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Conserved domains on  [gi|643729338|gb|KDP37218|]
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hypothetical protein JCGZ_06274 [Jatropha curcas]

Protein Classification

glutathione S-transferase( domain architecture ID 10122769)

glutathione S-transferase (GST) catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress; such as plant tau class GSTs that are primarily responsible for herbicide detoxification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 91-214 1.12e-48

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


:

Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 155.41  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  91 PYQRAHARFWADYIDKKIYPIGRMLWASKGEVKEASKKELVQCFKILEGELAD-KPYFGGESFGYIDLALIPFSNFFYSF 169
Cdd:cd03185    1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 643729338 170 ETLG--KLSMEVECPKLLEWSKRCLQKETVSKSIADPKTVYETVLGI 214
Cdd:cd03185   81 EEVGgvKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-80 3.45e-43

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: 139.72  E-value: 3.45e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPVHKQIPVLIHNDKPICESMIIVQYIDEVW 80
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 91-214 1.12e-48

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


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 155.41  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  91 PYQRAHARFWADYIDKKIYPIGRMLWASKGEVKEASKKELVQCFKILEGELAD-KPYFGGESFGYIDLALIPFSNFFYSF 169
Cdd:cd03185    1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 643729338 170 ETLG--KLSMEVECPKLLEWSKRCLQKETVSKSIADPKTVYETVLGI 214
Cdd:cd03185   81 EEVGgvKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-80 3.45e-43

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: 139.72  E-value: 3.45e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPVHKQIPVLIHNDKPICESMIIVQYIDEVW 80
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
7-209 1.77e-42

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 142.34  E-value: 1.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDL---SNKSPLLLQMNPVHKqIPVLIHNDKPICESMIIVQYIDEVwTHK 83
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLakgEQKSPEFLALNPLGK-VPVLVDDGLVLTESLAILEYLAER-YPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  84 SPLLPSHPYQRAHARFWADYIDKKIYPIGRMLWASKG-----EVKEASKKELVQCFKILEGELADKPYFGGESFGYIDLA 158
Cdd:COG0625   80 PPLLPADPAARARVRQWLAWADGDLHPALRNLLERLApekdpAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 643729338 159 LIPFSNFFYSFetlgKLSMEvECPKLLEWSKRCLQKETVSKSIADPKTVYE 209
Cdd:COG0625  160 LAPVLRRLDRL----GLDLA-DYPNLAAWLARLAARPAFQRALAAAEPDLA 205
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 8-193 2.69e-21

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


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 87.77  E-value: 2.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338    8 ILLDLFPSPFAARVRIALAEKELQYESKQEDLSNK----SPLLLQMNPVhKQIPVLIHNDKPICESMIIVQYIDEVWThK 83
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDgeqrSPEFLALNPQ-GLVPTLDIDGEVLTQSLAIIEYLEETYP-D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338   84 SPLLPSHPYQRAHARFWADYIDKKIYPI---------GRMLWASKGEVKEASKKELVQCFKILEGELADK--PYFGGESF 152
Cdd:TIGR01262  79 PPLLPADPIKRARVRALALLIACDIHPLnnlrvlqylREKLGVEEEARNRWYQHWISKGFAALEALLQPHagRFCVGDTP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 643729338  153 GYIDLALIPfsnFFYSFETLGkLSMEvECPKLLEWSKRCLQ 193
Cdd:TIGR01262 159 TLADLCLVP---QVYNAERFG-VDLT-PYPTLRRIAAALAA 194
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 6-78 2.88e-20

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: 81.20  E-value: 2.88e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 643729338    6 QLILLDLFPSPFAARVRIALAEKELQYESKQEDLS---NKSPLLLQMNPVhKQIPVLIHNDKPICESMIIVQYIDE 78
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPL-GKVPALEDGGKKLTESRAILEYIAR 76
sspA PRK09481
stringent starvation protein A; Provisional
 12-161 3.45e-20

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 84.76  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  12 LFPSP---FAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPvHKQIPVLIHNDKPICESMIIVQYIDEVWTHkSPLLP 88
Cdd:PRK09481  13 LFSGPtdiYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPH-PPLMP 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 643729338  89 SHPYQRAHARFWADYIDKKIYPIGRMLWASKGEVKEASKKELVQCFKILEGELADKPYFGGESFGYIDLALIP 161
Cdd:PRK09481  91 VYPVARGESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVDCYLAP 163
PRK15113 PRK15113
glutathione transferase;
13-98 4.72e-09

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 54.19  E-value: 4.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  13 FPSPFAARVRIALAEKELQYESKQEDLSNKSplllQMNPVHKQ------IPVLIHNDKPICESMIIVQYIDEVW--THKS 84
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFELKTVDLDAGE----HLQPTYQGysltrrVPTLQHDDFELSESSAIAEYLEERFapPAWE 89

                         90
                 ....*....|....
gi 643729338  85 PLLPSHPYQRAHAR 98
Cdd:PRK15113  90 RIYPADLQARARAR 103
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 122-190 3.03e-07

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 46.16  E-value: 3.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 643729338  122 VKEASKKELVQCFKILEGELADKPYFGGESFGYIDLALIPFsnFFYSFETLGKLSMEVECPKLLEWSKR 190
Cdd:pfam13410   1 ALERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPV--LARLDAAYPGLDLREGYPRLRAWLER 67
 
Name Accession Description Interval E-value
GST_C_Tau cd03185
C-terminal, alpha helical domain of Class Tau Glutathione S-transferases; Glutathione ...
 91-214 1.12e-48

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


Pssm-ID: 198294 [Multi-domain]  Cd Length: 127  Bit Score: 155.41  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  91 PYQRAHARFWADYIDKKIYPIGRMLWASKGEVKEASKKELVQCFKILEGELAD-KPYFGGESFGYIDLALIPFSNFFYSF 169
Cdd:cd03185    1 PYERAQARFWAAYIDDKLFPAGRKVWAAKGEEQEKAVEEALEALKVLEEELKGgKPFFGGDTIGYLDIALGSFLGWFKAI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 643729338 170 ETLG--KLSMEVECPKLLEWSKRCLQKETVSKSIADPKTVYETVLGI 214
Cdd:cd03185   81 EEVGgvKLLDEEKFPLLAAWAERFLEREAVKEVLPDRDKLVEFLKAL 127
GST_N_Tau cd03058
GST_N family, Class Tau subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-80 3.45e-43

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: 139.72  E-value: 3.45e-43
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPVHKQIPVLIHNDKPICESMIIVQYIDEVW 80
Cdd:cd03058    1 VKLLGAWASPFVLRVRIALALKGVPYEYVEEDLGNKSELLLASNPVHKKIPVLLHNGKPICESLIIVEYIDEAW 74
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
7-209 1.77e-42

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 142.34  E-value: 1.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDL---SNKSPLLLQMNPVHKqIPVLIHNDKPICESMIIVQYIDEVwTHK 83
Cdd:COG0625    2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLakgEQKSPEFLALNPLGK-VPVLVDDGLVLTESLAILEYLAER-YPE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  84 SPLLPSHPYQRAHARFWADYIDKKIYPIGRMLWASKG-----EVKEASKKELVQCFKILEGELADKPYFGGESFGYIDLA 158
Cdd:COG0625   80 PPLLPADPAARARVRQWLAWADGDLHPALRNLLERLApekdpAAIARARAELARLLAVLEARLAGGPYLAGDRFSIADIA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 643729338 159 LIPFSNFFYSFetlgKLSMEvECPKLLEWSKRCLQKETVSKSIADPKTVYE 209
Cdd:COG0625  160 LAPVLRRLDRL----GLDLA-DYPNLAAWLARLAARPAFQRALAAAEPDLA 205
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 8-193 2.69e-21

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


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 87.77  E-value: 2.69e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338    8 ILLDLFPSPFAARVRIALAEKELQYESKQEDLSNK----SPLLLQMNPVhKQIPVLIHNDKPICESMIIVQYIDEVWThK 83
Cdd:TIGR01262   1 KLYSYWRSSCSYRVRIALALKGIDYEYVPVNLLRDgeqrSPEFLALNPQ-GLVPTLDIDGEVLTQSLAIIEYLEETYP-D 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338   84 SPLLPSHPYQRAHARFWADYIDKKIYPI---------GRMLWASKGEVKEASKKELVQCFKILEGELADK--PYFGGESF 152
Cdd:TIGR01262  79 PPLLPADPIKRARVRALALLIACDIHPLnnlrvlqylREKLGVEEEARNRWYQHWISKGFAALEALLQPHagRFCVGDTP 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 643729338  153 GYIDLALIPfsnFFYSFETLGkLSMEvECPKLLEWSKRCLQ 193
Cdd:TIGR01262 159 TLADLCLVP---QVYNAERFG-VDLT-PYPTLRRIAAALAA 194
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 6-78 2.88e-20

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: 81.20  E-value: 2.88e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 643729338    6 QLILLDLFPSPFAARVRIALAEKELQYESKQEDLS---NKSPLLLQMNPVhKQIPVLIHNDKPICESMIIVQYIDE 78
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGagpEKSPELLKLNPL-GKVPALEDGGKKLTESRAILEYIAR 76
sspA PRK09481
stringent starvation protein A; Provisional
 12-161 3.45e-20

stringent starvation protein A; Provisional


Pssm-ID: 236537 [Multi-domain]  Cd Length: 211  Bit Score: 84.76  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  12 LFPSP---FAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPvHKQIPVLIHNDKPICESMIIVQYIDEVWTHkSPLLP 88
Cdd:PRK09481  13 LFSGPtdiYSHQVRIVLAEKGVSVEIEQVEKDNLPQDLIDLNP-YQSVPTLVDRELTLYESRIIMEYLDERFPH-PPLMP 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 643729338  89 SHPYQRAHARFWADYIDKKIYPIGRMLWASKGEVKEASKKELVQCFKILEGELADKPYFGGESFGYIDLALIP 161
Cdd:PRK09481  91 VYPVARGESRLMMHRIEKDWYSLMNKIVNGSASEADAARKQLREELLAIAPVFGEKPYFMSEEFSLVDCYLAP 163
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 7-77 9.14e-17

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: 71.83  E-value: 9.14e-17
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDLSNKSPL-LLQMNPvHKQIPVLIHNDKPICESMIIVQYID 77
Cdd:cd00570    1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEeFLALNP-LGKVPVLEDGGLVLTESLAILEYLA 71
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 97-191 4.98e-13

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: 62.90  E-value: 4.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  97 ARFWADYIDKKIYPIGR-------MLWASKGEVKEASKKELVQCFKILEGELADKPYFGGESFGYIDLALIPFsnFFYSF 169
Cdd:cd00299    1 VRALEDWADATLAPPLVrllylekVPLPKDEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPV--LARLE 78

                         90       100
                 ....*....|....*....|..
gi 643729338 170 ETLGKLSMEVECPKLLEWSKRC 191
Cdd:cd00299   79 ALGPYYDLLDEYPRLKAWYDRL 100
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 7-77 6.20e-13

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: 61.82  E-value: 6.20e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDLSN---KSPLLLQMNPVhKQIPVLIHNDKPICESMIIVQYID 77
Cdd:cd03042    1 MILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKgeqLSPAYRALNPQ-GLVPTLVIDGLVLTQSLAIIEYLD 73
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 15-78 9.61e-13

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 61.11  E-value: 9.61e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 643729338   15 SPFAARVRIALAEKELQYESKQEDL--SNKSPLLLQMNPVHKqIPVL-IHNDKPICESMIIVQYIDE 78
Cdd:pfam13409   2 SPFSHRVRLALEEKGLPYEIELVDLdpKDKPPELLALNPLGT-VPVLvLPDGTVLTDSLVILEYLEE 67
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
15-78 1.07e-12

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 61.09  E-value: 1.07e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643729338   15 SPFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPVHKqIPVLIHNDKPICESMIIVQYIDE 78
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVPIPPGDHPPELLAKNPLGK-VPVLEDDGGILCESLAIIDYLEE 69
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 16-78 1.07e-11

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: 58.49  E-value: 1.07e-11
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 643729338  16 PFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPVHkQIPVLIHNDKPICESMIIVQYIDE 78
Cdd:cd03059   10 VYSHRVRIVLAEKGVSVEIIDVDPDNPPEDLAELNPYG-TVPTLVDRDLVLYESRIIMEYLDE 71
PLN02395 PLN02395
glutathione S-transferase
 12-199 4.86e-10

glutathione S-transferase


Pssm-ID: 166036 [Multi-domain]  Cd Length: 215  Bit Score: 57.18  E-value: 4.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  12 LFPSPfaARVRIALAEKELQYESKQEDL---SNKSPLLLQMNPVHKqIPVLIHNDKPICESMIIVQYIDEVWTHKSP-LL 87
Cdd:PLN02395   9 AFASP--KRALVTLIEKGVEFETVPVDLmkgEHKQPEYLALQPFGV-VPVIVDGDYKIFESRAIMRYYAEKYRSQGPdLL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  88 PSHPYQRAHARFWADYIDKKIYP-----IGRMLWASK------GEVKEASKKELVQCFKILEGELADKPYFGGESFGYID 156
Cdd:PLN02395  86 GKTIEERGQVEQWLDVEATSYHPpllnlTLHILFASKmgfpadEKVIKESEEKLAKVLDVYEARLSKSKYLAGDFVSLAD 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 643729338 157 LALIPFSNffYSFETLGKLSMEVECPKLLEW----SKRCLQKETVSK 199
Cdd:PLN02395 166 LAHLPFTE--YLVGPIGKAYLIKDRKHVSAWwddiSSRPAWKEVLAK 210
GST_N_3 cd03049
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ...
 15-77 2.13e-09

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: 52.26  E-value: 2.13e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 643729338  15 SPFAARVRIALAEKEL--QYESKQEDLSNKSPLLLQMNPVHKqIPVLIHND-KPICESMIIVQYID 77
Cdd:cd03049    9 SPYVRKVRVAAHETGLgdDVELVLVNPWSDDESLLAVNPLGK-IPALVLDDgEALFDSRVICEYLD 73
GST_C_Omega cd03184
C-terminal, alpha helical domain of Class Omega Glutathione S-transferases; Glutathione ...
 92-206 2.44e-09

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: 53.48  E-value: 2.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  92 YQRAHARFWADYIDKKIYPIGRMLwaSKGEVKEASKKELVQCFKILEGELADK--PYFGGESFGYIDLALIPFsnfFYSF 169
Cdd:cd03184    1 YEKAQQKMLIERFSKVPSAFYKFL--RSGEDRKGLKEELRSALENLEEELAKRgtPFFGGNSPGMVDYMIWPW---FERL 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 643729338 170 ETLGKLSMEVEC----PKLLEWSKRCLQKETVSKSIADPKT 206
Cdd:cd03184   76 EALKLLDGYELCldrfPKLKKWMAAMKQDPAVKAFYTDPET 116
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 7-77 3.30e-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: 51.91  E-value: 3.30e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDL---SNKSPLLLQMNPvHKQIPVLIHND-KPICESMIIVQYID 77
Cdd:cd03051    1 MKLYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLaagEQRSPEFLAKNP-AGTVPVLELDDgTVITESVAICRYLE 74
PRK15113 PRK15113
glutathione transferase;
13-98 4.72e-09

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 54.19  E-value: 4.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  13 FPSPFAARVRIALAEKELQYESKQEDLSNKSplllQMNPVHKQ------IPVLIHNDKPICESMIIVQYIDEVW--THKS 84
Cdd:PRK15113  14 FFSPYVMSAFVALQEKGLPFELKTVDLDAGE----HLQPTYQGysltrrVPTLQHDDFELSESSAIAEYLEERFapPAWE 89

                         90
                 ....*....|....
gi 643729338  85 PLLPSHPYQRAHAR 98
Cdd:PRK15113  90 RIYPADLQARARAR 103
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 13-78 6.53e-09

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: 51.11  E-value: 6.53e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 643729338  13 FPSPFAARVRIALAEKELQYESKQEDLS---NKSPLLLQMNPVhKQIPVLIHNDKPICESMIIVQYIDE 78
Cdd:cd03053    8 AMSTCVRRVLLCLEEKGVDYELVPVDLTkgeHKSPEHLARNPF-GQIPALEDGDLKLFESRAITRYLAE 75
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 16-207 6.69e-09

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 54.61  E-value: 6.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  16 PFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPVHKqIPVLIHNDKPICESMIIVQYIDEvwTHKSPLLPSHPYQRA 95
Cdd:PLN02817  74 PFCQRVLLTLEEKHLPYDMKLVDLTNKPEWFLKISPEGK-VPVVKLDEKWVADSDVITQALEE--KYPDPPLATPPEKAS 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  96 harfwadyIDKKIYPIGRMLWASKgEVKEASKKELVQCFKILEGELADK-PYFGGESFGYIDLALIPfsnFFYSFE-TLG 173
Cdd:PLN02817 151 --------VGSKIFSTFIGFLKSK-DPGDGTEQALLDELTSFDDYIKENgPFINGEKISAADLSLGP---KLYHLEiALG 218

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 643729338 174 ---KLSMEVECPKLLEWSKRCLQKETVSKSIADPKTV 207
Cdd:PLN02817 219 hykNWSVPDSLPFVKSYMKNIFSMESFVKTRALPEDV 255
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 122-190 3.03e-07

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 46.16  E-value: 3.03e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 643729338  122 VKEASKKELVQCFKILEGELADKPYFGGESFGYIDLALIPFsnFFYSFETLGKLSMEVECPKLLEWSKR 190
Cdd:pfam13410   1 ALERAREQLRAALDALEARLADGPGLLGDRPTLADIALAPV--LARLDAAYPGLDLREGYPRLRAWLER 67
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 99-195 7.52e-07

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: 45.74  E-value: 7.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338   99 FWADYIDKKIYPIGRMLWASKGEVKEASKKELVQcFKILEGELADKPYFGGESFGYIDLALIPFsnFFYSFETLGKLSME 178
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPEVDEALEKVARV-LSALEEVLKGQTYLVGDKLTLADIALAPA--LLWLYELDPACLRE 77

                          90
                  ....*....|....*..
gi 643729338  179 vECPKLLEWSKRCLQKE 195
Cdd:pfam00043  78 -KFPNLKAWFERVAARP 93
PLN02378 PLN02378
glutathione S-transferase DHAR1
 16-161 1.17e-06

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 47.40  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  16 PFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPVHKqIPVLIHNDKPICESMIIVQYIDEvwthKSPllpsHPYQRA 95
Cdd:PLN02378  21 PFSQRALLTLEEKSLTYKIHLINLSDKPQWFLDISPQGK-VPVLKIDDKWVTDSDVIVGILEE----KYP----DPPLKT 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 643729338  96 HARFWAdyIDKKIYPIGRMLWASKgEVKEASKKELVQCFKILEGELA--DKPYFGGESFGYIDLALIP 161
Cdd:PLN02378  92 PAEFAS--VGSNIFGTFGTFLKSK-DSNDGSEHALLVELEALENHLKshDGPFIAGERVSAVDLSLAP 156
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 16-77 1.18e-06

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: 45.42  E-value: 1.18e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 643729338  16 PFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPVHKqIPVL-IHNDKPICESMIIVQYID 77
Cdd:cd03055   28 PYAQRARLVLAAKNIPHEVININLKDKPDWFLEKNPQGK-VPALeIDEGKVVYESLIICEYLD 89
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 18-76 4.72e-06

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


Pssm-ID: 239344 [Multi-domain]  Cd Length: 76  Bit Score: 43.26  E-value: 4.72e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 643729338  18 AARVRIALAEKELQYESK---QEDLSNKSPLLLQMNPvHKQIPVLIHNDKPICESMIIVQYI 76
Cdd:cd03046   11 SFRILWLLEELGLPYELVlydRGPGEQAPPEYLAINP-LGKVPVLVDGDLVLTESAAIILYL 71
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 15-75 2.17e-05

GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Delta and Epsilon subfamily is made up primarily of insect GSTs, which play major roles in insecticide resistance by facilitating reductive dehydrochlorination of insecticides or conjugating them with GSH to produce water-soluble metabolites that are easily excreted. They are also implicated in protection against cellular damage by oxidative stress.


Pssm-ID: 239343 [Multi-domain]  Cd Length: 74  Bit Score: 41.44  E-value: 2.17e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643729338  15 SPFAARVRIALAEKELQYESKQEDLSNK---SPLLLQMNPVHkQIPVLIHNDKPICESMIIVQY 75
Cdd:cd03045    9 SPPCRAVLLTAKALGLELNLKEVNLMKGehlKPEFLKLNPQH-TVPTLVDNGFVLWESHAILIY 71
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 121-197 2.18e-05

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: 42.31  E-value: 2.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 643729338 121 EVKEASKKELVQCFKILEGELADKPYFGGESFGYIDLALIPFSNffysFETLGKLSMEVECPKLLEWSKRCLQKETV 197
Cdd:cd03182   44 EWGERNKKRVIDFLPVLDKRLAESPYVAGDRFSIADITAFVALD----FAKNLKLPVPEELTALRRWYERMAARPSA 116
GST_N_GDAP1 cd03052
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ...
 7-77 3.11e-05

GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; GDAP1 was originally identified as a highly expressed gene at the differentiated stage of GD3 synthase-transfected cells. More recently, mutations in GDAP1 have been reported to cause both axonal and demyelinating autosomal-recessive Charcot-Marie-Tooth (CMT) type 4A neuropathy. CMT is characterized by slow and progressive weakness and atrophy of muscles. Sequence analysis of GDAP1 shows similarities and differences with GSTs; it appears to contain both N-terminal TRX-fold and C-terminal alpha helical domains of GSTs, however, it also contains additional C-terminal transmembrane domains unlike GSTs. GDAP1 is mainly expressed in neuronal cells and is localized in the mitochondria through its transmembrane domains. It does not exhibit GST activity using standard substrates.


Pssm-ID: 239350 [Multi-domain]  Cd Length: 73  Bit Score: 40.99  E-value: 3.11e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDL---SNKSPLLLQMNPVhKQIPVLIHNDKPICESMIIVQYID 77
Cdd:cd03052    1 LVLYHWTQSFSSQKVRLVIAEKGLRCEEYDVSLplsEHNEPWFMRLNPT-GEVPVLIHGDNIICDPTQIIDYLE 73
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 7-75 4.10e-05

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: 40.64  E-value: 4.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 643729338   7 LILLDLFPSPFAARVRIALAEKELQYESKQEDLSN---KSPLLLQMNPvHKQIPVLIHNDKPICESMIIVQY 75
Cdd:cd03056    1 MKLYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKgetRTPEFLALNP-NGEVPVLELDGRVLAESNAILVY 71
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 47-178 1.13e-04

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 41.59  E-value: 1.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  47 LQMNPvHKQIPVLIHNDKPI-CESMIIVQYIDEVWTHKSPLLPSHPYQRAHARFWADYIDKKIYPIGRMLWASKG--EVK 123
Cdd:PRK10542  44 LAINP-KGQVPALLLDDGTLlTEGVAIMQYLADSVPDRQLLAPVGSLSRYHTIEWLNYIATELHKGFTPLFRPDTpeEYK 122

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 643729338 124 EASKKELVQCFKILEGELADKPYFGGESFGYIDLALIPFSNFFYSFetlgKLSME 178
Cdd:PRK10542 123 PTVRAQLEKKFQYVDEALADEQWICGQRFTIADAYLFTVLRWAYAV----KLNLE 173
GST_N_Omega_like cd03060
GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to ...
 16-75 1.44e-04

GST_N family, Omega-like subfamily; composed of uncharacterized proteins with similarity to class Omega GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. Like Omega enzymes, proteins in this subfamily contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism.


Pssm-ID: 239358 [Multi-domain]  Cd Length: 71  Bit Score: 38.88  E-value: 1.44e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 643729338  16 PFAARVRIALAEKELQYESKQEDLSNKSPLLLQMNPvHKQIPVLI-HNDKPICESMIIVQY 75
Cdd:cd03060   10 PYAMRARMALLLAGITVELREVELKNKPAEMLAASP-KGTVPVLVlGNGTVIEESLDIMRW 69
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 94-159 3.01e-04

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: 39.15  E-value: 3.01e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643729338  94 RAHARFWADYIDKKIYPIGRMLW--------ASKGEVKEASKKELVQCFKILEGELADKPYFGGESFGYIDLAL 159
Cdd:cd03188    3 RARLLEWLNFIASELHKAFGPLFyparwaddALAEEVKAAARERLERRLAYLDAQLAGGPYLLGDQFSVADAYL 76
GST_C_SspA cd03186
C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase ...
 91-201 4.50e-04

C-terminal, alpha helical domain of Stringent starvation protein A; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-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: 198295 [Multi-domain]  Cd Length: 108  Bit Score: 38.42  E-value: 4.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  91 PYQRAHARFWADYIDKKIYP-IGRMLWASKGEVKEASKKELVQCFKILEGELADKPYFGGESFGYIDLALIPFsnffysf 169
Cdd:cd03186    1 PVSRARSRLMMHRIEQDWYPlLDTILNGRDEKEAEKARKELRESLTALAPVFAASPYFLSEEFSLVDCYLAPL------- 73

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 643729338 170 etLGKL-SMEVECPK----LLEWSKRCLQKETVSKSI 201
Cdd:cd03186   74 --LWRLpALGIELPKqakaIKDYMERVFARDSFQASL 108
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 124-159 4.94e-04

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: 38.41  E-value: 4.94e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 643729338 124 EASKKELVQCFKILEGELADKPYFGGESFGYIDLAL 159
Cdd:cd03180   42 AASLAACNKLMAILDAQLARQAYLAGDRFTLADIAL 77
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 13-78 7.98e-04

GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related GSTs. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The N-terminal TRX-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. Characterized GSTs in this subfamily include Aspergillus fumigatus GSTs 1 and 2, and Schizosaccharomyces pombe GST-I. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes.


Pssm-ID: 239346 [Multi-domain]  Cd Length: 81  Bit Score: 37.14  E-value: 7.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 643729338  13 FPSPFAARVRIALAEKELQYESKQEDLS---NKSPLLLQMNPvHKQIPVLI-HNDKPIC--ESMIIVQYIDE 78
Cdd:cd03048    7 HGTPNGFKVSIMLEELGLPYEIHPVDISkgeQKKPEFLKINP-NGRIPAIVdHNGTPLTvfESGAILLYLAE 77
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 93-205 5.02e-03

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: 35.61  E-value: 5.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643729338  93 QRAHARFWADYIDKKIYP---------IGRMLwASKGEVKEAsKKELVQCFKILEGELADKPYFGGESFGYIDLALipFS 163
Cdd:cd03181    1 EAAQVLQWISFANSELLPaaatwvlplLGIAP-YNKKAVDKA-KEDLKRALGVLEEHLLTRTYLVGERITLADIFV--AS 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 643729338 164 NFFYSFETLGKLSMEVECPKLLEWSKRCLQKETVSKSIADPK 205
Cdd:cd03181   77 ALLRGFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVK 118
 
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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