NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|543735265|ref|XP_005508604|]
View 

glutathione S-transferase omega-1 [Columba livia]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-94 1.29e-57

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: 177.93  E-value: 1.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265   5 HSRSLAKGSAAPGPVPeGLIRLYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKGQLIY 84
Cdd:cd03055    1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                         90
                 ....*....|
gi 543735265  85 ESPITCEYLD 94
Cdd:cd03055   80 ESLIICEYLD 89
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 108-230 8.64e-55

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


:

Pssm-ID: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 171.73  E-value: 8.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 108 YERALQKMLLEHFSKLTSIVFKhvmAVKEGQDTTALKAEIAEKLDKFEEILSKRNTVFYGGDSISMLDYMMWPWFERLEA 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYK---FLRSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 543735265 188 LQLK----DSLSHTPKLQHWMEAMKEDPAVKATMTDPQIYKDYLQLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
 
Name Accession Description Interval E-value
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-94 1.29e-57

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: 177.93  E-value: 1.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265   5 HSRSLAKGSAAPGPVPeGLIRLYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKGQLIY 84
Cdd:cd03055    1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                         90
                 ....*....|
gi 543735265  85 ESPITCEYLD 94
Cdd:cd03055   80 ESLIICEYLD 89
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 108-230 8.64e-55

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


Pssm-ID: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 171.73  E-value: 8.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 108 YERALQKMLLEHFSKLTSIVFKhvmAVKEGQDTTALKAEIAEKLDKFEEILSKRNTVFYGGDSISMLDYMMWPWFERLEA 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYK---FLRSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 543735265 188 LQLK----DSLSHTPKLQHWMEAMKEDPAVKATMTDPQIYKDYLQLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
24-223 3.66e-48

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 157.75  E-value: 3.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVININLK---NKPDWFFEKNPFGLVPVLEtSKGQLIYESPITCEYLDEAFPGK 100
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGKVPVLV-DDGLVLTESLAILEYLAERYPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 101 KLMPSDPYERALQKMLL----EHFSKLTSIVFKHVMAVKEGQDTTALKAEIAEKLDKFEEILSKRNtvFYGGDSISMLDY 176
Cdd:COG0625   81 PLLPADPAARARVRQWLawadGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGP--YLAGDRFSIADI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 543735265 177 MMWPWFERLEALQLkdSLSHTPKLQHWMEAMKEDPAVKATMTDPQIY 223
Cdd:COG0625  159 ALAPVLRRLDRLGL--DLADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 31-96 3.20e-21

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 83.83  E-value: 3.20e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543735265   31 FCPFAQRARLVLRAKGISHEV--ININLKNKPDWFFEKNPFGLVPVLETSKGQLIYESPITCEYLDEA 96
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIelVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68
sspA PRK09481
stringent starvation protein A; Provisional
 26-219 9.21e-15

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 70.51  E-value: 9.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  26 LYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLeTSKGQLIYESPITCEYLDEAFPGKKLMPS 105
Cdd:PRK09481  13 LFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTL-VDRELTLYESRIIMEYLDERFPHPPLMPV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 106 DPYERAlQKMLLEHFSKLTSIVFKHVMAVKEGQDTTALKAEIAEKLDKFEEILSKrnTVFYGGDSISMLDYMMWPWFERL 185
Cdd:PRK09481  92 YPVARG-ESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIAPVFGE--KPYFMSEEFSLVDCYLAPLLWRL 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 543735265 186 EALQLKDSLSHTPKLQHWMEAMKEDPAVKATMTD 219
Cdd:PRK09481 169 PVLGIELSGPGAKELKGYMTRVFERDSFLASLTE 202
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 33-107 2.96e-09

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 55.11  E-value: 2.96e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543735265  33 PFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKGQLIYESPITCEYLDEAFPGKKLMPSDP 107
Cdd:PRK10357  10 PFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALVTEEGECWFDSPIIAEYIELLNVAPAMLPRDP 84
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 142-206 1.31e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 41.92  E-value: 1.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543735265  142 ALKAEIAEKLDKFEEILSKRNTVFygGDSISMLDYMMWPWFERLEALQL-KDSLSHTPKLQHWMEA 206
Cdd:pfam13410   4 RAREQLRAALDALEARLADGPGLL--GDRPTLADIALAPVLARLDAAYPgLDLREGYPRLRAWLER 67
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
24-54 3.41e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 38.26  E-value: 3.41e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVINI 54
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDV 32
 
Name Accession Description Interval E-value
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-94 1.29e-57

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: 177.93  E-value: 1.29e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265   5 HSRSLAKGSAAPGPVPeGLIRLYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKGQLIY 84
Cdd:cd03055    1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                         90
                 ....*....|
gi 543735265  85 ESPITCEYLD 94
Cdd:cd03055   80 ESLIICEYLD 89
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 108-230 8.64e-55

C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases.


Pssm-ID: 198293 [Multi-domain]  Cd Length: 124  Bit Score: 171.73  E-value: 8.64e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 108 YERALQKMLLEHFSKLTSIVFKhvmAVKEGQDTTALKAEIAEKLDKFEEILSKRNTVFYGGDSISMLDYMMWPWFERLEA 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYK---FLRSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 543735265 188 LQLK----DSLSHTPKLQHWMEAMKEDPAVKATMTDPQIYKDYLQLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
24-223 3.66e-48

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 157.75  E-value: 3.66e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVININLK---NKPDWFFEKNPFGLVPVLEtSKGQLIYESPITCEYLDEAFPGK 100
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGKVPVLV-DDGLVLTESLAILEYLAERYPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 101 KLMPSDPYERALQKMLL----EHFSKLTSIVFKHVMAVKEGQDTTALKAEIAEKLDKFEEILSKRNtvFYGGDSISMLDY 176
Cdd:COG0625   81 PLLPADPAARARVRQWLawadGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEARLAGGP--YLAGDRFSIADI 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 543735265 177 MMWPWFERLEALQLkdSLSHTPKLQHWMEAMKEDPAVKATMTDPQIY 223
Cdd:COG0625  159 ALAPVLRRLDRLGL--DLADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 31-96 3.20e-21

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 83.83  E-value: 3.20e-21
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 543735265   31 FCPFAQRARLVLRAKGISHEV--ININLKNKPDWFFEKNPFGLVPVLETSKGQLIYESPITCEYLDEA 96
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIelVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
26-101 8.75e-21

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 83.05  E-value: 8.75e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543735265   26 LYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSkGQLIYESPITCEYLDEAFPGKK 101
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDD-GGILCESLAIIDYLEELYPGPP 75
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 24-94 2.90e-19

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: 78.77  E-value: 2.90e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVININLKNKP-DWFFEKNPFGLVPVLETSkGQLIYESPITCEYLD 94
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEqEEFLALNPLGKVPVLEDG-GLVLTESLAILEYLA 71
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 26-97 1.95e-15

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: 68.89  E-value: 1.95e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543735265  26 LYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLeTSKGQLIYESPITCEYLDEAF 97
Cdd:cd03059    3 LYSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYGTVPTL-VDRDLVLYESRIIMEYLDERF 73
sspA PRK09481
stringent starvation protein A; Provisional
 26-219 9.21e-15

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 70.51  E-value: 9.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  26 LYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLeTSKGQLIYESPITCEYLDEAFPGKKLMPS 105
Cdd:PRK09481  13 LFSGPTDIYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTL-VDRELTLYESRIIMEYLDERFPHPPLMPV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 106 DPYERAlQKMLLEHFSKLTSIVFKHVMAVKEGQDTTALKAEIAEKLDKFEEILSKrnTVFYGGDSISMLDYMMWPWFERL 185
Cdd:PRK09481  92 YPVARG-ESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIAPVFGE--KPYFMSEEFSLVDCYLAPLLWRL 168

                        170       180       190
                 ....*....|....*....|....*....|....
gi 543735265 186 EALQLKDSLSHTPKLQHWMEAMKEDPAVKATMTD 219
Cdd:PRK09481 169 PVLGIELSGPGAKELKGYMTRVFERDSFLASLTE 202
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 26-86 1.04e-13

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: 64.30  E-value: 1.04e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543735265  26 LYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKGQLIYES 86
Cdd:cd03060    3 LYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASPKGTVPVLVLGNGTVIEES 63
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 24-95 5.81e-13

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: 62.32  E-value: 5.81e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543735265   24 IRLYSMRFCPFAQRARLVLRAKGISHEVININLK---NKPDWFFEKNPFGLVPVLETsKGQLIYESPITCEYLDE 95
Cdd:pfam02798   3 LTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPLGKVPALED-GGKKLTESRAILEYIAR 76
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 24-95 5.85e-13

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: 62.28  E-value: 5.85e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVININLK---NKPDWFFEKNPFGLVPVLETSkGQLIYESPITCEYLDE 95
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNPFGQIPALEDG-DLKLFESRAITRYLAE 75
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 25-94 6.41e-13

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: 61.93  E-value: 6.41e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543735265  25 RLYSMRFCPFAQRARLVLRAKGISHEVININL---KNKPDWFFEKNPFGLVPVLETSKGQLIYESPITCEYLD 94
Cdd:cd03051    2 KLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLaagEQRSPEFLAKNPAGTVPVLELDDGTVITESVAICRYLE 74
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 32-199 2.02e-12

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 65.01  E-value: 2.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  32 CPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKgQLIYESPITCEYLDEAFPGKKLmpSDPYERA 111
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDE-KWVADSDVITQALEEKYPDPPL--ATPPEKA 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 112 LQKmllehfSKLTSiVFKHVMAVKEGQDTTalKAEIAEKLDKFEEILsKRNTVFYGGDSISMLDYMMWPWFERLE-AL-- 188
Cdd:PLN02817 150 SVG------SKIFS-TFIGFLKSKDPGDGT--EQALLDELTSFDDYI-KENGPFINGEKISAADLSLGPKLYHLEiALgh 219

                        170
                 ....*....|....*
gi 543735265 189 ----QLKDSLSHTPK 199
Cdd:PLN02817 220 yknwSVPDSLPFVKS 234
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 24-97 3.78e-10

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: 54.59  E-value: 3.78e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNP-FGLVPVLeTSKGQLIYESPITCEYLDEAF 97
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPvHKKIPVL-LHNGKPICESLIIVEYIDEAW 74
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 107-230 5.06e-10

C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The plant-specific class Tau GST subfamily has undergone extensive gene duplication. The Arabidopsis and Oryza genomes contain 28 and 40 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Phi GSTs, showing class specificity in substrate preference. Tau enzymes are highly efficient in detoxifying diphenylether and aryloxyphenoxypropionate herbicides. In addition, Tau GSTs play important roles in intracellular signalling, biosynthesis of anthocyanin, responses to soil stresses and responses to auxin and cytokinin hormones.


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 55.65  E-value: 5.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 107 PYERALQ----KMLLEHFSKLTSIVFKhvmavKEGQDTTALKAEIAEKLDKFEEILsKRNTVFYGGDSISMLD---YMMW 179
Cdd:cd03185    1 PYERAQArfwaAYIDDKLFPAGRKVWA-----AKGEEQEKAVEEALEALKVLEEEL-KGGKPFFGGDTIGYLDialGSFL 74

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 543735265 180 PWFERLEAL---QLKDSlSHTPKLQHWMEAMKEDPAVKATMTDPQIYKDYLQLY 230
Cdd:cd03185   75 GWFKAIEEVggvKLLDE-EKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127
PLN02378 PLN02378
glutathione S-transferase DHAR1
 32-186 2.22e-09

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 55.87  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  32 CPFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKgQLIYESPITCEYLDEAFPGKKLmpSDPYEra 111
Cdd:PLN02378  20 CPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDD-KWVTDSDVIVGILEEKYPDPPL--KTPAE-- 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543735265 112 lqkmllehFSKLTSIVFKHVMAVKEGQDTT-ALKAEIAEKLDKFEEILSKRNTVFYGGDSISMLDYMMWPWFERLE 186
Cdd:PLN02378  95 --------FASVGSNIFGTFGTFLKSKDSNdGSEHALLVELEALENHLKSHDGPFIAGERVSAVDLSLAPKLYHLQ 162
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 33-107 2.96e-09

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 55.11  E-value: 2.96e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 543735265  33 PFAQRARLVLRAKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKGQLIYESPITCEYLDEAFPGKKLMPSDP 107
Cdd:PRK10357  10 PFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALVTEEGECWFDSPIIAEYIELLNVAPAMLPRDP 84
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 110-207 6.58e-09

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: 52.12  E-value: 6.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 110 RALQKMLLEHFSK-LTSIVFKHVM-AVKEGQDTTALKAEIAEKLDKFEEILSKRNtvFYGGDSISMLDYMMWPWFERLEA 187
Cdd:cd00299    2 RALEDWADATLAPpLVRLLYLEKVpLPKDEAAVEAAREELPALLAALEQLLAGRP--YLAGDQFSLADVALAPVLARLEA 79

                         90       100
                 ....*....|....*....|.
gi 543735265 188 LQLK-DSLSHTPKLQHWMEAM 207
Cdd:cd00299   80 LGPYyDLLDEYPRLKAWYDRL 100
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 33-94 1.66e-08

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: 49.95  E-value: 1.66e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543735265  33 PFAQRARLVLR--AKGISHEVININLKNKPDWFFEKNPFGLVPVLETSKGQLIYESPITCEYLD 94
Cdd:cd03049   10 PYVRKVRVAAHetGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYLD 73
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 37-94 7.18e-07

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: 45.64  E-value: 7.18e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 543735265  37 RARLVLRAKGISHEVININL----KNKPDwFFEKNPFGLVPVLETSkGQLIYESPITCEYLD 94
Cdd:cd03042   14 RVRIALNLKGLDYEYVPVNLlkgeQLSPA-YRALNPQGLVPTLVID-GLVLTQSLAIIEYLD 73
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 24-93 7.30e-07

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: 45.64  E-value: 7.30e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVININLKN---KPDWFFEKNPFGLVPVLETSkGQLIYESPITCEYL 93
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKgetRTPEFLALNPNGEVPVLELD-GRVLAESNAILVYL 72
PLN02473 PLN02473
glutathione S-transferase
 32-217 2.07e-06

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 47.29  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  32 CPfaQRARLVLRAKGISHEVININL----KNKPDWFFeKNPFGLVPVLETSKGQLiYESPITCEYLDEAFP--GKKLMPS 105
Cdd:PLN02473  13 NP--QRVLLCFLEKGIEFEVIHVDLdkleQKKPEHLL-RQPFGQVPAIEDGDLKL-FESRAIARYYATKYAdqGTDLLGK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 106 DPYERALQKMLLE----HFSKLT-SIVFKHVMAVKEGQDT-TALKAEIAEKLDKFEEILSKR--NTVFYGGDSISMLDYM 177
Cdd:PLN02473  89 TLEHRAIVDQWVEvennYFYAVAlPLVINLVFKPRLGEPCdVALVEELKVKFDKVLDVYENRlaTNRYLGGDEFTLADLT 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 543735265 178 MWPWFERLEAL-QLKDSLSHTPKLQHWMEAMKEDPAVKATM 217
Cdd:PLN02473 169 HMPGMRYIMNEtSLSGLVTSRENLNRWWNEISARPAWKKLM 209
PRK15113 PRK15113
glutathione transferase;
24-116 2.65e-06

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 46.88  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  24 IRLYS--MRFCPFAQRARLVLRAKGISHEVININLKNK----PDWFfEKNPFGLVPVLETSKGQLiYESPITCEYLDEAF 97
Cdd:PRK15113   6 ITLYSdaHFFSPYVMSAFVALQEKGLPFELKTVDLDAGehlqPTYQ-GYSLTRRVPTLQHDDFEL-SESSAIAEYLEERF 83

                         90       100
                 ....*....|....*....|..
gi 543735265  98 PG---KKLMPSDPYERALQKML 116
Cdd:PRK15113  84 APpawERIYPADLQARARARQI 105
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 32-98 9.53e-06

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: 42.52  E-value: 9.53e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543735265  32 CPFAqrARLVLRAKGISHEVININLKNK----PDwFFEKNPFGLVPVLETSKGQLIYESPITCEYLDEAFP 98
Cdd:cd03057   10 CSLA--PHIALEELGLPFELVRVDLRTKtqkgAD-YLAINPKGQVPALVLDDGEVLTESAAILQYLADLHP 77
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
 155-215 1.14e-05

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related 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 active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 43.03  E-value: 1.14e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543735265 155 EEILSKRNtvFYGGDSISMLDYMMWPWFERLEALQLkdSLSHTPKLQHWMEAMKEDPAVKA 215
Cdd:cd10291   53 DRRLAKSK--YLAGDEYSIADIAIWPWVARHEWQGI--DLADFPNLKRWFERLAARPAVQK 109
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 142-206 1.31e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 41.92  E-value: 1.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 543735265  142 ALKAEIAEKLDKFEEILSKRNTVFygGDSISMLDYMMWPWFERLEALQL-KDSLSHTPKLQHWMEA 206
Cdd:pfam13410   4 RAREQLRAALDALEARLADGPGLL--GDRPTLADIALAPVLARLDAAYPgLDLREGYPRLRAWLER 67
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 142-217 3.53e-05

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 41.85  E-value: 3.53e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 543735265 142 ALKAEIAEKLDKFEEILSKRNtvFYGGDSISMLD---YMMWPWferLEALQLkdSLSHTPKLQHWMEAMKEDPAVKATM 217
Cdd:cd03188   42 AARERLERRLAYLDAQLAGGP--YLLGDQFSVADaylFVVLRW---ARAVGL--DLSDWPHLAAYLARVAARPAVQAAL 113
PLN02395 PLN02395
glutathione S-transferase
 35-187 4.09e-05

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 43.31  E-value: 4.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  35 AQRARLVLRAKGISHEVININL---KNKPDWFFEKNPFGLVPVLETSKGQLiYESPITCEYLDEAF--PGKKLMPSDPYE 109
Cdd:PLN02395  13 PKRALVTLIEKGVEFETVPVDLmkgEHKQPEYLALQPFGVVPVIVDGDYKI-FESRAIMRYYAEKYrsQGPDLLGKTIEE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 110 RALQKMLLE--------HFSKLT-SIVFKHVMA-------VKEGQDttalkaEIAEKLDKFEEILSKRNtvFYGGDSISM 173
Cdd:PLN02395  92 RGQVEQWLDveatsyhpPLLNLTlHILFASKMGfpadekvIKESEE------KLAKVLDVYEARLSKSK--YLAGDFVSL 163

                        170
                 ....*....|....
gi 543735265 174 LDYMMWPWFERLEA 187
Cdd:PLN02395 164 ADLAHLPFTEYLVG 177
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 135-215 4.82e-05

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 41.39  E-value: 4.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  135 KEGQDTTALKAEIAEK-----LDKFEEILSKRNTVFYGGDSISMLDYMMWPWFERLEALQLKDSLSHTPKLQHWMEAMKE 209
Cdd:pfam14497  14 EDEKKKAKRRKEFREErlpkfLGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPDALDKYPKLKALHERVAA 93


                  ....*.
gi 543735265  210 DPAVKA 215
Cdd:pfam14497  94 RPNIKA 99
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 24-93 7.30e-05

GST_N family, Class Delta and Epsilon 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. 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. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.


Pssm-ID: 239343 [Multi-domain]  Cd Length: 74  Bit Score: 39.90  E-value: 7.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVININLKN----KPDwFFEKNPFGLVPVLETSkGQLIYESPITCEYL 93
Cdd:cd03045    1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKgehlKPE-FLKLNPQHTVPTLVDN-GFVLWESHAILIYL 72
GST_C_Phi cd03187
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione ...
 109-217 1.32e-04

C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau 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: 198296 [Multi-domain]  Cd Length: 118  Bit Score: 40.29  E-value: 1.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 109 ERALQKMLLE----HFSKLTS-IVFKHVMAVKEGQDT-TALKAEIAEKLDK----FEEILSKrnTVFYGGDSISMLDYMM 178
Cdd:cd03187    2 ERALVEQWLEveahQFDPPASkLVFELVFKPMLGLKTdEAVVEENEAKLKKvldvYEARLSK--SKYLAGDSFTLADLSH 79

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 543735265 179 WPWFERLEALQLKDSLSHTPKLQHWMEAMKEDPAVKATM 217
Cdd:cd03187   80 LPNLHYLMATPSKKLFDSRPHVKAWWEDISARPAWKKVL 118
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 35-98 2.51e-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: 38.64  E-value: 2.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 543735265  35 AQRARLVLRAKGISHEVININLKN---KPDWFFEKNPFGLVPVLETSkGQLIYESPITCEYLDEAFP 98
Cdd:cd03046   11 SFRILWLLEELGLPYELVLYDRGPgeqAPPEYLAINPLGKVPVLVDG-DLVLTESAAIILYLAEKYG 76
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
24-54 3.41e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 38.26  E-value: 3.41e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVINI 54
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDV 32
GST_C_Pi cd03210
C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione ...
 146-215 3.88e-04

C-terminal, alpha helical domain of Class Pi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Pi 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 Pi GST is a homodimeric eukaryotic protein. The human GSTP1 is mainly found in erythrocytes, kidney, placenta and fetal liver. It is involved in stress responses and in cellular proliferation pathways as an inhibitor of JNK (c-Jun N-terminal kinase). Following oxidative stress, monomeric GSTP1 dissociates from JNK and dimerizes, losing its ability to bind JNK and causing an increase in JNK activity, thereby promoting apoptosis. GSTP1 is expressed in various tumors and is the predominant GST in a wide range of cancer cells. It has been implicated in the development of multidrug-resistant tumors.


Pssm-ID: 198319 [Multi-domain]  Cd Length: 126  Bit Score: 39.22  E-value: 3.88e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 543735265 146 EIAEKLDKFEEILSKRN-TVFYGGDSISMLDYMMwpwFERLEALQLKD--SLSHTPKLQHWMEAMKEDPAVKA 215
Cdd:cd03210   39 DLPEQLKPFEKLLAKNNgKGFIVGDKISFADYNL---FDLLDIHLVLApgCLDAFPLLKAFVERLSARPKLKA 108
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 24-98 9.71e-04

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: 37.33  E-value: 9.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  24 IRLYSMR-------FCPFAQRARLVLRAKGISHEVININLKNKPDWFFE--KNPFGLVPVLETSKGQLIYESPITCEYLD 94
Cdd:cd03038    1 ITLYDLAgkdpvraFSPNVWKTRLALNHKGLEYKTVPVEFPDIPPILGEltSGGFYTVPVIVDGSGEVIGDSFAIAEYLE 80


                 ....
gi 543735265  95 EAFP 98
Cdd:cd03038   81 EAYP 84
GST_N_GRX2 cd03037
GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. ...
 25-95 9.81e-04

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: 36.60  E-value: 9.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 543735265  25 RLYSMRFCPFAQRARLVLRAKGISHEVInINLKNKPDWFFEKNPFGLVPVLETSKGQLIYESPITCEYLDE 95
Cdd:cd03037    2 KLYIYEHCPFCVKARMIAGLKNIPVEQI-ILQNDDEATPIRMIGAKQVPILEKDDGSFMAESLDIVAFIDE 71
Glutaredoxin pfam00462
Glutaredoxin;
24-54 1.13e-03

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 36.33  E-value: 1.13e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 543735265   24 IRLYSMRFCPFAQRARLVLRAKGISHEVINI 54
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDV 31
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 142-211 1.84e-03

Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety of targets including S-crystallin from squid, the eukaryotic elongation factor 1-gamma, the HSP26 family of stress-related proteins and auxin-regulated proteins in plants. Stringent starvation proteins in E. coli are also included in the alignment but are not known to have GST activity. The glutathione molecule binds in a cleft between N and C-terminal domains. The catalytically important residues are proposed to reside in the N-terminal domain. In plants, GSTs are encoded by a large gene family (48 GST genes in Arabidopsis) and can be divided into the phi, tau, theta, zeta, and lambda classes.


Pssm-ID: 459647 [Multi-domain]  Cd Length: 93  Bit Score: 36.49  E-value: 1.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  142 ALKAEIAEKLDKFEEILSKRntVFYGGDSISMLDYMMWPWFERLEALQLKDSLSHTPKLQHWMEAMKEDP 211
Cdd:pfam00043  26 EALEKVARVLSALEEVLKGQ--TYLVGDKLTLADIALAPALLWLYELDPACLREKFPNLKAWFERVAARP 93
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 24-55 2.69e-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: 2.69e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVININ 55
Cdd:cd02066    2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDIL 33
GST_C_YghU_like cd10292
C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and ...
 146-214 3.56e-03

C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU and related 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 active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU does not contain a redox active cysteine residue, and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YghU reveals two GSH molecules bound in its active site.


Pssm-ID: 198325 [Multi-domain]  Cd Length: 118  Bit Score: 36.29  E-value: 3.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 543735265 146 EIAEKLDKFEEILSkrNTVFYGGDSISMLDYMMWPWFERLEALQLKD-----SLSHTPKLQHWMEAMKEDPAVK 214
Cdd:cd10292   44 EAKRQLDVLDRQLA--THKYLAGDEYTIADMAIWPWYGGLALGSLYDaaeflDVDEYKHVQRWAKDIAARPAVK 115
GRX_GRXb_1_3_like cd03418
Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of ...
 24-54 3.80e-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: 35.26  E-value: 3.80e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 543735265  24 IRLYSMRFCPFAQRARLVLRAKGISHEVINI 54
Cdd:cd03418    2 VEIYTKPNCPYCVRAKALLDKKGVDYEEIDV 32
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 26-93 5.34e-03

GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression.


Pssm-ID: 239342 [Multi-domain]  Cd Length: 75  Bit Score: 34.92  E-value: 5.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  26 LYSMRFCPFAQRARLVLRAKGISHEVINI--NLKNKPDWFFEKNPFGLVPVLETSKGQLIYESPITCEYL 93
Cdd:cd03044    3 LYTYPGNPRSLKILAAAKYNGLDVEIVDFqpGKENKTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYV 72
GST_N_CLIC cd03061
GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, ...
 32-73 7.38e-03

GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, parchorin and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division and apoptosis. They can exist in both water-soluble and membrane-bound states, and are found in various vesicles and membranes. Biochemical studies of the C. elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. The structure of soluble human CLIC1 reveals that it is monomeric and it adopts a fold similar to GSTs, containing an N-terminal domain with a TRX fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved.


Pssm-ID: 239359  Cd Length: 91  Bit Score: 34.66  E-value: 7.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 543735265  32 CPFAQRARLVLRAKGISHEVININLKNKPDwFFEKNPFGLVP 73
Cdd:cd03061   22 CPFCQRLFMVLWLKGVVFNVTTVDMKRKPE-DLKDLAPGTQP 62
GrxB COG2999
Glutaredoxin 2 [Posttranslational modification, protein turnover, chaperones];
25-209 7.90e-03

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


Pssm-ID: 442237 [Multi-domain]  Cd Length: 215  Bit Score: 36.36  E-value: 7.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265  25 RLYSMRFCPFAQRARLVLRAKGISHEVinINLKNKpDwffEKNPFGL-----VPVLETSKGQLIYESPITCEYLDEAFpG 99
Cdd:COG2999    2 KLYIYDHCPFCVRARMIFGLKNIPVEL--IVLLND-D---EETPIRMigkkmVPILEKDDGSYMPESLDIVHYIDELD-G 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 100 KKLMPSDPYERalqkmLLEHFSKLTSIVFKHVM---------------AV------KEGQ---------DTTALKAEIAE 149
Cdd:COG2999   75 KPILTGPVRPE-----IAAWLKKVSSYVNRLLYprwakaplpefatpsARayfinkKEASigdfeellaNTPELIAELNQ 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 543735265 150 KLDKFEEILSKRNTVfygGDSISMLDYMMWPwfeRLEALQLKDSLSHTPKLQHWMEAMKE 209
Cdd:COG2999  150 DLEELEPLIKSPSAV---NGELSLDDIILFP---LLRSLTIVKGIQFPPKVRAYRDRMSK 203
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH