210
Cdd:pfam04399  81 ngqLSYDDILLFPILRSLTIVKGLQWPPEVRAYLDRMSAATGVPLLDDI 129
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 1-70 1.13e-10

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: 55.66  E-value: 1.13e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIV--LFDDDIETPTKMIGRKMLPILQkDDGSYLPESLDIVHYVD 70
Cdd:cd00570     1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPvdLGEGEQEEFLALNPLGKVPVLE-DGGLVLTESLAILEYLA 71
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
3-72 7.48e-09

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 50.69  E-value: 7.48e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393763089   3 LYIYDHCPFCVRARMIFGLKKLAVEQI-VLFDDDIETPTKMIGRKMLPILQkDDGSYLPESLDIVHYVDSI 72
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVpIPPGDHPPELLAKNPLGKVPVLE-DDGGILCESLAIIDYLEEL 70
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-199 3.01e-08

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 51.82  E-value: 3.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGRK----MLPILQkDDGSYLPESLDIVHYVDSinepK 76
Cdd:COG0625     2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALnplgKVPVLV-DDGLVLTESLAILEYLAE----R 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1393763089  77 YAKGSIAP-------EIETWSKTVSAVVYKLVTPRFTQtdFPEISTAEARAAYISrtsksygdlnelkkethtllvELEP 149
Cdd:COG0625    77 YPEPPLLPadpaaraRVRQWLAWADGDLHPALRNLLER--LAPEKDPAAIARARA---------------------ELAR 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1393763089 150 QLSLLDAWLETR----SEDIDINDFIIFPTLRSLSIVE-HLSFSTNIRNYMERIA 199
Cdd:COG0625   134 LLAVLEARLAGGpylaGDRFSIADIALAPVLRRLDRLGlDLADYPNLAAWLARLA 188
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 8-72 4.04e-08

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 48.40  E-value: 4.04e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1393763089   8 HCPFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMI---GRKMLPILQKDDGSYLPESLDIVHYVDSI 72
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLDPKDKPPELLalnPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 3-68 1.39e-05

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: 41.57  E-value: 1.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1393763089   3 LYIYDHCPFCVRARMIFGLKKLAVE--QIVLFDddieTPTKMIG---RKMLPILQKDDGSYLPESLDIVHY 68
Cdd:cd03060     3 LYSFRRCPYAMRARMALLLAGITVElrEVELKN----KPAEMLAaspKGTVPVLVLGNGTVIEESLDIMRW 69
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 1-70 4.51e-04

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


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 37.66  E-value: 4.51e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1393763089   1 MKLYIYDHCPFCVRARMIFGLKKLAVEQIVLfddDI-------ETPTKMIGRKMLPILQKDDGSYLPESLDIVHYVD 70
Cdd:cd03051     1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTV---DLaageqrsPEFLAKNPAGTVPVLELDDGTVITESVAICRYLE 74
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 2-45 7.99e-03

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, 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 E. coli GRX1 and GRX3, which are members of this subfamily.


Pssm-ID: 239510 [Multi-domain]  Cd Length: 75  Bit Score: 34.10  E-value: 7.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1393763089   2 KLYIYDHCPFCVRARMIFGLKKLAVEQIVLfDDDIETPTKMIGR 45
Cdd:cd03418     3 EIYTKPNCPYCVRAKALLDKKGVDYEEIDV-DGDPALREEMINR 45
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 10-70 8.43e-03

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: 34.24  E-value: 8.43e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1393763089  10 PFCVRARMIFGLKKLAVEQIVLFDDDIETPTKMIGR---KMLPILQKDDGSYLPESLDIVHYVD 70
Cdd:cd03038    17 PNVWKTRLALNHKGLEYKTVPVEFPDIPPILGELTSggfYTVPVIVDGSGEVIGDSFAIAEYLE 80
 
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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