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Conserved domains on  [gi|30581160|ref|NP_076939|]
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ganglioside-induced differentiation-associated protein 1-like 1 isoform 2 [Homo sapiens]

Protein Classification

ganglioside-induced differentiation-associated family protein( domain architecture ID 10122725)

ganglioside-induced differentiation-associated protein (GDAP) such as GDAP1 and GDAP1-like 1 (GDAP1L1), which are glutathione S-transferase (GST) family proteins that do not possess GSH-conjugating activity using standard substrates

CATH:  3.40.30.10|1.20.1050.10
PubMed:  14595091|9074797|15822171|15607001
SCOP:  4000472|4000976

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_family super family cl02776
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 201-311 6.55e-78

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.


The actual alignment was detected with superfamily member cd10302:

Pssm-ID: 470672  Cd Length: 111  Bit Score: 234.90  E-value: 6.55e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 201 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 280
Cdd:cd10302   1 PQLTEPYLSKQKKLMAKILEHDNVNYLKKILGELAMVLDQIEAELEKRKLEYEGQKCELWLCGCIFTLADVLLGATLHRL 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 30581160 281 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 311
Cdd:cd10302  81 KFLGLSKKYWEDGSRPNLQSFFERVQKRYAF 111
GST_N_GDAP1 cd03052
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ...
 47-119 8.17e-46

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: 151.16  E-value: 8.17e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVE 119
Cdd:cd03052   1 LVLYHWTQSFSSQKVRLVIAEKGLRCEEYDVSLPLSEHNEPWFMRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73
 
Name Accession Description Interval E-value
GST_C_GDAP1L1 cd10302
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein ...
 201-311 6.55e-78

C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1-like 1; Glutathione S-transferase (GST) C-terminal domain family, Ganglioside-induced differentiation-associated protein 1-like 1 (GDAP1L1) subfamily; GDAP1L1 is a paralogue of GDAP1 with about 56% sequence identity and 70% similarity. It's function is unknown. Like GDAP1, it does not exhibit GST activity using standard substrates. 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 thioredoxin-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.


Pssm-ID: 198335  Cd Length: 111  Bit Score: 234.90  E-value: 6.55e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 201 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 280
Cdd:cd10302   1 PQLTEPYLSKQKKLMAKILEHDNVNYLKKILGELAMVLDQIEAELEKRKLEYEGQKCELWLCGCIFTLADVLLGATLHRL 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 30581160 281 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 311
Cdd:cd10302  81 KFLGLSKKYWEDGSRPNLQSFFERVQKRYAF 111
GST_N_GDAP1 cd03052
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ...
 47-119 8.17e-46

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: 151.16  E-value: 8.17e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVE 119
Cdd:cd03052   1 LVLYHWTQSFSSQKVRLVIAEKGLRCEEYDVSLPLSEHNEPWFMRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
47-317 2.93e-25

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 101.13  E-value: 2.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLN-LGeEVPVIIHRDNIISDYDQIIDYVERTFTGE 125
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNpLG-KVPVLVDDGLVLTESLAILEYLAERYPEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 126 hvvALMPEvGSLQHARVLQyrelldalpMDAYTHGcILHPELTTdsmipkyataeirrhlanattdlmkldheeepqlse 205
Cdd:COG0625  81 ---PLLPA-DPAARARVRQ---------WLAWADG-DLHPALRN------------------------------------ 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 206 pylskqkkLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGL 285
Cdd:COG0625 111 --------LLERLAPEKDPAAIARARAELARLLAVLEARLAGGP----------YLAGDRFSIADIALAPVLRRLDRLGL 172

                       250       260       270
                ....*....|....*....|....*....|..
gi 30581160 286 SkkyWEDgsRPNLQSFFERVQRRFAFRKVLGD 317
Cdd:COG0625 173 D---LAD--YPNLAAWLARLAARPAFQRALAA 199
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 58-121 9.91e-09

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 51.48  E-value: 9.91e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30581160    58 SQKVRLVIAEKGLVCEERDVSLPqSEHKEPWFMRLNLGEEVPVIIHRDN-IISDYDQIIDYVERT 121
Cdd:pfam13409   5 SHRVRLALEEKGLPYEIELVDLD-PKDKPPELLALNPLGTVPVLVLPDGtVLTDSLVILEYLEEL 68
PRK15113 PRK15113
glutathione transferase;
47-133 8.83e-06

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 46.11  E-value: 8.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160   47 LVLYHWTQSFS--SQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVERTFTG 124
Cdd:PRK15113   6 ITLYSDAHFFSpyVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAP 85


                 ....*....
gi 30581160  125 EHVVALMPE 133
Cdd:PRK15113  86 PAWERIYPA 94
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 225-308 1.28e-04

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: 40.35  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160   225 SYLKKILGELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKkywEDGSRPNLQSFFER 304
Cdd:pfam00043  22 PEVDEALEKVARVLSALEEVLKGQT----------YLVGDKLTLADIALAPALLWLYELDPAC---LREKFPNLKAWFER 88


                  ....
gi 30581160   305 VQRR 308
Cdd:pfam00043  89 VAAR 92
 
Name Accession Description Interval E-value
GST_C_GDAP1L1 cd10302
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein ...
 201-311 6.55e-78

C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1-like 1; Glutathione S-transferase (GST) C-terminal domain family, Ganglioside-induced differentiation-associated protein 1-like 1 (GDAP1L1) subfamily; GDAP1L1 is a paralogue of GDAP1 with about 56% sequence identity and 70% similarity. It's function is unknown. Like GDAP1, it does not exhibit GST activity using standard substrates. 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 thioredoxin-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.


Pssm-ID: 198335  Cd Length: 111  Bit Score: 234.90  E-value: 6.55e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 201 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 280
Cdd:cd10302   1 PQLTEPYLSKQKKLMAKILEHDNVNYLKKILGELAMVLDQIEAELEKRKLEYEGQKCELWLCGCIFTLADVLLGATLHRL 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 30581160 281 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 311
Cdd:cd10302  81 KFLGLSKKYWEDGSRPNLQSFFERVQKRYAF 111
GST_C_GDAP1_like cd03204
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein ...
 201-311 7.82e-60

C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ganglioside-induced differentiation-associated protein 1 (GDAP1)-like 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 thioredoxin-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: 198313  Cd Length: 111  Bit Score: 188.43  E-value: 7.82e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 201 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 280
Cdd:cd03204   1 PDLAEAYTAKQKKLAIQLRDHEDSSYLKKILDELEVVLDQVEKELGERKRETDESGQQQWLCGESFTAADISLSVLLHRL 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 30581160 281 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 311
Cdd:cd03204  81 KFLGLSRRFWGNGKRPNIESYFERVRQRESF 111
GST_N_GDAP1 cd03052
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ...
 47-119 8.17e-46

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: 151.16  E-value: 8.17e-46
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVE 119
Cdd:cd03052   1 LVLYHWTQSFSSQKVRLVIAEKGLRCEEYDVSLPLSEHNEPWFMRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73
GST_C_GDAP1 cd10303
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1; ...
 201-311 6.08e-43

C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-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: 198336 [Multi-domain]  Cd Length: 111  Bit Score: 145.15  E-value: 6.08e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 201 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 280
Cdd:cd10303   1 PDLQDAYIAKQKRLKSKLLDHDNIKYLKKILDELEKVLDQVETELQRRNEETPEEGQQPWLCGEFFSLADVSLAVTLHRL 80

                        90       100       110
                ....*....|....*....|....*....|.
gi 30581160 281 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 311
Cdd:cd10303  81 KFLGLARRNWGNGKRPNLETYYERVLKRKTF 111
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
47-317 2.93e-25

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 101.13  E-value: 2.93e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLN-LGeEVPVIIHRDNIISDYDQIIDYVERTFTGE 125
Cdd:COG0625   2 MKLYGSPPSPNSRRVRIALEEKGLPYELVPVDLAKGEQKSPEFLALNpLG-KVPVLVDDGLVLTESLAILEYLAERYPEP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 126 hvvALMPEvGSLQHARVLQyrelldalpMDAYTHGcILHPELTTdsmipkyataeirrhlanattdlmkldheeepqlse 205
Cdd:COG0625  81 ---PLLPA-DPAARARVRQ---------WLAWADG-DLHPALRN------------------------------------ 110

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160 206 pylskqkkLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGL 285
Cdd:COG0625 111 --------LLERLAPEKDPAAIARARAELARLLAVLEARLAGGP----------YLAGDRFSIADIALAPVLRRLDRLGL 172

                       250       260       270
                ....*....|....*....|....*....|..
gi 30581160 286 SkkyWEDgsRPNLQSFFERVQRRFAFRKVLGD 317
Cdd:COG0625 173 D---LAD--YPNLAAWLARLAARPAFQRALAA 199
GST_N_family cd00570
Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ...
 47-119 4.72e-12

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: 60.66  E-value: 4.72e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEpwFMRLNLGEEVPVIIHRDNIISDYDQIIDYVE 119
Cdd:cd00570   1 LKLYYFPGSPRSLRVRLALEEKGLPYELVPVDLGEGEQEE--FLALNPLGKVPVLEDGGLVLTESLAILEYLA 71
GST_N_2 pfam13409
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798.
 58-121 9.91e-09

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


Pssm-ID: 433184 [Multi-domain]  Cd Length: 68  Bit Score: 51.48  E-value: 9.91e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 30581160    58 SQKVRLVIAEKGLVCEERDVSLPqSEHKEPWFMRLNLGEEVPVIIHRDN-IISDYDQIIDYVERT 121
Cdd:pfam13409   5 SHRVRLALEEKGLPYEIELVDLD-PKDKPPELLALNPLGTVPVLVLPDGtVLTDSLVILEYLEEL 68
GST_N_3 pfam13417
Glutathione S-transferase, N-terminal domain;
49-126 8.15e-08

Glutathione S-transferase, N-terminal domain;


Pssm-ID: 433190 [Multi-domain]  Cd Length: 75  Bit Score: 49.15  E-value: 8.15e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30581160    49 LYHWTQSFSSQKVRLVIAEKGLVCEERDVSLpqsEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVERTFTGEH 126
Cdd:pfam13417   1 LYGFPGSPYARRVRIALNEKGLPYEFVPIPP---GDHPPELLAKNPLGKVPVLEDDGGILCESLAIIDYLEELYPGPP 75
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 45-120 2.49e-07

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: 47.69  E-value: 2.49e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30581160    45 ESLVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVER 120
Cdd:pfam02798   1 MVLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGGKKLTESRAILEYIAR 76
GST_N_GTT2_like cd03051
GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ...
 49-119 2.68e-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: 47.68  E-value: 2.68e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 30581160  49 LYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRD-NIISDYDQIIDYVE 119
Cdd:cd03051   3 LYDSPTAPNPRRVRIFLAEKGIDVPLVTVDLAAGEQRSPEFLAKNPAGTVPVLELDDgTVITESVAICRYLE 74
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 233-305 1.05e-06

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: 46.72  E-value: 1.05e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30581160 233 ELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKKYWEDgsRPNLQSFFERV 305
Cdd:cd00299  40 ELPALLAALEQLLAGRP----------YLAGDQFSLADVALAPVLARLEALGPYYDLLDE--YPRLKAWYDRL 100
GST_N_Zeta cd03042
GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ...
 47-119 3.94e-06

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


Pssm-ID: 239340 [Multi-domain]  Cd Length: 73  Bit Score: 44.10  E-value: 3.94e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVE 119
Cdd:cd03042   1 MILYSYFRSSASYRVRIALNLKGLDYEYVPVNLLKGEQLSPAYRALNPQGLVPTLVIDGLVLTQSLAIIEYLD 73
PRK15113 PRK15113
glutathione transferase;
47-133 8.83e-06

glutathione transferase;


Pssm-ID: 185068 [Multi-domain]  Cd Length: 214  Bit Score: 46.11  E-value: 8.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160   47 LVLYHWTQSFS--SQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVERTFTG 124
Cdd:PRK15113   6 ITLYSDAHFFSpyVMSAFVALQEKGLPFELKTVDLDAGEHLQPTYQGYSLTRRVPTLQHDDFELSESSAIAEYLEERFAP 85


                 ....*....
gi 30581160  125 EHVVALMPE 133
Cdd:PRK15113  86 PAWERIYPA 94
GST_N_4 cd03056
GST_N family, unknown subfamily 4; composed of uncharacterized bacterial proteins with ...
 49-118 9.59e-06

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


Pssm-ID: 239354 [Multi-domain]  Cd Length: 73  Bit Score: 42.95  E-value: 9.59e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160  49 LYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYV 118
Cdd:cd03056   3 LYGFPLSGNCYKVRLLLALLGIPYEWVEVDILKGETRTPEFLALNPNGEVPVLELDGRVLAESNAILVYL 72
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 238-315 4.39e-05

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: 42.23  E-value: 4.39e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30581160 238 LDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKKYWedgsrPNLQSFFERVQRRFAFRKVL 315
Cdd:cd03188  51 LAYLDAQLAGGP----------YLLGDQFSVADAYLFVVLRWARAVGLDLSDW-----PHLAAYLARVAARPAVQAAL 113
GST_N_Phi cd03053
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ...
 47-105 8.29e-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: 40.33  E-value: 8.29e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRD 105
Cdd:cd03053   2 LKLYGAAMSTCVRRVLLCLEEKGVDYELVPVDLTKGEHKSPEHLARNPFGQIPALEDGD 60
GST_N_SspA cd03059
GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ...
 47-122 1.21e-04

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: 40.00  E-value: 1.21e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLpqsEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVERTF 122
Cdd:cd03059   1 MTLYSGPDDVYSHRVRIVLAEKGVSVEIIDVDP---DNPPEDLAELNPYGTVPTLVDRDLVLYESRIIMEYLDERF 73
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 225-308 1.28e-04

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: 40.35  E-value: 1.28e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160   225 SYLKKILGELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKkywEDGSRPNLQSFFER 304
Cdd:pfam00043  22 PEVDEALEKVARVLSALEEVLKGQT----------YLVGDKLTLADIALAPALLWLYELDPAC---LREKFPNLKAWFER 88


                  ....
gi 30581160   305 VQRR 308
Cdd:pfam00043  89 VAAR 92
GST_N_Delta_Epsilon cd03045
GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ...
 47-117 2.47e-04

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: 39.13  E-value: 2.47e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30581160  47 LVLYHWTQSFSSQKVRLVIAEKGLVCEERDVSLPQSEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDY 117
Cdd:cd03045   1 IDLYYLPGSPPCRAVLLTAKALGLELNLKEVNLMKGEHLKPEFLKLNPQHTVPTLVDNGFVLWESHAILIY 71
PLN02817 PLN02817
glutathione dehydrogenase (ascorbate)
 58-136 4.78e-04

glutathione dehydrogenase (ascorbate)


Pssm-ID: 166458 [Multi-domain]  Cd Length: 265  Bit Score: 41.52  E-value: 4.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30581160   58 SQKVRLVIAEKGLVCEERDVSLpqsEHKEPWFMRLNLGEEVPVIIHRDNIISDYDQIIDYVERTFTgEHVVALMPE---V 134
Cdd:PLN02817  76 CQRVLLTLEEKHLPYDMKLVDL---TNKPEWFLKISPEGKVPVVKLDEKWVADSDVITQALEEKYP-DPPLATPPEkasV 151


                 ..
gi 30581160  135 GS 136
Cdd:PLN02817 152 GS 153
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 232-308 5.04e-04

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


Pssm-ID: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 39.60  E-value: 5.04e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 30581160 232 GELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHR-LKFLGLSKKYwedgsrPNLQSFFERVQRR 308
Cdd:cd03189  61 PELKRHLDFLEDHLAKHP----------YFAGDELTAADIMMSFPLEAaLARGPLLEQY------PNIAAYLERIEAR 122
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 260-311 6.18e-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: 38.80  E-value: 6.18e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 30581160 260 WLCGCAFTLADVLLGATLHRLKFLGLskkywEDGSRPNLQSFFERVQRRFAF 311
Cdd:cd03180  64 YLAGDRFTLADIALGCSVYRWLELPI-----ERPALPHLERWYARLSQRPAF 110
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 232-310 1.27e-03

C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 8; composed of Agrobacterium tumefaciens GST and other uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins, and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. The three-dimensional structure of Agrobacterium tumefaciens GST has been determined but there is no information on its functional characterization.


Pssm-ID: 198316 [Multi-domain]  Cd Length: 101  Bit Score: 37.66  E-value: 1.27e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30581160 232 GELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKKYwedgsrPNLQSFFERVQRRFA 310
Cdd:cd03207  39 GDLDERLAALEAALAGRP----------YLVGERFSAADLLLASVLRWARAFGLLPEY------PALRAYVARCTARPA 101
 
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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