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Conserved domains on  [gi|16130237|ref|NP_416805|]
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disulfide bond oxidoreductase YfcG [Escherichia coli str. K-12 substr. MG1655]

Protein Classification

thiol:disulfide oxidoreductase( domain architecture ID 11487024)

thiol:disulfide oxidoreductase YfcG-like, a glutathione S-transferase family protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
1-215 5.05e-160

GSH-dependent disulfide bond oxidoreductase; Provisional


:

Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 440.67  E-value: 5.05e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237    1 MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLA 80
Cdd:PRK13972   1 MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   81 EKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYS 160
Cdd:PRK13972  81 EKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16130237  161 IADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS 215
Cdd:PRK13972 161 IADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS 215
 
Name Accession Description Interval E-value
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
1-215 5.05e-160

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 440.67  E-value: 5.05e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237    1 MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLA 80
Cdd:PRK13972   1 MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   81 EKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYS 160
Cdd:PRK13972  81 EKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16130237  161 IADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS 215
Cdd:PRK13972 161 IADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS 215
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-207 3.36e-70

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 212.83  E-value: 3.36e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   1 MIDLY-FAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDhspadggEPLSLFESGAILLYL 79
Cdd:COG0625   1 MMKLYgSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVD-------DGLVLTESLAILEYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  80 AEKTGL--FLSHETRERAATLQWLFWQVGGLGPMLGQnhHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGE 157
Cdd:COG0625  74 AERYPEppLLPADPAARARVRQWLAWADGDLHPALRN--LLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16130237 158 NYSIADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQ 207
Cdd:COG0625 152 RFSIADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAAE 201
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
93-202 2.06e-67

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 202.50  E-value: 2.06e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  93 ERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVNA 172
Cdd:cd10291   1 ERYAVLQWLMWQMGGLGPMQGQAHHFKRYAPEKIPYAIKRYTNETKRLYGVLDRRLAKSKYLAGDEYSIADIAIWPWVAR 80
                        90       100       110
                ....*....|....*....|....*....|
gi 16130237 173 WTRQRIDLAMYPAVKNWHERIRSRPATGQA 202
Cdd:cd10291  81 HEWQGIDLADFPNLKRWFERLAARPAVQKG 110
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
8-81 2.14e-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: 65.40  E-value: 2.14e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130237     8 PTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAE 81
Cdd:pfam02798  10 GSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGG-------KKLTESRAILEYIAR 76
 
Name Accession Description Interval E-value
PRK13972 PRK13972
GSH-dependent disulfide bond oxidoreductase; Provisional
1-215 5.05e-160

GSH-dependent disulfide bond oxidoreductase; Provisional


Pssm-ID: 172475 [Multi-domain]  Cd Length: 215  Bit Score: 440.67  E-value: 5.05e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237    1 MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLA 80
Cdd:PRK13972   1 MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSPADGGEPLSLFESGAILLYLA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   81 EKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYS 160
Cdd:PRK13972  81 EKTGLFLSHETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYS 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 16130237  161 IADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS 215
Cdd:PRK13972 161 IADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQLGDERSDS 215
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
1-207 3.36e-70

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 212.83  E-value: 3.36e-70
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   1 MIDLY-FAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDhspadggEPLSLFESGAILLYL 79
Cdd:COG0625   1 MMKLYgSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVD-------DGLVLTESLAILEYL 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  80 AEKTGL--FLSHETRERAATLQWLFWQVGGLGPMLGQnhHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGE 157
Cdd:COG0625  74 AERYPEppLLPADPAARARVRQWLAWADGDLHPALRN--LLERLAPEKDPAAIARARAELARLLAVLEARLAGGPYLAGD 151
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 16130237 158 NYSIADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPATGQALLKAQ 207
Cdd:COG0625 152 RFSIADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRALAAAE 201
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
93-202 2.06e-67

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 202.50  E-value: 2.06e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  93 ERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVNA 172
Cdd:cd10291   1 ERYAVLQWLMWQMGGLGPMQGQAHHFKRYAPEKIPYAIKRYTNETKRLYGVLDRRLAKSKYLAGDEYSIADIAIWPWVAR 80
                        90       100       110
                ....*....|....*....|....*....|
gi 16130237 173 WTRQRIDLAMYPAVKNWHERIRSRPATGQA 202
Cdd:cd10291  81 HEWQGIDLADFPNLKRWFERLAARPAVQKG 110
PRK11752 PRK11752
putative S-transferase; Provisional
4-198 7.81e-67

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 206.32  E-value: 7.81e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237    4 LYFAPTPNGHKITLFLEE------AELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadGGEPLSLFESGAILL 77
Cdd:PRK11752  47 LYSLGTPNGQKVTIMLEEllalgvKGAEYDAWLIRIGEGDQFSSGFVEINPNSKIPALLDRS---GNPPIRVFESGAILL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   78 YLAEKTGLFLSHETRERAATLQWLFWQVGGlGPMLGQNH-HFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGG 156
Cdd:PRK11752 124 YLAEKFGAFLPKDLAARTETLNWLFWQQGS-APFLGGGFgHFYAYAPEKIEYAINRFTMEAKRQLDVLDKQLAEHEYIAG 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16130237  157 ENYSIADIACWPWVNAWTRQRI-------DLAMYPAVKNWHERIRSRPA 198
Cdd:PRK11752 203 DEYTIADIAIWPWYGNLVLGNLydaaeflDVGSYKHVQRWAKEIAERPA 251
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
93-198 3.84e-56

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. 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 thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-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. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. 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. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198288 [Multi-domain]  Cd Length: 110  Bit Score: 173.59  E-value: 3.84e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  93 ERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVNA 172
Cdd:cd03178   1 ERAEVLQWLFFQMSGLGPMFGQAGHFLYFAPEKIPYAIERYTDEVKRLYGVLDKRLSDRPYLAGEEYSIADIALYPWTHY 80
                        90       100
                ....*....|....*....|....*..
gi 16130237 173 WTRQRI-DLAMYPAVKNWHERIRSRPA 198
Cdd:cd03178  81 ADLGGFaDLSEYPNVKRWLERIAARPA 107
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
1-84 1.32e-46

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: 148.46  E-value: 1.32e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   1 MIDLYFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadgGEPLSLFESGAILLYLA 80
Cdd:cd03048   1 MITLYTHGTPNGFKVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIVDHN----GTPLTVFESGAILLYLA 76

                ....
gi 16130237  81 EKTG 84
Cdd:cd03048  77 EKYD 80
GST_C_YghU_like cd10292
C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and ...
93-198 1.14e-29

C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU and related proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU does not contain a redox active cysteine residue, and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YghU reveals two GSH molecules bound in its active site.


Pssm-ID: 198325 [Multi-domain]  Cd Length: 118  Bit Score: 106.39  E-value: 1.14e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  93 ERAATLQWLFWQVGGlGPMLGQNH-HFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVN 171
Cdd:cd10292   1 KRTETLNWLFWQMGS-APYLGGGFgHFYSYAPVKIEYAIDRFTMEAKRQLDVLDRQLATHKYLAGDEYTIADMAIWPWYG 79
                        90       100       110
                ....*....|....*....|....*....|....
gi 16130237 172 AWTRQR-------IDLAMYPAVKNWHERIRSRPA 198
Cdd:cd10292  80 GLALGSlydaaefLDVDEYKHVQRWAKDIAARPA 113
GST_C_Ure2p cd10293
C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione ...
99-198 6.34e-24

C-terminal, alpha helical domain of fungal Ure2p Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Ure2p subfamily; composed of the Saccharomyces cerevisiae Ure2p and related fungal proteins. 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 thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-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. 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. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198326 [Multi-domain]  Cd Length: 117  Bit Score: 91.72  E-value: 6.34e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  99 QWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENS--PWLGGENYSIADIACWPWVNAWTRQ 176
Cdd:cd10293   7 QWLFFQASGQGPYWGQAGWFNVFHAEKVPSAIERYTNEIRRVLGVLETALAERyrVWLVGDKFTIADLAFVPWNNVVDMI 86
                        90       100
                ....*....|....*....|....*..
gi 16130237 177 RID-----LAMYPAVKNWHERIRSRPA 198
Cdd:cd10293  87 FIDpeldiKKEFPHVYKWLKRMLARPA 113
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
19-84 1.09e-17

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: 74.08  E-value: 1.09e-17
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130237  19 LEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHspadggePLSLFESGAILLYLAEKTG 84
Cdd:cd03046  18 LEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDG-------DLVLTESAAIILYLAEKYG 76
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
5-80 3.17e-16

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: 70.29  E-value: 3.17e-16
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 16130237   5 YFAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQfrPEFLRISPNNKIPAIVDhspadggEPLSLFESGAILLYLA 80
Cdd:cd00570   5 YFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQ--EEFLALNPLGKVPVLED-------GGLVLTESLAILEYLA 71
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
4-82 4.08e-15

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: 67.29  E-value: 4.08e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   4 LY-FAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHspadggePLSLFESGAILLYLAEK 82
Cdd:cd03053   4 LYgAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDG-------DLKLFESRAITRYLAEK 76
PRK10542 PRK10542
glutathionine S-transferase; Provisional
19-207 8.92e-15

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 69.71  E-value: 8.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   19 LEEAELDYRLIKVDLGKGgqfRPE----FLRISPNNKIPAIVdhspADGGEPLSlfESGAILLYLAEKT---GLFLSHET 91
Cdd:PRK10542  18 LRESGLDFTLVSVDLAKK---RLEngddYLAINPKGQVPALL----LDDGTLLT--EGVAIMQYLADSVpdrQLLAPVGS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   92 RERAATLQWLFWQVG----GLGPMlgqnhhFNHAAPQTipY-AIERYQVETQrlYHVLNKRLENSPWLGGENYSIAD--- 163
Cdd:PRK10542  89 LSRYHTIEWLNYIATelhkGFTPL------FRPDTPEE--YkPTVRAQLEKK--FQYVDEALADEQWICGQRFTIADayl 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 16130237  164 --IACW-PWVNawtrqrIDLAMYPAVKNWHERIRSRPATgQALLKAQ 207
Cdd:PRK10542 159 ftVLRWaYAVK------LNLEGLEHIAAYMQRVAERPAV-AAALKAE 198
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
4-80 1.05e-14

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: 66.44  E-value: 1.05e-14
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16130237   4 LY-FAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDhspaDGgepLSLFESGAILLYLA 80
Cdd:cd03056   3 LYgFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLEL----DG---RVLAESNAILVYLA 73
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
8-81 2.14e-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: 65.40  E-value: 2.14e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130237     8 PTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAE 81
Cdd:pfam02798  10 GSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGG-------KKLTESRAILEYIAR 76
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
19-82 2.77e-14

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: 65.25  E-value: 2.77e-14
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130237  19 LEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDhspaDGGEPlsLFESGAILLYLAEK 82
Cdd:cd03057  18 LEELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALVL----DDGEV--LTESAAILQYLADL 75
PLN02395 PLN02395
glutathione S-transferase
19-198 6.66e-13

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 64.88  E-value: 6.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   19 LEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAEK-----TGLfLSHETRE 93
Cdd:PLN02395  20 LIEKGVEFETVPVDLMKGEHKQPEYLALQPFGVVPVIVDGD-------YKIFESRAIMRYYAEKyrsqgPDL-LGKTIEE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   94 RAATLQWLFWQVGGLGP-MLGQNHHFNHAAPQTIP---YAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPW 169
Cdd:PLN02395  92 RGQVEQWLDVEATSYHPpLLNLTLHILFASKMGFPadeKVIKESEEKLAKVLDVYEARLSKSKYLAGDFVSLADLAHLPF 171
                        170       180       190
                 ....*....|....*....|....*....|..
gi 16130237  170 VNAWTRQRIDLAMYPA---VKNWHERIRSRPA 198
Cdd:PLN02395 172 TEYLVGPIGKAYLIKDrkhVSAWWDDISSRPA 203
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
92-198 1.88e-12

C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 2; 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 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.


Pssm-ID: 198289 [Multi-domain]  Cd Length: 110  Bit Score: 61.53  E-value: 1.88e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  92 RERAATLQWLFWQVGGLGPMLGQN--HHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPW 169
Cdd:cd03180   1 AQRALADRWMDWQTSTLNPAFRYAfwGLVRTPPEQRDPAAIAASLAACNKLMAILDAQLARQAYLAGDRFTLADIALGCS 80
                        90       100
                ....*....|....*....|....*....
gi 16130237 170 VNAWTRQRIDLAMYPAVKNWHERIRSRPA 198
Cdd:cd03180  81 VYRWLELPIERPALPHLERWYARLSQRPA 109
GST_N_Theta cd03050
GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial ...
18-82 4.86e-12

GST_N family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. 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. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from aryl or alkyl sulfate esters.


Pssm-ID: 239348 [Multi-domain]  Cd Length: 76  Bit Score: 59.18  E-value: 4.86e-12
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 16130237  18 FLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAEK 82
Cdd:cd03050  18 FLKLNKIPFEECPIDLRKGEQLTPEFKKINPFGKVPAIVDGD-------FTLAESVAILRYLARK 75
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
2-81 1.54e-11

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: 58.00  E-value: 1.54e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   2 IDLYFAP-TPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHspadggePLSLFESGAILLYLA 80
Cdd:cd03045   1 IDLYYLPgSPPCRAVLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDN-------GFVLWESHAILIYLV 73

                .
gi 16130237  81 E 81
Cdd:cd03045  74 E 74
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
92-203 2.52e-11

C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they are involved in the protection against oxidative stress and are able to bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs, contributing to antibiotic resistance. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. One member of this subfamily is a GST from Burkholderia xenovorans LB400 that is encoded by the bphK gene and is part of the biphenyl catabolic pathway.


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 58.41  E-value: 2.52e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  92 RERAATLQWLFWQVGGLGPMLGqnHHFNHAAPqTIPYAIERYQVET----QRLYHVLNKRLENSPWLGGENYSIADIACW 167
Cdd:cd03188   1 LERARLLEWLNFIASELHKAFG--PLFYPARW-ADDALAEEVKAAArerlERRLAYLDAQLAGGPYLLGDQFSVADAYLF 77
                        90       100       110
                ....*....|....*....|....*....|....*..
gi 16130237 168 PWVNaWTR-QRIDLAMYPAVKNWHERIRSRPATGQAL 203
Cdd:cd03188  78 VVLR-WARaVGLDLSDWPHLAAYLARVAARPAVQAAL 113
GST_C_7 cd03206
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ...
127-197 1.17e-10

C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized 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 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.


Pssm-ID: 198315 [Multi-domain]  Cd Length: 100  Bit Score: 56.46  E-value: 1.17e-10
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130237 127 PYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVnAWTRQ-RIDLAMYPAVKNWHERIRSRP 197
Cdd:cd03206  28 PLDPERARAISHRLLRLLDQHLAGRDWLAGDRPTIADVACYPYI-ALAPEgGVSLEPYPAIRAWLARVEALP 98
PLN02473 PLN02473
glutathione S-transferase
11-198 1.84e-10

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 58.46  E-value: 1.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   11 NGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAEK---TGLFL 87
Cdd:PLN02473  13 NPQRVLLCFLEKGIEFEVIHVDLDKLEQKKPEHLLRQPFGQVPAIEDGD-------LKLFESRAIARYYATKyadQGTDL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   88 SHETRE-RAATLQWLfwQVgglgpmlgQNHHFNHAA-PQTIPYAI-------------ERYQVETQRLYHVLNKRLENSP 152
Cdd:PLN02473  86 LGKTLEhRAIVDQWV--EV--------ENNYFYAVAlPLVINLVFkprlgepcdvalvEELKVKFDKVLDVYENRLATNR 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 16130237  153 WLGGENYSIADIACWPWVNAWTRQRIDLAMYPAVKN---WHERIRSRPA 198
Cdd:PLN02473 156 YLGGDEFTLADLTHMPGMRYIMNETSLSGLVTSRENlnrWWNEISARPA 204
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
10-82 1.88e-10

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 54.94  E-value: 1.88e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 16130237    10 PNGHKITLFLEEAELDYRLIKVDLgKGGQFRPEFLRISPNNKIPAIVDhspaDGGEPLSlfESGAILLYLAEK 82
Cdd:pfam13409   3 PFSHRVRLALEEKGLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVL----PDGTVLT--DSLVILEYLEEL 68
GST_N_2 cd03047
GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ...
11-80 3.20e-09

GST_N family, unknown subfamily 2; 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. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions.


Pssm-ID: 239345 [Multi-domain]  Cd Length: 73  Bit Score: 51.55  E-value: 3.20e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  11 NGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDhspadgGEpLSLFESGAILLYLA 80
Cdd:cd03047  11 NVQKVLWLLDELGLPYERIDAGGQFGGLDTPEFLAMNPNGRVPVLED------GD-FVLWESNAILRYLA 73
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
99-193 5.19e-09

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


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 51.73  E-value: 5.19e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  99 QWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVNAWTR--- 175
Cdd:cd00299   3 ALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAlgp 82
                        90
                ....*....|....*...
gi 16130237 176 QRIDLAMYPAVKNWHERI 193
Cdd:cd00299  83 YYDLLDEYPRLKAWYDRL 100
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
98-198 5.18e-08

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other 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 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 three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 49.22  E-value: 5.18e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  98 LQWLFWQVGGLGP-MLGQNHHFNHAAPQTIPYAIERYQVETQRLyHVLNKRLENSPWLGGENYSIADIaCWPWVNAWTRQ 176
Cdd:cd03207   2 LRWLFFAAGTVEPpLLNKALGRFFEPPWGEPAIAAAYGDLDERL-AALEAALAGRPYLVGERFSAADL-LLASVLRWARA 79
                        90       100
                ....*....|....*....|..
gi 16130237 177 RIDLAMYPAVKNWHERIRSRPA 198
Cdd:cd03207  80 FGLLPEYPALRAYVARCTARPA 101
GST_C_5 cd03196
C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; ...
128-189 5.18e-08

C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 5; 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 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.


Pssm-ID: 198305 [Multi-domain]  Cd Length: 115  Bit Score: 49.46  E-value: 5.18e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130237 128 YAiERYQVETQRLY--------HVLNKRLENSPWLGGENYSIADIACWPWVnawtRQ--RIDL-----AMYPAVKNW 189
Cdd:cd03196  30 YA-DRYPEDDEEEYraqaeeflAELEARLSQHAYLFGDRPSLADYAIFPFV----RQfaHVDRdwfdaSPYPNLRRW 101
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
141-198 1.00e-07

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces 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 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. 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: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 48.86  E-value: 1.00e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237 141 YHVLNKRLENSPWLGGENYSIADIACWPWVN--AWTRQRIDlAMYPAVKNWHERIRSRPA 198
Cdd:cd03182  57 LPVLDKRLAESPYVAGDRFSIADITAFVALDfaKNLKLPVP-EELTALRRWYERMAARPS 115
GST_N_2GST_N cd03041
GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed ...
1-82 1.14e-07

GST_N family, 2 repeats of the N-terminal domain of soluble GSTs (2 GST_N) subfamily; composed of uncharacterized proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains.


Pssm-ID: 239339 [Multi-domain]  Cd Length: 77  Bit Score: 47.73  E-value: 1.14e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   1 MIDLY-FAPTPNGHKITLFLEEAELDYRLIKVdlGKGGQFRPEFLRISPNNKIPAIVDhsPADGgepLSLFESGAILLYL 79
Cdd:cd03041   1 PLELYeFEGSPFCRLVREVLTELELDVILYPC--PKGSPKRDKFLEKGGKVQVPYLVD--PNTG---VQMFESADIVKYL 73

                ...
gi 16130237  80 AEK 82
Cdd:cd03041  74 FKT 76
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
141-198 2.51e-07

C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 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: 198287 [Multi-domain]  Cd Length: 117  Bit Score: 47.53  E-value: 2.51e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130237 141 YHVLNKRLENSPWLGGENYSIADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPA 198
Cdd:cd03177  47 LEFLETFLEGSDYVAGDQLTIADLSLVATVSTLEVVGFDLSKYPNVAAWYERLKALPP 104
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
4-79 4.58e-07

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: 45.75  E-value: 4.58e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130237   4 LY-FAPTPNGHKITLFLEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVdhspADGGEPLSlfESGAILLYL 79
Cdd:cd03051   3 LYdSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLE----LDDGTVIT--ESVAICRYL 73
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
4-82 9.02e-07

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 44.91  E-value: 9.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237     4 LYFAPT-PNGHKITLFLEEAELDYRLIKVDLGKGgqfRPEFLRISPNNKIPAIVDhspaDGGeplSLFESGAILLYLAEK 82
Cdd:pfam13417   1 LYGFPGsPYARRVRIALNEKGLPYEFVPIPPGDH---PPELLAKNPLGKVPVLED----DGG---ILCESLAIIDYLEEL 70
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
89-197 1.36e-06

C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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. 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: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 45.76  E-value: 1.36e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  89 HETRERAATLQWLFWQVGGLGPMLGQNHHFNHAAPQTIPYAIE------------RYQVETQRLYHVLNKRLENSPWLGG 156
Cdd:cd03189   3 PDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFFRPisrkiadkplqaFINPELKRHLDFLEDHLAKHPYFAG 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 16130237 157 ENYSIADIACWPWVNAWTRQRIDLAMYPAVKNWHERIRSRP 197
Cdd:cd03189  83 DELTAADIMMSFPLEAALARGPLLEQYPNIAAYLERIEARP 123
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
139-197 1.70e-06

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: 44.97  E-value: 1.70e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16130237   139 RLYHVLNKRLENSPWLGGENYSIADIACWPWVNAWTRQRIDL--AMYPAVKNWHERIRSRP 197
Cdd:pfam00043  33 RVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPAClrEKFPNLKAWFERVAARP 93
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
24-79 7.68e-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: 42.56  E-value: 7.68e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130237  24 LDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVdhspaDGGEPLSlfESGAILLYL 79
Cdd:cd03042  24 LDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLV-----IDGLVLT--QSLAIIEYL 72
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
129-192 5.33e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 40.00  E-value: 5.33e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16130237   129 AIERYQVETQRLYHVLNKRLENSPWLGGENYSIADIACWP---WVNAWTRQRIDLAMYPAVKNWHER 192
Cdd:pfam13410   1 ALERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPvlaRLDAAYPGLDLREGYPRLRAWLER 67
GST_N_EF1Bgamma cd03044
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ...
24-82 1.64e-04

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: 38.77  E-value: 1.64e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 16130237  24 LDYRLIKVDLGKGGqFRPEFLRISPNNKIPAIVDhspADGGeplSLFESGAILLYLAEK 82
Cdd:cd03044  24 LDVEIVDFQPGKEN-KTPEFLKKFPLGKVPAFEG---ADGF---CLFESNAIAYYVANL 75
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
93-210 1.68e-04

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) 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 thioredoxin-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 to 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. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 39.85  E-value: 1.68e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  93 ERAATLQWLFWqvgglgpmlGQNHHFNHAAPQT------IPY---AIERYQVETQRLYHVLNKRLENSPWLGGENYSIAD 163
Cdd:cd03181   1 EAAQVLQWISF---------ANSELLPAAATWVlpllgiAPYnkkAVDKAKEDLKRALGVLEEHLLTRTYLVGERITLAD 71
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 16130237 164 IAC-----WPWvnawtRQRIDLAM---YPAVKNWHERIRSRPAtgqalLKAQLGD 210
Cdd:cd03181  72 IFVasallRGF-----ETVLDPEFrkkYPNVTRWFNTVVNQPK-----FKAVFGE 116
PRK15113 PRK15113
glutathione transferase;
19-101 2.27e-04

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 40.71  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   19 LEEAELDYRLIKVDLGKGGQFRPEFLRISPNNKIPAIVDhspaDGgepLSLFESGAILLYLAEktgLFLSH--------- 89
Cdd:PRK15113  26 LQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQH----DD---FELSESSAIAEYLEE---RFAPPaweriypad 95
                         90
                 ....*....|....
gi 16130237   90 -ETRERAATLQ-WL 101
Cdd:PRK15113  96 lQARARARQIQaWL 109
GST_C_AIMP2 cd03200
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
136-189 3.64e-04

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 2 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP2, also called p38 or JTV-1, contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It plays an important role in the control of cell fate via antiproliferative (by enhancing the TGF-beta signal) and proapoptotic (activation of p53 and TNF-alpha) activities. Its roles in the control of cell proliferation and death suggest that it is a potent tumor suppressor. AIMP2 heterozygous mice with lower than normal expression of AIMP2 show high susceptibility to tumorigenesis. AIMP2 is also a substrate of Parkin, an E3 ubiquitin ligase that is involved in the ubiquitylation and proteasomal degradation of its substrates. Mutations in the Parkin gene is found in 50% of patients with autosomal-recessive early-onset parkinsonism. The accumulation of AIMP2, due to impaired Parkin function, may play a role in the pathogenesis of Parkinson's disease.


Pssm-ID: 198309 [Multi-domain]  Cd Length: 96  Bit Score: 38.27  E-value: 3.64e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 16130237 136 ETQRLYHVLNKRLENSPWLGGENYSIADIACWPWVnawtrQRIDLAM-YPA-VKNW 189
Cdd:cd03200  39 EKAAVLRALNSALGRSPWLVGSEPTVADIALWSAV-----LQTGLASgAPAnVQRW 89
GST_N_1 cd03043
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ...
17-80 3.65e-04

GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, 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: 239341 [Multi-domain]  Cd Length: 73  Bit Score: 37.96  E-value: 3.65e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16130237  17 LFLEEAELDYRLIKVDLGkGGQFRPEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLA 80
Cdd:cd03043  18 LLLKAAGIPFEEILVPLY-TPDTRARILEFSPTGKVPVLVDGG-------IVVWDSLAICEYLA 73
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
136-189 4.47e-04

Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198322 [Multi-domain]  Cd Length: 82  Bit Score: 37.68  E-value: 4.47e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 16130237 136 ETQRLYHVLNKRLENSPWLGGENYSIADIACW----PWVNAWtrQRIDLAMYPAVKNW 189
Cdd:cd10289  20 ELEALLKSLNSYLASRTFLVGYSLTLADVAVFsalyPSGQKL--SDKEKKKFPHVTRW 75
GST_C_Phi cd03187
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione ...
93-198 1.65e-03

C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity.


Pssm-ID: 198296 [Multi-domain]  Cd Length: 118  Bit Score: 37.21  E-value: 1.65e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237  93 ERAATLQWLfwQVgglgpmlgQNHHFNhaaPQTIPYAIERY--------------QVETQRLYHVLN---KRLENSPWLG 155
Cdd:cd03187   2 ERALVEQWL--EV--------EAHQFD---PPASKLVFELVfkpmlglktdeavvEENEAKLKKVLDvyeARLSKSKYLA 68
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 16130237 156 GENYSIADIACWPW----VNAWTRQRIDlaMYPAVKNWHERIRSRPA 198
Cdd:cd03187  69 GDSFTLADLSHLPNlhylMATPSKKLFD--SRPHVKAWWEDISARPA 113
GST_C_6 cd03205
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ...
130-198 4.29e-03

C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization.


Pssm-ID: 198314 [Multi-domain]  Cd Length: 109  Bit Score: 35.64  E-value: 4.29e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16130237 130 IERYQVETQRLYHVLNKRLensPWLGGENYSIADIA---CWPWVNAWTRQRIDLAMYPAVKNWHERIRSRPA 198
Cdd:cd03205  35 IERQWGKIERALDALEAEL---GDLPGGRLTLGDIAvacALGYLDFRFPELDWRAGHPALAAWFARFEARPS 103
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
4-82 4.54e-03

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: 34.61  E-value: 4.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16130237   4 LYFAPT-PNGHKITLFLEEAELDYRLIKVDLGKGGQfrpEFLRISPNNKIPAIVDHSpadggepLSLFESGAILLYLAEK 82
Cdd:cd03059   3 LYSGPDdVYSHRVRIVLAEKGVSVEIIDVDPDNPPE---DLAELNPYGTVPTLVDRD-------LVLYESRIIMEYLDER 72
 
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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