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Conserved domains on  [gi|300360532|ref|NP_001177931|]
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glutathione S-transferase omega-1 isoform 2 [Homo sapiens]

Protein Classification

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 5-94 1.09e-56

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: 174.08  E-value: 1.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532   5 SARSLGKGSAPPGPVPeGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIY 84
Cdd:cd03055    1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                         90
                 ....*....|
gi 300360532  85 ESAITCEYLD 94
Cdd:cd03055   80 ESLIICEYLD 89
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 84-196 7.03e-47

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: 150.55  E-value: 7.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  84 YESAITCEYLDEAYPGKKLLP----DDPYEKACQKMILELFSKVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLN-- 157
Cdd:cd03184    4 AQQKMLIERFSKVPSAFYKFLrsgeDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEALKLLdg 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 300360532 158 --ECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELY 196
Cdd:cd03184   84 yeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 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 1.09e-56

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: 174.08  E-value: 1.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532   5 SARSLGKGSAPPGPVPeGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIY 84
Cdd:cd03055    1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                         90
                 ....*....|
gi 300360532  85 ESAITCEYLD 94
Cdd:cd03055   80 ESLIICEYLD 89
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 84-196 7.03e-47

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: 150.55  E-value: 7.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  84 YESAITCEYLDEAYPGKKLLP----DDPYEKACQKMILELFSKVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLN-- 157
Cdd:cd03184    4 AQQKMLIERFSKVPSAFYKFLrsgeDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEALKLLdg 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 300360532 158 --ECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELY 196
Cdd:cd03184   84 yeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
24-189 1.28e-34

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 121.54  E-value: 1.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  24 IRIYSMRFCPFAERTRLVLKAKGIRHEVININLK---NKPEWFFKKNPFGLVPVLENsQGQLIYESAITCEYLDEAYPGK 100
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGKVPVLVD-DGLVLTESLAILEYLAERYPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532 101 KLLPDDPYEKA------------CQKMILELFSKVLTNK------------------------KTTFFGGNSISMIDYLI 144
Cdd:COG0625   81 PLLPADPAARArvrqwlawadgdLHPALRNLLERLAPEKdpaaiararaelarllavlearlaGGPYLAGDRFSIADIAL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 300360532 145 WPWFERLEAMKLNecVDHTPKLKLWMAAMKEDPTVSALLTSEKDW 189
Cdd:COG0625  161 APVLRRLDRLGLD--LADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 31-96 1.64e-20

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 81.14  E-value: 1.64e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300360532   31 FCPFAERTRLVLKAKGIRHEV--ININLKNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEA 96
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIelVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 37-116 4.76e-12

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


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 62.34  E-value: 4.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532   37 RTRLVLKAKGIRHEVININLKNKPEWF---FKK-NPFGLVPVLENSqGQLIYESAITCEYLDEAYPGKKLLPDDPYEKAC 112
Cdd:TIGR01262  13 RVRIALALKGIDYEYVPVNLLRDGEQRspeFLAlNPQGLVPTLDID-GEVLTQSLAIIEYLEETYPDPPLLPADPIKRAR 91


                  ....
gi 300360532  113 QKMI 116
Cdd:TIGR01262  92 VRAL 95
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 32-111 4.06e-11

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 60.39  E-value: 4.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  32 CPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQgQLIYESAITCEYLDEAYPGKKLlpDDPYEKA 111
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDE-KWVADSDVITQALEEKYPDPPL--ATPPEKA 149
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 117-186 1.97e-06

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 44.85  E-value: 1.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  117 LELFSKVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSE 186
Cdd:pfam14497  35 LGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPDALDKYPKLKALHERVAARPNIKAYLASR 104
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
24-54 5.21e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.48  E-value: 5.21e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 300360532  24 IRIYSMRFCPFAERTRLVLKAKGIRHEVINI 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 1.09e-56

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: 174.08  E-value: 1.09e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532   5 SARSLGKGSAPPGPVPeGSIRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIY 84
Cdd:cd03055    1 SSKHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVY 79

                         90
                 ....*....|
gi 300360532  85 ESAITCEYLD 94
Cdd:cd03055   80 ESLIICEYLD 89
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 84-196 7.03e-47

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: 150.55  E-value: 7.03e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  84 YESAITCEYLDEAYPGKKLLP----DDPYEKACQKMILELFSKVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLN-- 157
Cdd:cd03184    4 AQQKMLIERFSKVPSAFYKFLrsgeDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEALKLLdg 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 300360532 158 --ECVDHTPKLKLWMAAMKEDPTVSALLTSEKDWQGFLELY 196
Cdd:cd03184   84 yeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
24-189 1.28e-34

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 121.54  E-value: 1.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  24 IRIYSMRFCPFAERTRLVLKAKGIRHEVININLK---NKPEWFFKKNPFGLVPVLENsQGQLIYESAITCEYLDEAYPGK 100
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGKVPVLVD-DGLVLTESLAILEYLAERYPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532 101 KLLPDDPYEKA------------CQKMILELFSKVLTNK------------------------KTTFFGGNSISMIDYLI 144
Cdd:COG0625   81 PLLPADPAARArvrqwlawadgdLHPALRNLLERLAPEKdpaaiararaelarllavlearlaGGPYLAGDRFSIADIAL 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 300360532 145 WPWFERLEAMKLNecVDHTPKLKLWMAAMKEDPTVSALLTSEKDW 189
Cdd:COG0625  161 APVLRRLDRLGLD--LADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 31-96 1.64e-20

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 81.14  E-value: 1.64e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300360532   31 FCPFAERTRLVLKAKGIRHEV--ININLKNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEA 96
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIelVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
27-101 2.60e-19

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 78.04  E-value: 2.60e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300360532   27 YSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENsQGQLIYESAITCEYLDEAYPGKK 101
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLED-DGGILCESLAIIDYLEELYPGPP 75
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 24-94 1.61e-18

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: 76.07  E-value: 1.61e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300360532  24 IRIYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKK-NPFGLVPVLENSqGQLIYESAITCEYLD 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) ...
 27-97 3.18e-14

GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP)-associated protein required for the lytic development of phage P1 and for stationary phase-induced acid tolerance of E. coli. It is implicated in survival during nutrient starvation. SspA adopts the GST fold with an N-terminal TRX-fold domain and a C-terminal alpha helical domain, but it does not bind glutathione (GSH) and lacks GST activity. SspA is highly conserved among gram-negative bacteria. Related proteins found in Neisseria (called RegF), Francisella and Vibrio regulate the expression of virulence factors necessary for pathogenesis.


Pssm-ID: 239357 [Multi-domain]  Cd Length: 73  Bit Score: 65.04  E-value: 3.18e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300360532  27 YSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLiYESAITCEYLDEAY 97
Cdd:cd03059    4 YSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYGTVPTLVDRDLVL-YESRIIMEYLDERF 73
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 23-95 3.79e-14

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: 64.63  E-value: 3.79e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300360532   23 SIRIYSMRFCPFAERTRLVLKAKGIRHEVININLK---NKPEWFFKKNPFGLVPVLENsQGQLIYESAITCEYLDE 95
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPLGKVPALED-GGKKLTESRAILEYIAR 76
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 24-95 5.23e-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: 61.90  E-value: 5.23e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300360532  24 IRIYSMRFCPFAERTRLVLKAKGIRHEVININLK---NKPEWFFKKNPFGLVPVLENSqGQLIYESAITCEYLDE 95
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNPFGQIPALEDG-DLKLFESRAITRYLAE 75
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 37-116 4.76e-12

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


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 62.34  E-value: 4.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532   37 RTRLVLKAKGIRHEVININLKNKPEWF---FKK-NPFGLVPVLENSqGQLIYESAITCEYLDEAYPGKKLLPDDPYEKAC 112
Cdd:TIGR01262  13 RVRIALALKGIDYEYVPVNLLRDGEQRspeFLAlNPQGLVPTLDID-GEVLTQSLAIIEYLEETYPDPPLLPADPIKRAR 91


                  ....
gi 300360532  113 QKMI 116
Cdd:TIGR01262  92 VRAL 95
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 32-111 4.06e-11

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 60.39  E-value: 4.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  32 CPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQgQLIYESAITCEYLDEAYPGKKLlpDDPYEKA 111
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDE-KWVADSDVITQALEEKYPDPPL--ATPPEKA 149
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 25-94 5.65e-11

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: 56.15  E-value: 5.65e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300360532  25 RIYSMRFCPFAERTRLVLKAKGIRHEVININL---KNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLD 94
Cdd:cd03051    2 KLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLaagEQRSPEFLAKNPAGTVPVLELDDGTVITESVAICRYLE 74
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 26-86 8.39e-11

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: 55.83  E-value: 8.39e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300360532  26 IYSMRFCPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIYES 86
Cdd:cd03060    3 LYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASPKGTVPVLVLGNGTVIEES 63
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 33-97 1.11e-09

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: 52.67  E-value: 1.11e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300360532  33 PFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNP-FGLVPVLENSqGQLIYESAITCEYLDEAY 97
Cdd:cd03058   10 PFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPvHKKIPVLLHN-GKPICESLIIVEYIDEAW 74
sspA PRK09481
stringent starvation protein A; Provisional
 34-104 2.68e-09

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 54.72  E-value: 2.68e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300360532  34 FAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLiYESAITCEYLDEAYPGKKLLP 104
Cdd:PRK09481  21 YSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTLVDRELTL-YESRIIMEYLDERFPHPPLMP 90
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 33-94 3.53e-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: 48.80  E-value: 3.53e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300360532  33 PFAERTRLVL--KAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLD 94
Cdd:cd03049   10 PYVRKVRVAAheTGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYLD 73
PLN02378 PLN02378
glutathione S-transferase DHAR1
 32-102 3.01e-07

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 48.94  E-value: 3.01e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300360532  32 CPFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQgQLIYESAITCEYLDEAYPGKKL 102
Cdd:PLN02378  20 CPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDD-KWVTDSDVIVGILEEKYPDPPL 89
PRK10357 PRK10357
putative glutathione S-transferase; Provisional
 33-107 4.26e-07

putative glutathione S-transferase; Provisional


Pssm-ID: 182405 [Multi-domain]  Cd Length: 202  Bit Score: 48.56  E-value: 4.26e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300360532  33 PFAERTRLVLKAKGIRHEVININLKNKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYPGKKLLPDDP 107
Cdd:PRK10357  10 PFVRKISILLLEKGITFEFVNELPYNADNGVAQYNPLGKVPALVTEEGECWFDSPIIAEYIELLNVAPAMLPRDP 84
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 116-173 7.89e-07

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: 45.95  E-value: 7.89e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 300360532 116 ILELFSKVLtnKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECV-DHTPKLKLWMAAM 173
Cdd:cd00299   44 LLAALEQLL--AGRPYLAGDQFSLADVALAPVLARLEALGPYYDLlDEYPRLKAWYDRL 100
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 117-186 1.97e-06

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 44.85  E-value: 1.97e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  117 LELFSKVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTPKLKLWMAAMKEDPTVSALLTSE 186
Cdd:pfam14497  35 LGYFEKVLNKNGGGYLVGDKLTYADLALFQVLDGLLYPKAPDALDKYPKLKALHERVAARPNIKAYLASR 104
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 24-93 1.99e-06

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: 44.10  E-value: 1.99e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300360532  24 IRIYSMRFCPFAERTRLVLKAKGIRHEVININLKN---KPEWFFKKNPFGLVPVLENSqGQLIYESAITCEYL 93
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKgetRTPEFLALNPNGEVPVLELD-GRVLAESNAILVYL 72
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 37-94 4.53e-06

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: 42.94  E-value: 4.53e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300360532  37 RTRLVLKAKGIRHEVININL----KNKPEwFFKKNPFGLVPVLENSqGQLIYES-AItCEYLD 94
Cdd:cd03042   14 RVRIALNLKGLDYEYVPVNLlkgeQLSPA-YRALNPQGLVPTLVID-GLVLTQSlAI-IEYLD 73
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 35-98 7.10e-06

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: 42.49  E-value: 7.10e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300360532  35 AERTRLVLKAKGIRHEVININLKN---KPEWFFKKNPFGLVPVLENsQGQLIYESAITCEYLDEAYP 98
Cdd:cd03046   11 SFRILWLLEELGLPYELVLYDRGPgeqAPPEYLAINPLGKVPVLVD-GDLVLTESAAIILYLAEKYG 76
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 24-93 2.95e-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: 40.67  E-value: 2.95e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300360532  24 IRIYSMRFCPFAERTRLVLKAKGIRHEVININLKN----KPEwFFKKNPFGLVPVLENSqGQLIYESAITCEYL 93
Cdd:cd03045    1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKgehlKPE-FLKLNPQHTVPTLVDN-GFVLWESHAILIYL 72
GST_N_Sigma_like cd03039
GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, ...
 35-93 4.21e-05

GST_N family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation and mediation of allergy and inflammation. Other class Sigma members include the class II insect GSTs, S-crystallins from cephalopods and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase and PGD2 synthase activities, and may play an important role in host-parasite interactions. Also members are novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 239337 [Multi-domain]  Cd Length: 72  Bit Score: 40.22  E-value: 4.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  35 AERTRLVLKAKGIRHEVININLKNKPEWFFKKN-PFGLVPVLENSqGQLIYESAITCEYL 93
Cdd:cd03039   12 GEPIRLLLADAGVEYEDVRITYEEWPELDLKPTlPFGQLPVLEID-GKKLTQSNAILRYL 70
GST_N_etherase_LigE cd03038
GST_N family, Beta etherase LigE subfamily; composed of proteins similar to Sphingomonas ...
 31-98 6.51e-05

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: 40.02  E-value: 6.51e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  31 FCPFAERTRLVLKAKGIRHEVININLKNKPEWFFK--KNPFGLVPVLENSQGQLIYESAITCEYLDEAYP 98
Cdd:cd03038   15 FSPNVWKTRLALNHKGLEYKTVPVEFPDIPPILGEltSGGFYTVPVIVDGSGEVIGDSFAIAEYLEEAYP 84
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 32-98 9.65e-05

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: 39.44  E-value: 9.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  32 CPFAerTRLVLKAKGIRHEVININLKNKPEW---FFKKNPFGLVPVLENSQGQLIYESAITCEYLDEAYP 98
Cdd:cd03057   10 CSLA--PHIALEELGLPFELVRVDLRTKTQKgadYLAINPKGQVPALVLDDGEVLTESAAILQYLADLHP 77
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 109-183 1.48e-04

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: 40.24  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532 109 EKACQKMIlELFsKVL-----TNKKttFFGGNSISMID---YLIWPWFERLEAM---KLNEcVDHTPKLKLWMAAMKEDP 177
Cdd:cd03185   34 EKAVEEAL-EAL-KVLeeelkGGKP--FFGGDTIGYLDialGSFLGWFKAIEEVggvKLLD-EEKFPLLAAWAERFLERE 108


                 ....*.
gi 300360532 178 TVSALL 183
Cdd:cd03185  109 AVKEVL 114
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 92-167 1.59e-04

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 39.53  E-value: 1.59e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300360532  92 YLDEAYPGKKLLPDDPYEKACQKMiLELFSKVLTNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTPKLK 167
Cdd:cd03192   24 FYEPDGEEKKEKKKEFLEEALPKF-LGKFEKILKKSGGGYFVGDKLTWADLALFDVLDYLLYLLPKDLLEKYPKLK 98
PRK15113 PRK15113
glutathione transferase;
31-116 3.97e-04

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 39.94  E-value: 3.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532  31 FCPFAERTRLVLKAKGIRHEVININLKNK----PEWFfKKNPFGLVPVLENSQGQLIYESAItCEYLDEAYPG---KKLL 103
Cdd:PRK15113  15 FSPYVMSAFVALQEKGLPFELKTVDLDAGehlqPTYQ-GYSLTRRVPTLQHDDFELSESSAI-AEYLEERFAPpawERIY 92

                         90
                 ....*....|...
gi 300360532 104 PDDPYEKACQKMI 116
Cdd:PRK15113  93 PADLQARARARQI 105
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
24-54 5.21e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.48  E-value: 5.21e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 300360532  24 IRIYSMRFCPFAERTRLVLKAKGIRHEVINI 54
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDV 32
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 40-98 9.11e-04

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing 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 N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of 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.


Pssm-ID: 239346 [Multi-domain]  Cd Length: 81  Bit Score: 36.75  E-value: 9.11e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300360532  40 LVLKAKGIRHEVININLK---NKPEWFFKKNPFGLVPVLE--NSQGQLIYESAITCEYLDEAYP 98
Cdd:cd03048   17 IMLEELGLPYEIHPVDISkgeQKKPEFLKINPNGRIPAIVdhNGTPLTVFESGAILLYLAEKYD 80
GST_C_Mu cd03209
C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione ...
 101-187 1.45e-03

C-terminal, alpha helical domain of Class Mu Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Mu 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 class Mu subfamily is composed of eukaryotic GSTs. In rats, at least six distinct class Mu subunits have been identified, with homologous genes in humans for five of these subunits. Class Mu GSTs can form homodimers and heterodimers, giving a large number of possible isoenzymes that can be formed, all with overlapping activities but different substrate specificities. They are the most abundant GSTs in human liver, skeletal muscle and brain, and are believed to provide protection against diseases including cancer and neurodegenerative disorders. Some isoenzymes have additional specific functions. Human GST M1-1 acts as an endogenous inhibitor of ASK1 (apoptosis signal-regulating kinase 1) thereby suppressing ASK1-mediated cell death. Human GSTM2-2 and 3-3 have been identified as prostaglandin E2 synthases in the brain and may play crucial roles in temperature and sleep-wake regulation.


Pssm-ID: 198318 [Multi-domain]  Cd Length: 121  Bit Score: 37.23  E-value: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300360532 101 KLLPDdpYEKACQKMiLELFSKVLTNKKttFFGGNSISMIDYLIWPWFERLEAMKlNECVDHTPKLKLWMAAMKEDPTVS 180
Cdd:cd03209   31 KLKPD--YLEKLPDK-LKLFSEFLGDRP--WFAGDKITYVDFLLYEALDQHRIFE-PDCLDAFPNLKDFLERFEALPKIS 104


                 ....*..
gi 300360532 181 ALLTSEK 187
Cdd:cd03209  105 AYMKSDR 111
Glutaredoxin pfam00462
Glutaredoxin;
24-54 1.76e-03

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 35.56  E-value: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 300360532   24 IRIYSMRFCPFAERTRLVLKAKGIRHEVINI 54
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDV 31
PLN02473 PLN02473
glutathione S-transferase
 32-92 1.88e-03

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 38.05  E-value: 1.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300360532  32 CPfaERTRLVLKAKGIRHEVININL----KNKPEWFFKKnPFGLVPVLENSQGQLIYESAITCEY 92
Cdd:PLN02473  13 NP--QRVLLCFLEKGIEFEVIHVDLdkleQKKPEHLLRQ-PFGQVPAIEDGDLKLFESRAIARYY 74
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
 58-93 4.45e-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: 4.45e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 300360532  58 NKPEWFFKKNPFGLVPVLENSQGQLIYESAITCEYL 93
Cdd:cd03044   37 NKTPEFLKKFPLGKVPAFEGADGFCLFESNAIAYYV 72
GST_N_CLIC cd03061
GST_N family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLIC1-5, p64, ...
 32-73 5.16e-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: 35.04  E-value: 5.16e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 300360532  32 CPFAERTRLVLKAKGIRHEVININLKNKPEwFFKKNPFGLVP 73
Cdd:cd03061   22 CPFCQRLFMVLWLKGVVFNVTTVDMKRKPE-DLKDLAPGTQP 62
PLN02395 PLN02395
glutathione S-transferase
 24-97 6.32e-03

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 36.38  E-value: 6.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300360532  24 IRIYSMRFCPfAERTRLVLKAKGIRHEVININL---KNKPEWFFKKNPFGLVPVLENSQGQLiYESAITCEYLDEAY 97
Cdd:PLN02395   3 LKVYGPAFAS-PKRALVTLIEKGVEFETVPVDLmkgEHKQPEYLALQPFGVVPVIVDGDYKI-FESRAIMRYYAEKY 77
GST_N_GRX2 cd03037
GST_N family, Glutaredoxin 2 (GRX2) subfamily; composed of bacterial proteins similar to E. ...
 25-95 6.59e-03

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: 34.29  E-value: 6.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300360532  25 RIYSMRFCPFAERTRLVLKAKGIRHEVINinLKNKPEwffkKNPFG-----LVPVLENSQGQLIYESAITCEYLDE 95
Cdd:cd03037    2 KLYIYEHCPFCVKARMIAGLKNIPVEQII--LQNDDE----ATPIRmigakQVPILEKDDGSFMAESLDIVAFIDE 71
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 104-177 7.94e-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: 34.57  E-value: 7.94e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300360532  104 PDDPYEKACQKMILELFSKVL-TNKKTTFFGGNSISMIDYLIWPWFERLEAMKLNECVDHTPKLKLWMAAMKEDP 177
Cdd:pfam00043  19 KKEPEVDEALEKVARVLSALEeVLKGQTYLVGDKLTLADIALAPALLWLYELDPACLREKFPNLKAWFERVAARP 93
 
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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