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Conserved domains on  [gi|495164157|ref|WP_007888955|]
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MULTISPECIES: glutaredoxin 2 [Cronobacter]

Protein Classification

glutaredoxin 2( domain architecture ID 11484691)

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
PRK10387 PRK10387
glutaredoxin 2; Provisional
 1-210 1.31e-145

glutaredoxin 2; Provisional


:

Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 403.88  E-value: 1.31e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMIGQKMAPILQKDDSRYLPESMDIVHYVDNLDGKPLLTG 80
Cdd:PRK10387   1 MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYIDELDGKPLLTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  81 KRNPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQ 160
Cdd:PRK10387  81 KRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHTPGLIKEINADLRALDPLIVK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495164157 161 PNAVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLL 210
Cdd:PRK10387 161 PNAVNGELSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL 210
 
Name Accession Description Interval E-value
PRK10387 PRK10387
glutaredoxin 2; Provisional
 1-210 1.31e-145

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 403.88  E-value: 1.31e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMIGQKMAPILQKDDSRYLPESMDIVHYVDNLDGKPLLTG 80
Cdd:PRK10387   1 MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYIDELDGKPLLTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  81 KRNPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQ 160
Cdd:PRK10387  81 KRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHTPGLIKEINADLRALDPLIVK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495164157 161 PNAVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLL 210
Cdd:PRK10387 161 PNAVNGELSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL 210
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
1-215 2.41e-141

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


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 393.44  E-value: 2.41e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMIGQKMAPILQKDDSRYLPESMDIVHYVDNLDGKPLLTG 80
Cdd:COG2999    1 MKLYIYDHCPFCVRARMIFGLKNIPVELIVLLNDDEETPIRMIGKKMVPILEKDDGSYMPESLDIVHYIDELDGKPILTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  81 KRNPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQ 160
Cdd:COG2999   81 PVRPEIAAWLKKVSSYVNRLLYPRWAKAPLPEFATPSARAYFINKKEASIGDFEELLANTPELIAELNQDLEELEPLIKS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495164157 161 PNAVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLLSKMAI 215
Cdd:COG2999  161 PSAVNGELSLDDIILFPLLRSLTIVKGIQFPPKVRAYRDRMSKKTGVPLLDDVAV 215
GRXB TIGR02182
Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 2-210 1.69e-119

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: 337.90  E-value: 1.69e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157    2 KLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMIGQKMAPILQKDDSRYLPESMDIVHYVDNLDGKPLLTGK 81
Cdd:TIGR02182   1 KLYIYDHCPFCVRARMIFGLKNIPVEKHVLLNDDEETPIRMIGAKQVPILQKDDGRAMPESLDIVAYFDKLDGEPLLTGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   82 RNPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQP 161
Cdd:TIGR02182  81 VSPEIEAWLRKVTGYANKLLLPRFAKSDLPEFATQSARKYFTDKKEASAGNFSALLNHTPGLLEEINADLEELDKLIDGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 495164157  162 NAVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLL 210
Cdd:TIGR02182 161 NAVNGELSEDDILVFPLLRNLTLVAGINWPSRVADYLDNMSKKSKVPLL 209
Glutaredoxin2_C pfam04399
Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of ...
 85-214 6.31e-68

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: 204.35  E-value: 6.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   85 AIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQPNAV 164
Cdd:pfam04399   1 EIAAWLKRVFPYLNRLLLPRFAAAPLPEFATQSAREYFRNKKEASIGSFEELLAKSPELIAQLNADLEALEPLILSSHAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 495164157  165 NGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLLSKMA 214
Cdd:pfam04399  81 NGQLSYDDILLFPILRSLTIVKGLQWPPEVRAYLDRMSAATGVPLLDDIA 130
GST_C_GRX2 cd03199
C-terminal, alpha helical domain of Glutaredoxin 2; Glutathione S-transferase (GST) C-terminal ...
 83-210 1.12e-67

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: 203.55  E-value: 1.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  83 NPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQPN 162
Cdd:cd03199    1 RPEIAAWLKQVGPYYNRLLLPRFAKADLPEFATPSARAYFIRKKEASIGSFEELLAKTPELIAELNADLEALDPLILSSD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495164157 163 AVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLL 210
Cdd:cd03199   81 AVNGELSYDDIILFPLLRNLTIVKGLEFPPKVRAYIDNMSALSDVPLY 128
 
Name Accession Description Interval E-value
PRK10387 PRK10387
glutaredoxin 2; Provisional
 1-210 1.31e-145

glutaredoxin 2; Provisional


Pssm-ID: 236679 [Multi-domain]  Cd Length: 210  Bit Score: 403.88  E-value: 1.31e-145
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMIGQKMAPILQKDDSRYLPESMDIVHYVDNLDGKPLLTG 80
Cdd:PRK10387   1 MKLYIYDHCPFCVKARMIFGLKNIPVELIVLANDDEATPIRMIGQKQVPILQKDDGSYMPESLDIVHYIDELDGKPLLTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  81 KRNPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQ 160
Cdd:PRK10387  81 KRSPAIEEWLRKVFGYLNKLLYPRFAKADLPEFATPSARQYFIDKKEASIGDFDALLAHTPGLIKEINADLRALDPLIVK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495164157 161 PNAVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLL 210
Cdd:PRK10387 161 PNAVNGELSTDDIHLFPILRNLTLVKGIEWPPRVADYRDNMSKKTQVPLL 210
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
1-215 2.41e-141

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


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 393.44  E-value: 2.41e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMIGQKMAPILQKDDSRYLPESMDIVHYVDNLDGKPLLTG 80
Cdd:COG2999    1 MKLYIYDHCPFCVRARMIFGLKNIPVELIVLLNDDEETPIRMIGKKMVPILEKDDGSYMPESLDIVHYIDELDGKPILTG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  81 KRNPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQ 160
Cdd:COG2999   81 PVRPEIAAWLKKVSSYVNRLLYPRWAKAPLPEFATPSARAYFINKKEASIGDFEELLANTPELIAELNQDLEELEPLIKS 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495164157 161 PNAVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLLSKMAI 215
Cdd:COG2999  161 PSAVNGELSLDDIILFPLLRSLTIVKGIQFPPKVRAYRDRMSKKTGVPLLDDVAV 215
GRXB TIGR02182
Glutaredoxin, GrxB family; Glutaredoxins are thioltransferases (disulfide reductases) which ...
 2-210 1.69e-119

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: 337.90  E-value: 1.69e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157    2 KLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMIGQKMAPILQKDDSRYLPESMDIVHYVDNLDGKPLLTGK 81
Cdd:TIGR02182   1 KLYIYDHCPFCVRARMIFGLKNIPVEKHVLLNDDEETPIRMIGAKQVPILQKDDGRAMPESLDIVAYFDKLDGEPLLTGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   82 RNPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQP 161
Cdd:TIGR02182  81 VSPEIEAWLRKVTGYANKLLLPRFAKSDLPEFATQSARKYFTDKKEASAGNFSALLNHTPGLLEEINADLEELDKLIDGP 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 495164157  162 NAVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLL 210
Cdd:TIGR02182 161 NAVNGELSEDDILVFPLLRNLTLVAGINWPSRVADYLDNMSKKSKVPLL 209
Glutaredoxin2_C pfam04399
Glutaredoxin 2, C terminal domain; Glutaredoxins are a multifunctional family of ...
 85-214 6.31e-68

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: 204.35  E-value: 6.31e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   85 AIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQPNAV 164
Cdd:pfam04399   1 EIAAWLKRVFPYLNRLLLPRFAAAPLPEFATQSAREYFRNKKEASIGSFEELLAKSPELIAQLNADLEALEPLILSSHAV 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 495164157  165 NGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLLSKMA 214
Cdd:pfam04399  81 NGQLSYDDILLFPILRSLTIVKGLQWPPEVRAYLDRMSAATGVPLLDDIA 130
GST_C_GRX2 cd03199
C-terminal, alpha helical domain of Glutaredoxin 2; Glutathione S-transferase (GST) C-terminal ...
 83-210 1.12e-67

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: 203.55  E-value: 1.12e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  83 NPAIEEWLRRVNGYVNRLLLPRFAKAPFDEFATPEARRYFTEKKEAAIGSFEEHMSHSAGLIKNISDDLRALDKHIVQPN 162
Cdd:cd03199    1 RPEIAAWLKQVGPYYNRLLLPRFAKADLPEFATPSARAYFIRKKEASIGSFEELLAKTPELIAELNADLEALDPLILSSD 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495164157 163 AVNGELSEDDIHLFPLLRNLTLVAGVNYPTRVADYRDNMAKQTQINLL 210
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 1.23e-41

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: 135.60  E-value: 1.23e-41
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMIGQKMAPILQKDDSRYLPESMDIVHYVD 70
Cdd:cd03037    1 MKLYIYEHCPFCVKARMIAGLKNIPVEQIILQNDDEATPIRMIGAKQVPILEKDDGSFMAESLDIVAFID 70
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 1-70 4.70e-12

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: 59.12  E-value: 4.70e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATP--TRMIGQKMAPILQkDDSRYLPESMDIVHYVD 70
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEefLALNPLGKVPVLE-DGGLVLTESLAILEYLA 71
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-202 3.43e-11

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 59.91  E-value: 3.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEAT---------PTRMIgqkmaPILQkDDSRYLPESMDIVHYVDN 71
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQkspeflalnPLGKV-----PVLV-DDGLVLTESLAILEYLAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  72 LDGKPLLTGKRNPA---IEEWLRRVNGYVNRLLLPRFakapfdefatpeaRRYFTEKKEAAIgsfeehmshsAGLIKNIS 148
Cdd:COG0625   76 RYPEPPLLPADPAArarVRQWLAWADGDLHPALRNLL-------------ERLAPEKDPAAI----------ARARAELA 132

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495164157 149 DDLRALDKHIV-QPNAVNGELSEDDIHLFPLLRNLtLVAGV---NYPtRVADYRDNMA 202
Cdd:COG0625  133 RLLAVLEARLAgGPYLAGDRFSIADIALAPVLRRL-DRLGLdlaDYP-NLAAWLARLA 188
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
3-76 4.16e-09

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 51.46  E-value: 4.16e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495164157    3 LYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATPTRMI-GQKMAPILQkDDSRYLPESMDIVHYVDNLDGKP 76
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKnPLGKVPVLE-DDGGILCESLAIIDYLEELYPGP 74
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 8-72 1.85e-08

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 49.55  E-value: 1.85e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495164157    8 HCPFCLKARMIFGLKNLPVELIVMSNDD--------EATPTRMIgqkmaPILQKDDSRYLPESMDIVHYVDNL 72
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDLDPkdkppellALNPLGTV-----PVLVLPDGTVLTDSLVILEYLEEL 68
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 3-68 8.54e-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: 36.95  E-value: 8.54e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495164157   3 LYIYDHCPFCLKARMIFGLKNLPVEL--IVMSNddeaTPTRMIG---QKMAPILQKDDSRYLPESMDIVHY 68
Cdd:cd03060    3 LYSFRRCPYAMRARMALLLAGITVELreVELKN----KPAEMLAaspKGTVPVLVLGNGTVIEESLDIMRW 69
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
2-55 3.60e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 35.17  E-value: 3.60e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495164157   2 KLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEATpTRMI---GQKMAPILQKDD 55
Cdd:COG0695    3 TLYTTPGCPYCARAKRLLDEKGIPYEEIDVDEDPEAR-EELRersGRRTVPVIFIGG 58
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 85-201 4.61e-03

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: 35.55  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495164157  85 AIEEWLRR-VNGYVNRLLLPRFAKAPFDEFATPEARryftekkeaaigsfeehmshsagliKNISDDLRALDKHIVQPNA 163
Cdd:cd00299    3 ALEDWADAtLAPPLVRLLYLEKVPLPKDEAAVEAAR-------------------------EELPALLAALEQLLAGRPY 57

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 495164157 164 VNGE-LSEDDIHLFPLLRNLTLVAGV-----NYPtRVADYRDNM 201
Cdd:cd00299   58 LAGDqFSLADVALAPVLARLEALGPYydlldEYP-RLKAWYDRL 100
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
 1-68 6.54e-03

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST 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: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 34.63  E-value: 6.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495164157   1 MKLYIYDHCPFCLKARMIFGLKNLPVELIvmsNDDEATPTRMI-----GQKMAPILQKDDSR-YLPESMDIVHY 68
Cdd:cd03041    2 LELYEFEGSPFCRLVREVLTELELDVILY---PCPKGSPKRDKflekgGKVQVPYLVDPNTGvQMFESADIVKY 72
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 2-37 6.81e-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: 34.49  E-value: 6.81e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 495164157   2 KLYIYDHCPFCLKARMIFGLKNLPVELIVMSNDDEA 37
Cdd:cd03418    3 EIYTKPNCPYCVRAKALLDKKGVDYEEIDVDGDPAL 38
 
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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