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Conserved domains on  [gi|1974787772|emb|CAE3747316|]
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unnamed protein product, partial [Bigelowiella natans]

Protein Classification

glutathione S-transferase N-terminal domain-containing protein( domain architecture ID 10599306)

glutathione S-transferase (GST) N-terminal domain-containing protein belongs to the GST family, 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

PubMed:  9074797|15822171|11695986
SCOP:  4000472

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 84-150 9.72e-20

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


:

Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 78.44  E-value: 9.72e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974787772  84 WCPYCQKIWLWLEEMKIPYKVVKVTMfCYGKKENWYLSRVPSGMLPALEL-DGKIITESDVILETLEE 150
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEE 67
 
Name Accession Description Interval E-value
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 84-150 9.72e-20

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 78.44  E-value: 9.72e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974787772  84 WCPYCQKIWLWLEEMKIPYKVVKVTMfCYGKKENWYLSRVPSGMLPALEL-DGKIITESDVILETLEE 150
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEE 67
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
82-184 2.25e-18

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 78.78  E-value: 2.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974787772  82 HAWCPYCQKIWLWLEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEFGPlhrgmnd 161
Cdd:COG0625     7 SPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPE------- 79

                          90       100
                  ....*....|....*....|....*....
gi 1974787772 162 ssvykcRKL------ERVLFRAWCMWLCS 184
Cdd:COG0625    80 ------PPLlpadpaARARVRQWLAWADG 102
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 82-149 3.29e-18

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


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 74.53  E-value: 3.29e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974787772  82 HAWCPYCQKIWLWLEEMKIPYKVVKVTMFcyGKKENWYLSRVPSGMLPALELDGKIITESDVILETLE 149
Cdd:cd00570     6 FPGSPRSLRVRLALEEKGLPYELVPVDLG--EGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 80-152 5.10e-13

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 65.40  E-value: 5.10e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974787772  80 DKHAWCPYCQKIWLWLEEMKIPYKVVKVTMfcyGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEF 152
Cdd:PLN02817   68 NKLGDCPFCQRVLLTLEEKHLPYDMKLVDL---TNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKY 137
 
Name Accession Description Interval E-value
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 84-150 9.72e-20

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 78.44  E-value: 9.72e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974787772  84 WCPYCQKIWLWLEEMKIPYKVVKVTMfCYGKKENWYLSRVPSGMLPALEL-DGKIITESDVILETLEE 150
Cdd:pfam13409   1 FSPFSHRVRLALEEKGLPYEIELVDL-DPKDKPPELLALNPLGTVPVLVLpDGTVLTDSLVILEYLEE 67
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
82-184 2.25e-18

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 78.78  E-value: 2.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974787772  82 HAWCPYCQKIWLWLEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEFGPlhrgmnd 161
Cdd:COG0625     7 SPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGLVLTESLAILEYLAERYPE------- 79

                          90       100
                  ....*....|....*....|....*....
gi 1974787772 162 ssvykcRKL------ERVLFRAWCMWLCS 184
Cdd:COG0625    80 ------PPLlpadpaARARVRQWLAWADG 102
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 82-149 3.29e-18

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


Pssm-ID: 238319 [Multi-domain]  Cd Length: 71  Bit Score: 74.53  E-value: 3.29e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974787772  82 HAWCPYCQKIWLWLEEMKIPYKVVKVTMFcyGKKENWYLSRVPSGMLPALELDGKIITESDVILETLE 149
Cdd:cd00570     6 FPGSPRSLRVRLALEEKGLPYELVPVDLG--EGEQEEFLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
85-154 1.92e-16

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 70.33  E-value: 1.92e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974787772  85 CPYCQKIWLWLEEMKIPYKVVKVTmfcYGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEFGP 154
Cdd:pfam13417   7 SPYARRVRIALNEKGLPYEFVPIP---PGDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPG 73
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 80-152 5.10e-13

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 65.40  E-value: 5.10e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974787772  80 DKHAWCPYCQKIWLWLEEMKIPYKVVKVTMfcyGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEF 152
Cdd:PLN02817   68 NKLGDCPFCQRVLLTLEEKHLPYDMKLVDL---TNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKY 137
GST_N_Omega cd03055
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 85-149 1.69e-10

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: 55.05  E-value: 1.69e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1974787772  85 CPYCQKIWLWLEEMKIPYKVVKVTMfcyGKKENWYLSRVPSGMLPALELD-GKIITESDVILETLE 149
Cdd:cd03055    27 CPYAQRARLVLAAKNIPHEVININL---KDKPDWFLEKNPQGKVPALEIDeGKVVYESLIICEYLD 89
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 88-148 7.86e-10

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: 52.96  E-value: 7.86e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1974787772  88 CQKIWLWLEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPALELDGKIITESDVILETL 148
Cdd:cd03056    12 CYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72
GST_N_Metaxin_like cd03080
GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, ...
 81-153 2.79e-09

GST_N family, Metaxin subfamily, Metaxin-like proteins; a heterogenous group of proteins, predominantly uncharacterized, with similarity to metaxins and GSTs. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. One characterized member of this subgroup is a novel GST from Rhodococcus with toluene o-monooxygenase and gamma-glutamylcysteine synthetase activities. Also members are the cadmium-inducible lysosomal protein CDR-1 and its homologs from C. elegans, and the failed axon connections (fax) protein from Drosophila. CDR-1 is an integral membrane protein that functions to protect against cadmium toxicity and may also have a role in osmoregulation to maintain salt balance in C. elegans. The fax gene of Drosophila was identified as a genetic modifier of Abelson (Abl) tyrosine kinase. The fax protein is localized in cellular membranes and is expressed in embryonic mesoderm and axons of the central nervous system.


Pssm-ID: 239378 [Multi-domain]  Cd Length: 75  Bit Score: 51.47  E-value: 2.79e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974787772  81 KHAWCPYCQKIWLWLEEMKIPYKVvkvtmfcygkKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEFG 153
Cdd:cd03080    13 VPSLSPFCLKVETFLRMAGIPYEN----------KFGGLAKRSPKGKLPFIELNGEKIADSELIIDHLEEKYG 75
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 91-153 8.71e-09

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: 50.19  E-value: 8.71e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1974787772  91 IWLwLEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEFG 153
Cdd:cd03046    15 LWL-LEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDLVLTESAAIILYLAEKYG 76
GST_N_Metaxin cd03054
GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a ...
 76-151 1.23e-08

GST_N family, Metaxin subfamily; composed of metaxins and related proteins. Metaxin 1 is a component of a preprotein import complex of the mitochondrial outer membrane. It extends to the cytosol and is anchored to the mitochondrial membrane through its C-terminal domain. In mice, metaxin is required for embryonic development. In humans, alterations in the metaxin gene may be associated with Gaucher disease. Metaxin 2 binds to metaxin 1 and may also play a role in protein translocation into the mitochondria. Genome sequencing shows that a third metaxin gene also exists in zebrafish, Xenopus, chicken and mammals. Sequence analysis suggests that all three metaxins share a common ancestry and that they possess similarity to GSTs. Also included in the subfamily are uncharacterized proteins with similarity to metaxins, including a novel GST from Rhodococcus with toluene o-monooxygenase and glutamylcysteine synthetase activities.


Pssm-ID: 239352 [Multi-domain]  Cd Length: 72  Bit Score: 49.53  E-value: 1.23e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974787772  76 TFYRDKHA--WCPYCQKIWLWLEEMKIPYKVVkvtmfcygkkENWYLSRVPSGMLPALELDGKIITESDVILETLEEE 151
Cdd:cd03054     5 QWGRAFGLpsLSPECLKVETYLRMAGIPYEVV----------FSSNPWRSPTGKLPFLELNGEKIADSEKIIEYLKKK 72
PLN02378 PLN02378
glutathione S-transferase DHAR1
 85-152 1.62e-08

glutathione S-transferase DHAR1


Pssm-ID: 166019 [Multi-domain]  Cd Length: 213  Bit Score: 52.41  E-value: 1.62e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974787772  85 CPYCQKIWLWLEEMKIPYKVVKVTMfcyGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEF 152
Cdd:PLN02378   20 CPFSQRALLTLEEKSLTYKIHLINL---SDKPQWFLDISPQGKVPVLKIDDKWVTDSDVIVGILEEKY 84
GST_N_4 pfam17172
Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.
 86-184 8.96e-08

Glutathione S-transferase N-terminal domain; This domain is homologous to pfam02798.


Pssm-ID: 465370 [Multi-domain]  Cd Length: 97  Bit Score: 47.96  E-value: 8.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974787772  86 PYCQKIWLWLEEMKIPYKVVkvtmfcygkkENWYLSRVPSGMLPALELDGKIITESDVILETLEEEFGPLHRGMN----- 160
Cdd:pfam17172   1 PFCLKVETYLRMAGIPYEVE----------PSSNPSASPKGKLPFIELNGDLIADSEFIIEFLKEKGVDLDAGLSpeqka 70

                          90       100
                  ....*....|....*....|....*.
gi 1974787772 161 DSSVYKcRKLERVLFRAW--CMWLCS 184
Cdd:pfam17172  71 DARALK-ALVEEHLYWALlyERWLDP 95
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 83-149 3.90e-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: 3.90e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1974787772  83 AWCPYCQKIWLWLEEMKIPYKVVKVTmfcYGKKEN---WYLSRVPSGMLPALEL-DGKIITESDVILETLE 149
Cdd:cd03051     7 PTAPNPRRVRIFLAEKGIDVPLVTVD---LAAGEQrspEFLAKNPAGTVPVLELdDGTVITESVAICRYLE 74
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 92-150 1.88e-06

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: 43.83  E-value: 1.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1974787772  92 WLwLEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEE 150
Cdd:pfam02798  19 WL-LAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 82-150 1.73e-05

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: 41.10  E-value: 1.73e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1974787772  82 HAWCPYCQKIWLWLEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEE 150
Cdd:cd03053     7 AAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGDLKLFESRAITRYLAE 75
GST_N_Beta cd03057
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 95-145 2.06e-05

GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH.


Pssm-ID: 239355 [Multi-domain]  Cd Length: 77  Bit Score: 40.98  E-value: 2.06e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1974787772  95 LEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPALEL-DGKIITESDVIL 145
Cdd:cd03057    18 LEELGLPFELVRVDLRTKTQKGADYLAINPKGQVPALVLdDGEVLTESAAIL 69
GST_N_Ure2p_like cd03048
GST_N family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p and related ...
 90-154 1.33e-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: 39.06  E-value: 1.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1974787772  90 KIWLWLEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPAL---ELDGKIITESDVILETLEEEFGP 154
Cdd:cd03048    14 KVSIMLEELGLPYEIHPVDISKGEQKKPEFLKINPNGRIPAIvdhNGTPLTVFESGAILLYLAEKYDK 81
GST_N_mPGES2 cd03040
GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a ...
 75-150 1.82e-04

GST_N family; microsomal Prostaglandin E synthase Type 2 (mPGES2) subfamily; mPGES2 is a membrane-anchored dimeric protein containing a CXXC motif which catalyzes the isomerization of PGH2 to PGE2. Unlike cytosolic PGE synthase (cPGES) and microsomal PGES Type 1 (mPGES1), mPGES2 does not require glutathione (GSH) for its activity, although its catalytic rate is increased two- to four-fold in the presence of DTT, GSH or other thiol compounds. PGE2 is widely distributed in various tissues and is implicated in the sleep/wake cycle, relaxation/contraction of smooth muscle, excretion of sodium ions, maintenance of body temperature and mediation of inflammation. mPGES2 contains an N-terminal hydrophobic domain which is membrane associated, and a C-terminal soluble domain with a GST-like structure.


Pssm-ID: 239338  Cd Length: 77  Bit Score: 38.54  E-value: 1.82e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1974787772  75 VTFYRDKHawCPYCQKIWLWLEEMKIPYKVVKVT-MFcygKKE-NWYLSR-VPSgMLPALELDGKIITESDVILETLEE 150
Cdd:cd03040     2 ITLYQYKT--CPFCCKVRAFLDYHGIPYEVVEVNpVS---RKEiKWSSYKkVPI-LRVESGGDGQQLVDSSVIISTLKT 74
PRK15113 PRK15113
glutathione transferase;
74-154 4.56e-04

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 39.56  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1974787772  74 RVTFYRDKHAWCPYCQKIWLWLEEMKIPYKVVKVTMFCYGKKENWYLSRVPSGMLPALELDGKIITESDVILETLEEEFG 153
Cdd:PRK15113    5 AITLYSDAHFFSPYVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFA 84


                  .
gi 1974787772 154 P 154
Cdd:PRK15113   85 P 85
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 119-149 6.89e-04

GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Zeta GSTs, also known as maleylacetoacetate (MAA) isomerases, catalyze the isomerization of MAA to fumarylacetoacetate, the penultimate step in tyrosine/phenylalanine catabolism, using GSH as a cofactor. They show little GSH-conjugating activity towards traditional GST substrates but display modest GSH peroxidase activity. They are also implicated in the detoxification of the carcinogen dichloroacetic acid by catalyzing its dechlorination to glyoxylic acid.


Pssm-ID: 239340 [Multi-domain]  Cd Length: 73  Bit Score: 36.78  E-value: 6.89e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1974787772 119 YLSRVPSGMLPALELDGKIITESDVILETLE 149
Cdd:cd03042    43 YRALNPQGLVPTLVIDGLVLTQSLAIIEYLD 73
GrxC COG0695
Glutaredoxin [Posttranslational modification, protein turnover, chaperones];
74-108 2.38e-03

Glutaredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440459 [Multi-domain]  Cd Length: 74  Bit Score: 35.17  E-value: 2.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1974787772  74 RVTFY-RDkhaWCPYCQKIWLWLEEMKIPYKVVKVT 108
Cdd:COG0695     1 KVTLYtTP---GCPYCARAKRLLDEKGIPYEEIDVD 33
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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