NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|376319239|ref|NP_001243667|]
View 

ganglioside-induced differentiation-associated protein 1-like 1 isoform 3 [Homo sapiens]

Protein Classification

glutathione S-transferase family protein( domain architecture ID 88)

glutathione S-transferase (GST) family protein may catalyze 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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
GST_C_family super family cl02776
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 112-222 2.42e-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: 232.59  E-value: 2.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239 112 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 191
Cdd:cd10302    1 PQLTEPYLSKQKKLMAKILEHDNVNYLKKILGELAMVLDQIEAELEKRKLEYEGQKCELWLCGCIFTLADVLLGATLHRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 376319239 192 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 222
Cdd:cd10302   81 KFLGLSKKYWEDGSRPNLQSFFERVQKRYAF 111
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 1-30 4.39e-12

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


The actual alignment was detected with superfamily member cd03052:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 73  Bit Score: 60.25  E-value: 4.39e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 376319239   1 MRLNLGEEVPVIIHRDNIISDYDQIIDYVE 30
Cdd:cd03052   44 MRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73
 
Name Accession Description Interval E-value
GST_C_GDAP1L1 cd10302
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein ...
 112-222 2.42e-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: 232.59  E-value: 2.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239 112 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 191
Cdd:cd10302    1 PQLTEPYLSKQKKLMAKILEHDNVNYLKKILGELAMVLDQIEAELEKRKLEYEGQKCELWLCGCIFTLADVLLGATLHRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 376319239 192 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 222
Cdd:cd10302   81 KFLGLSKKYWEDGSRPNLQSFFERVQKRYAF 111
GST_N_GDAP1 cd03052
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ...
 1-30 4.39e-12

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: 60.25  E-value: 4.39e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 376319239   1 MRLNLGEEVPVIIHRDNIISDYDQIIDYVE 30
Cdd:cd03052   44 MRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-228 3.01e-11

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 61.45  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239   9 VPVIIHRDNIISDYDQIIDYVERTFTGEhvvALMPEvGSLQHARVLQyrelldalpMDAYTHGcILHPELTTdsmipkya 88
Cdd:COG0625   53 VPVLVDDGLVLTESLAILEYLAERYPEP---PLLPA-DPAARARVRQ---------WLAWADG-DLHPALRN-------- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239  89 taeirrhlanattdlmkldheeepqlsepylskqkkLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKlenegqkc 168
Cdd:COG0625  111 ------------------------------------LLERLAPEKDPAAIARARAELARLLAVLEARLAGGP-------- 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239 169 elWLCGCAFTLADVLLGATLHRLKFLGLSkkyWEDgsRPNLQSFFERVQRRFAFRKVLGD 228
Cdd:COG0625  147 --YLAGDRFSIADIALAPVLRRLDRLGLD---LAD--YPNLAAWLARLAARPAFQRALAA 199
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 136-219 1.60e-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: 39.96  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239  136 SYLKKILGELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKkywEDGSRPNLQSFFER 215
Cdd:pfam00043  22 PEVDEALEKVARVLSALEEVLKGQT----------YLVGDKLTLADIALAPALLWLYELDPAC---LREKFPNLKAWFER 88


                  ....
gi 376319239  216 VQRR 219
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 ...
 112-222 2.42e-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: 232.59  E-value: 2.42e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239 112 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 191
Cdd:cd10302    1 PQLTEPYLSKQKKLMAKILEHDNVNYLKKILGELAMVLDQIEAELEKRKLEYEGQKCELWLCGCIFTLADVLLGATLHRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 376319239 192 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 222
Cdd:cd10302   81 KFLGLSKKYWEDGSRPNLQSFFERVQKRYAF 111
GST_C_GDAP1_like cd03204
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein ...
 112-222 1.13e-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: 187.66  E-value: 1.13e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239 112 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 191
Cdd:cd03204    1 PDLAEAYTAKQKKLAIQLRDHEDSSYLKKILDELEVVLDQVEKELGERKRETDESGQQQWLCGESFTAADISLSVLLHRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 376319239 192 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 222
Cdd:cd03204   81 KFLGLSRRFWGNGKRPNIESYFERVRQRESF 111
GST_C_GDAP1 cd10303
C-terminal, alpha helical domain of Ganglioside-induced differentiation-associated protein 1; ...
 112-222 1.03e-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: 144.38  E-value: 1.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239 112 PQLSEPYLSKQKKLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKLENEGQKCELWLCGCAFTLADVLLGATLHRL 191
Cdd:cd10303    1 PDLQDAYIAKQKRLKSKLLDHDNIKYLKKILDELEKVLDQVETELQRRNEETPEEGQQPWLCGEFFSLADVSLAVTLHRL 80

                         90       100       110
                 ....*....|....*....|....*....|.
gi 376319239 192 KFLGLSKKYWEDGSRPNLQSFFERVQRRFAF 222
Cdd:cd10303   81 KFLGLARRNWGNGKRPNLETYYERVLKRKTF 111
GST_N_GDAP1 cd03052
GST_N family, Ganglioside-induced differentiation-associated protein 1 (GDAP1) subfamily; ...
 1-30 4.39e-12

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: 60.25  E-value: 4.39e-12
                         10        20        30
                 ....*....|....*....|....*....|
gi 376319239   1 MRLNLGEEVPVIIHRDNIISDYDQIIDYVE 30
Cdd:cd03052   44 MRLNPTGEVPVLIHGDNIICDPTQIIDYLE 73
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
9-228 3.01e-11

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 61.45  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239   9 VPVIIHRDNIISDYDQIIDYVERTFTGEhvvALMPEvGSLQHARVLQyrelldalpMDAYTHGcILHPELTTdsmipkya 88
Cdd:COG0625   53 VPVLVDDGLVLTESLAILEYLAERYPEP---PLLPA-DPAARARVRQ---------WLAWADG-DLHPALRN-------- 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239  89 taeirrhlanattdlmkldheeepqlsepylskqkkLMAKILEHDDVSYLKKILGELAMVLDQIEAELEKRKlenegqkc 168
Cdd:COG0625  111 ------------------------------------LLERLAPEKDPAAIARARAELARLLAVLEARLAGGP-------- 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239 169 elWLCGCAFTLADVLLGATLHRLKFLGLSkkyWEDgsRPNLQSFFERVQRRFAFRKVLGD 228
Cdd:COG0625  147 --YLAGDRFSIADIALAPVLRRLDRLGLD---LAD--YPNLAAWLARLAARPAFQRALAA 199
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 144-216 9.17e-07

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: 46.34  E-value: 9.17e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 376319239 144 ELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKKYWEDgsRPNLQSFFERV 216
Cdd:cd00299   40 ELPALLAALEQLLAGRP----------YLAGDQFSLADVALAPVLARLEALGPYYDLLDE--YPRLKAWYDRL 100
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 149-226 2.93e-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: 2.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 376319239 149 LDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKKYWedgsrPNLQSFFERVQRRFAFRKVL 226
Cdd:cd03188   51 LAYLDAQLAGGP----------YLLGDQFSVADAYLFVVLRWARAVGLDLSDW-----PHLAAYLARVAARPAVQAAL 113
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 136-219 1.60e-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: 39.96  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 376319239  136 SYLKKILGELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKkywEDGSRPNLQSFFER 215
Cdd:pfam00043  22 PEVDEALEKVARVLSALEEVLKGQT----------YLVGDKLTLADIALAPALLWLYELDPAC---LREKFPNLKAWFER 88


                  ....
gi 376319239  216 VQRR 219
Cdd:pfam00043  89 VAAR 92
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 171-222 2.37e-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: 39.57  E-value: 2.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 376319239 171 WLCGCAFTLADVLLGATLHRLKFLGLskkywEDGSRPNLQSFFERVQRRFAF 222
Cdd:cd03180   64 YLAGDRFTLADIALGCSVYRWLELPI-----ERPALPHLERWYARLSQRPAF 110
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 143-219 5.24e-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: 39.21  E-value: 5.24e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 376319239 143 GELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHR-LKFLGLSKKYwedgsrPNLQSFFERVQRR 219
Cdd:cd03189   61 PELKRHLDFLEDHLAKHP----------YFAGDELTAADIMMSFPLEAaLARGPLLEQY------PNIAAYLERIEAR 122
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 143-221 7.42e-04

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: 38.05  E-value: 7.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 376319239 143 GELAMVLDQIEAELEKRKlenegqkcelWLCGCAFTLADVLLGATLHRLKFLGLSKKYwedgsrPNLQSFFERVQRRFA 221
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH