NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767961579|ref|XP_011537572|]
View 

glutathione S-transferase omega-2 isoform X1 [Homo sapiens]

Protein Classification

glutathione S-transferase omega( domain architecture ID 10221648)

class-omega glutathione S-transferase (GST) catalyzes 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_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 108-230 2.28e-54

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: 170.96  E-value: 2.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579 108 YERARQKMLLELFCKVPHLTKECLvalRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDV 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYKFL---RSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767961579 188 YGIL----DCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 7-94 4.48e-47

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member cd03055:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 89  Bit Score: 150.97  E-value: 4.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579   7 RTLGKGSQPPGPVPeGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYES 86
Cdd:cd03055    3 KHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVYES 81


                 ....*...
gi 767961579  87 VIACEYLD 94
Cdd:cd03055   82 LIICEYLD 89
 
Name Accession Description Interval E-value
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 108-230 2.28e-54

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: 170.96  E-value: 2.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579 108 YERARQKMLLELFCKVPHLTKECLvalRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDV 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYKFL---RSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767961579 188 YGIL----DCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-94 4.48e-47

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: 150.97  E-value: 4.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579   7 RTLGKGSQPPGPVPeGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYES 86
Cdd:cd03055    3 KHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVYES 81


                 ....*...
gi 767961579  87 VIACEYLD 94
Cdd:cd03055   82 LIICEYLD 89
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
24-208 1.87e-30

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 111.91  E-value: 1.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579  24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLR---NKPEWYYTKHPFGHIPVLETSQcQLIYESVIACEYLDDAYPGR 100
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGKVPVLVDDG-LVLTESLAILEYLAERYPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579 101 KLFPYDPYERARQKMLLELFCKV--PHLTKecLVALRCGRECTNLKAALRQEFSNLEEILEYQ--NTTFFGGTCISMIDY 176
Cdd:COG0625   81 PLLPADPAARARVRQWLAWADGDlhPALRN--LLERLAPEKDPAAIARARAELARLLAVLEARlaGGPYLAGDRFSIADI 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767961579 177 LLWPWFERLDVYGIldCVSHTPALRLWISAMK 208
Cdd:COG0625  159 ALAPVLRRLDRLGL--DLADYPNLAAWLARLA 188
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
27-101 4.08e-16

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 70.72  E-value: 4.08e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961579   27 YSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQcQLIYESVIACEYLDDAYPGRK 101
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDDG-GILCESLAIIDYLEELYPGPP 75
sspA PRK09481
stringent starvation protein A; Provisional
 34-190 1.21e-08

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 53.56  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579  34 YSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLiYESVIACEYLDDAYPGRKLFPYDPYERARQ 113
Cdd:PRK09481  21 YSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTLVDRELTL-YESRIIMEYLDERFPHPPLMPVYPVARGES 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579 114 KMLLE--------LFCKVPHLTKEclvalrcgrECTNLKAALRQEFSNLEEIleYQNTTFFGGTCISMIDYLLWPWFERL 185
Cdd:PRK09481 100 RLMMHriekdwysLMNKIVNGSAS---------EADAARKQLREELLAIAPV--FGEKPYFMSEEFSLVDCYLAPLLWRL 168


                 ....*
gi 767961579 186 DVYGI 190
Cdd:PRK09481 169 PVLGI 173
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 32-119 2.64e-08

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 53.07  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579  32 CPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQcQLIYESVIACEYLDDAYP------------- 98
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDE-KWVADSDVITQALEEKYPdpplatppekasv 151

                         90       100
                 ....*....|....*....|....*....
gi 767961579  99 GRKLFPY--------DPYERARQKMLLEL 119
Cdd:PLN02817 152 GSKIFSTfigflkskDPGDGTEQALLDEL 180
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
24-54 4.48e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.87  E-value: 4.48e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767961579  24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNI 54
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDV 32
 
Name Accession Description Interval E-value
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 108-230 2.28e-54

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: 170.96  E-value: 2.28e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579 108 YERARQKMLLELFCKVPHLTKECLvalRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDV 187
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYKFL---RSGEDRKGLKEELRSALENLEEELAKRGTPFFGGNSPGMVDYMIWPWFERLEA 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767961579 188 YGIL----DCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLY 230
Cdd:cd03184   78 LKLLdgyeLCLDRFPKLKKWMAAMKQDPAVKAFYTDPETHAEFLNSY 124
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-94 4.48e-47

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: 150.97  E-value: 4.48e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579   7 RTLGKGSQPPGPVPeGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYES 86
Cdd:cd03055    3 KHLAKGSAEPPPVP-GIIRLYSMRFCPYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGKVPALEIDEGKVVYES 81


                 ....*...
gi 767961579  87 VIACEYLD 94
Cdd:cd03055   82 LIICEYLD 89
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
24-208 1.87e-30

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 111.91  E-value: 1.87e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579  24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLR---NKPEWYYTKHPFGHIPVLETSQcQLIYESVIACEYLDDAYPGR 100
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAkgeQKSPEFLALNPLGKVPVLVDDG-LVLTESLAILEYLAERYPEP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579 101 KLFPYDPYERARQKMLLELFCKV--PHLTKecLVALRCGRECTNLKAALRQEFSNLEEILEYQ--NTTFFGGTCISMIDY 176
Cdd:COG0625   81 PLLPADPAARARVRQWLAWADGDlhPALRN--LLERLAPEKDPAAIARARAELARLLAVLEARlaGGPYLAGDRFSIADI 158

                        170       180       190
                 ....*....|....*....|....*....|..
gi 767961579 177 LLWPWFERLDVYGIldCVSHTPALRLWISAMK 208
Cdd:COG0625  159 ALAPVLRRLDRLGL--DLADYPNLAAWLARLA 188
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
27-101 4.08e-16

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 70.72  E-value: 4.08e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961579   27 YSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQcQLIYESVIACEYLDDAYPGRK 101
Cdd:pfam13417   2 YGFPGSPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGKVPVLEDDG-GILCESLAIIDYLEELYPGPP 75
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 31-96 5.12e-16

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 70.35  E-value: 5.12e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767961579   31 FCPYSHRTRLVLKAKDIRHEV--VNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDA 96
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIelVDLDPKDKPPELLALNPLGTVPVLVLPDGTVLTDSLVILEYLEEL 68
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 24-94 6.70e-15

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: 67.21  E-value: 6.70e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961579  24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTK-HPFGHIPVLETSQCQlIYESVIACEYLD 94
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEEFLAlNPLGKVPVLEDGGLV-LTESLAILEYLA 71
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 27-97 4.14e-12

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: 60.03  E-value: 4.14e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767961579  27 YSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLiYESVIACEYLDDAY 97
Cdd:cd03059    4 YSGPDDVYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYGTVPTLVDRDLVL-YESRIIMEYLDERF 73
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 24-95 1.72e-11

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: 58.47  E-value: 1.72e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961579   24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINL---RNKPEWYYTKHPFGHIPVLETsQCQLIYESVIACEYLDD 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 2.70e-11

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: 57.66  E-value: 2.70e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961579  24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINL---RNKPEWYYTKHPFGHIPVLETSQCQLiYESVIACEYLDD 95
Cdd:cd03053    2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLtkgEHKSPEHLARNPFGQIPALEDGDLKL-FESRAITRYLAE 75
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 25-94 1.55e-09

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


Pssm-ID: 239349 [Multi-domain]  Cd Length: 74  Bit Score: 53.07  E-value: 1.55e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961579  25 RIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLR---NKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLD 94
Cdd:cd03051    2 KLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAageQRSPEFLAKNPAGTVPVLELDDGTVITESVAICRYLE 74
sspA PRK09481
stringent starvation protein A; Provisional
 34-190 1.21e-08

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 53.56  E-value: 1.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579  34 YSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLiYESVIACEYLDDAYPGRKLFPYDPYERARQ 113
Cdd:PRK09481  21 YSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNPYQSVPTLVDRELTL-YESRIIMEYLDERFPHPPLMPVYPVARGES 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579 114 KMLLE--------LFCKVPHLTKEclvalrcgrECTNLKAALRQEFSNLEEIleYQNTTFFGGTCISMIDYLLWPWFERL 185
Cdd:PRK09481 100 RLMMHriekdwysLMNKIVNGSAS---------EADAARKQLREELLAIAPV--FGEKPYFMSEEFSLVDCYLAPLLWRL 168


                 ....*
gi 767961579 186 DVYGI 190
Cdd:PRK09481 169 PVLGI 173
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 32-119 2.64e-08

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 53.07  E-value: 2.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579  32 CPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQcQLIYESVIACEYLDDAYP------------- 98
Cdd:PLN02817  73 CPFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGKVPVVKLDE-KWVADSDVITQALEEKYPdpplatppekasv 151

                         90       100
                 ....*....|....*....|....*....
gi 767961579  99 GRKLFPY--------DPYERARQKMLLEL 119
Cdd:PLN02817 152 GSKIFSTfigflkskDPGDGTEQALLDEL 180
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 26-87 1.86e-07

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: 47.35  E-value: 1.86e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767961579  26 IYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESV 87
Cdd:cd03060    3 LYSFRRCPYAMRARMALLLAGITVELREVELKNKPAEMLAASPKGTVPVLVLGNGTVIEESL 64
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 33-97 2.16e-06

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: 44.19  E-value: 2.16e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961579  33 PYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHP-FGHIPVLETSQCQlIYESVIACEYLDDAY 97
Cdd:cd03058   10 PFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPvHKKIPVLLHNGKP-ICESLIIVEYIDEAW 74
PLN02378 PLN02378
glutathione S-transferase DHAR1
 32-187 3.29e-06

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 46.63  E-value: 3.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579  32 CPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQcQLIYESVIACEYLDDAYPGRKLfpydpyera 111
Cdd:PLN02378  20 CPFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGKVPVLKIDD-KWVTDSDVIVGILEEKYPDPPL--------- 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767961579 112 rqKMLLELFCKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDV 187
Cdd:PLN02378  90 --KTPAEFASVGSNIFGTFGTFLKSKDSNDGSEHALLVELEALENHLKSHDGPFIAGERVSAVDLSLAPKLYHLQV 163
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 33-94 1.15e-05

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: 42.25  E-value: 1.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767961579  33 PYSHRTRLVL--KAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLD 94
Cdd:cd03049   10 PYVRKVRVAAheTGLGDDVELVLVNPWSDDESLLAVNPLGKIPALVLDDGEALFDSRVICEYLD 73
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 142-207 3.37e-05

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 41.72  E-value: 3.37e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961579 142 NLKAALRQEFSNLEEILeyQNTTFFGGTCISMIDYLLWPWFERLDVYG-ILDCVSHTPALRLWISAM 207
Cdd:cd00299   36 AAREELPALLAALEQLL--AGRPYLAGDQFSLADVALAPVLARLEALGpYYDLLDEYPRLKAWYDRL 100
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 35-94 2.71e-04

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: 38.32  E-value: 2.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767961579  35 SHRTRLVLKAKDIRHEVVNINLR----NKPEwyYTKH-PFGHIPVLETSQcQLIYESVIACEYLD 94
Cdd:cd03042   12 SYRVRIALNLKGLDYEYVPVNLLkgeqLSPA--YRALnPQGLVPTLVIDG-LVLTQSLAIIEYLD 73
Glutaredoxin pfam00462
Glutaredoxin;
24-54 3.72e-04

Glutaredoxin;


Pssm-ID: 425695 [Multi-domain]  Cd Length: 60  Bit Score: 37.48  E-value: 3.72e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 767961579   24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNI 54
Cdd:pfam00462   1 VVLYTKPTCPFCKRAKRLLKSLGVDFEEIDV 31
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 24-93 4.10e-04

GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 37.94  E-value: 4.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767961579  24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRN---KPEWYYTKHPFGHIPVLETSQCQLiYESVIACEYL 93
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKgetRTPEFLALNPNGEVPVLELDGRVL-AESNAILVYL 72
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
24-54 4.48e-04

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 37.87  E-value: 4.48e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 767961579  24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNI 54
Cdd:COG0695    2 VTLYTTPGCPYCARAKRLLDEKGIPYEEIDV 32
PRK15113 PRK15113
glutathione transferase;
31-116 6.16e-04

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 39.94  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767961579  31 FCPYSHRTRLVLKAKDIRHEVVNINL---RNKPEWYYTKHPFGHIPVLETSQCQLIYESVIaCEYLDDAYPG---RKLFP 104
Cdd:PRK15113  15 FSPYVMSAFVALQEKGLPFELKTVDLdagEHLQPTYQGYSLTRRVPTLQHDDFELSESSAI-AEYLEERFAPpawERIYP 93

                         90
                 ....*....|..
gi 767961579 105 YDPYERARQKML 116
Cdd:PRK15113  94 ADLQARARARQI 105
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 35-98 6.44e-04

GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals.


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 37.48  E-value: 6.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767961579  35 SHRTRLVLKAKDIRHEVVNINLRN---KPEWYYTKHPFGHIPVLETSQcQLIYESVIACEYLDDAYP 98
Cdd:cd03046   11 SFRILWLLEELGLPYELVLYDRGPgeqAPPEYLAINPLGKVPVLVDGD-LVLTESAAIILYLAEKYG 76
GRX_family cd02066
Glutaredoxin (GRX) family; composed of GRX, approximately 10 kDa in size, and proteins ...
 24-55 3.60e-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: 35.14  E-value: 3.60e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 767961579  24 IRIYSMRFCPYSHRTRLVLKAKDIRHEVVNIN 55
Cdd:cd02066    2 VVVFSKSTCPYCKRAKRLLESLGIEFEEIDIL 33
 
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