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Conserved domains on  [gi|1484499003|ref|XP_026479181|]
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probable maleylacetoacetate isomerase 2 [Ctenocephalides felis]

Protein Classification

glutathione S-transferase; glutathione S-transferase family protein( domain architecture ID 10123620)

glutathione S-transferase catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress; glutathione S-transferase (GST) family protein similar to human failed axon connections homolog, which may play a role in axonal development

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_Zeta cd03191
C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione ...
 18-125 4.89e-62

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class 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: 198300 [Multi-domain]  Cd Length: 121  Bit Score: 185.86  E-value: 4.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1484499003  18 RDLHKVISSGIQPLQNLIVLIYVG------EEKKKEWAQHWITRGFRAVEKLLSTSAGKYCVGDEITLADCCLIPQVFNA 91
Cdd:cd03191     8 RAIALIIACDIHPLQNLRVLKYLTeklgvsEEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICLVPQVYNA 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1484499003  92 RRFHVDLRPFPIILRIDRELETHPAFRAAHPSSQ 125
Cdd:cd03191    88 RRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121
 
Name Accession Description Interval E-value
GST_C_Zeta cd03191
C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione ...
 18-125 4.89e-62

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class 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: 198300 [Multi-domain]  Cd Length: 121  Bit Score: 185.86  E-value: 4.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1484499003  18 RDLHKVISSGIQPLQNLIVLIYVG------EEKKKEWAQHWITRGFRAVEKLLSTSAGKYCVGDEITLADCCLIPQVFNA 91
Cdd:cd03191     8 RAIALIIACDIHPLQNLRVLKYLTeklgvsEEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICLVPQVYNA 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1484499003  92 RRFHVDLRPFPIILRIDRELETHPAFRAAHPSSQ 125
Cdd:cd03191    88 RRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 18-129 4.30e-53

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


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 166.35  E-value: 4.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1484499003  18 RDLHKVISSGIQPLQNLIVLIYVG------EEKKKEWAQHWITRGFRAVEKLLSTSAGKYCVGDEITLADCCLIPQVFNA 91
Cdd:TIGR01262  93 RALALLIACDIHPLNNLRVLQYLReklgveEEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTPTLADLCLVPQVYNA 172

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1484499003  92 RRFHVDLRPFPIILRIDRELETHPAFRAAHPSSQPDCP 129
Cdd:TIGR01262 173 ERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
41-127 9.15e-20

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 80.71  E-value: 9.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1484499003  41 GEEKKKEWAQHWITRGFRAVEKLLStsAGKYCVGDEITLADCCLIPQVFNARRFHVDLRPFPIILRIDRELETHPAFRAA 120
Cdd:COG0625   119 KDPAAIARARAELARLLAVLEARLA--GGPYLAGDRFSIADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRA 196


                  ....*..
gi 1484499003 121 HPSSQPD 127
Cdd:COG0625   197 LAAAEPD 203
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 34-81 8.17e-05

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 39.08  E-value: 8.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1484499003  34 LIVLIYVGEEKKKEWAQHW-----ITRGFRAVEKLLSTSAGKYCVGDEITLAD 81
Cdd:pfam14497   7 IASSLYYEDEKKKAKRRKEfreerLPKFLGYFEKVLNKNGGGYLVGDKLTYAD 59
 
Name Accession Description Interval E-value
GST_C_Zeta cd03191
C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione ...
 18-125 4.89e-62

C-terminal, alpha helical domain of Class Zeta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Class 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: 198300 [Multi-domain]  Cd Length: 121  Bit Score: 185.86  E-value: 4.89e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1484499003  18 RDLHKVISSGIQPLQNLIVLIYVG------EEKKKEWAQHWITRGFRAVEKLLSTSAGKYCVGDEITLADCCLIPQVFNA 91
Cdd:cd03191     8 RAIALIIACDIHPLQNLRVLKYLTeklgvsEEEKLAWAQHWIERGFQALEKLLASTAGKYCVGDEPTLADICLVPQVYNA 87

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1484499003  92 RRFHVDLRPFPIILRIDRELETHPAFRAAHPSSQ 125
Cdd:cd03191    88 RRFGVDLSPYPTIVRINEACLELPAFQAAHPENQ 121
maiA TIGR01262
maleylacetoacetate isomerase; Maleylacetoacetate isomerase is an enzyme of tyrosine and ...
 18-129 4.30e-53

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


Pssm-ID: 273527 [Multi-domain]  Cd Length: 210  Bit Score: 166.35  E-value: 4.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1484499003  18 RDLHKVISSGIQPLQNLIVLIYVG------EEKKKEWAQHWITRGFRAVEKLLSTSAGKYCVGDEITLADCCLIPQVFNA 91
Cdd:TIGR01262  93 RALALLIACDIHPLNNLRVLQYLReklgveEEARNRWYQHWISKGFAALEALLQPHAGRFCVGDTPTLADLCLVPQVYNA 172

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1484499003  92 RRFHVDLRPFPIILRIDRELETHPAFRAAHPSSQPDCP 129
Cdd:TIGR01262 173 ERFGVDLTPYPTLRRIAAALAALPAFQRAHPENQPDTP 210
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
41-127 9.15e-20

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 80.71  E-value: 9.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1484499003  41 GEEKKKEWAQHWITRGFRAVEKLLStsAGKYCVGDEITLADCCLIPQVFNARRFHVDLRPFPIILRIDRELETHPAFRAA 120
Cdd:COG0625   119 KDPAAIARARAELARLLAVLEARLA--GGPYLAGDRFSIADIALAPVLRRLDRLGLDLADYPNLAAWLARLAARPAFQRA 196


                  ....*..
gi 1484499003 121 HPSSQPD 127
Cdd:COG0625   197 LAAAEPD 203
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 34-81 8.17e-05

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 39.08  E-value: 8.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1484499003  34 LIVLIYVGEEKKKEWAQHW-----ITRGFRAVEKLLSTSAGKYCVGDEITLAD 81
Cdd:pfam14497   7 IASSLYYEDEKKKAKRRKEfreerLPKFLGYFEKVLNKNGGGYLVGDKLTYAD 59
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 42-119 1.29e-04

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: 38.63  E-value: 1.29e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1484499003  42 EEKKKEWAQHWITRGFRAVEKLLSTsaGKYCVGDEITLADCCLIPQvfnarrfhvdLRPFPIILRIDRELETHPAFRA 119
Cdd:cd00299    30 DEAAVEAAREELPALLAALEQLLAG--RPYLAGDQFSLADVALAPV----------LARLEALGPYYDLLDEYPRLKA 95
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 41-121 1.87e-04

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


Pssm-ID: 198297 [Multi-domain]  Cd Length: 113  Bit Score: 38.38  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1484499003  41 GEEKKKEWAQHWITRGFRAVEKLLStsAGKYCVGDEITLADCCLIPQVFNARRFHVDLRPFPIILRIDRELETHPAFRAA 120
Cdd:cd03188    35 LAEEVKAAARERLERRLAYLDAQLA--GGPYLLGDQFSVADAYLFVVLRWARAVGLDLSDWPHLAAYLARVAARPAVQAA 112


                  .
gi 1484499003 121 H 121
Cdd:cd03188   113 L 113
GST_C_Sigma_like cd03192
C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione ...
 42-84 7.03e-04

C-terminal, alpha helical domain of Class Sigma-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Sigma_like; composed of GSTs belonging to class Sigma and similar proteins, including GSTs from class Mu, Pi, and Alpha. 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. Vertebrate class Sigma GSTs are characterized as GSH-dependent hematopoietic prostaglandin (PG) D synthases and are responsible for the production of PGD2 by catalyzing the isomerization of PGH2. The functions of PGD2 include the maintenance of body temperature, inhibition of platelet aggregation, bronchoconstriction, vasodilation, and mediation of allergy and inflammation. Other class Sigma-like members include the class II insect GSTs, S-crystallins from cephalopods, nematode-specific GSTs, and 28-kDa GSTs from parasitic flatworms. Drosophila GST2 is associated with indirect flight muscle and exhibits preference for catalyzing GSH conjugation to lipid peroxidation products, indicating an anti-oxidant role. S-crystallin constitutes the major lens protein in cephalopod eyes and is responsible for lens transparency and proper refractive index. The 28-kDa GST from Schistosoma is a multifunctional enzyme, exhibiting GSH transferase, GSH peroxidase, and PGD2 synthase activities, and may play an important role in host-parasite interactions. Members also include novel GSTs from the fungus Cunninghamella elegans, designated as class Gamma, and from the protozoan Blepharisma japonicum, described as a light-inducible GST.


Pssm-ID: 198301 [Multi-domain]  Cd Length: 104  Bit Score: 36.45  E-value: 7.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1484499003  42 EEKKKEWAQHWITRGFRAVEKLLSTSAGKYCVGDEITLADCCL 84
Cdd:cd03192    33 KEKKKEFLEEALPKFLGKFEKILKKSGGGYFVGDKLTWADLAL 75
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 40-106 4.31e-03

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


Pssm-ID: 198287 [Multi-domain]  Cd Length: 117  Bit Score: 34.82  E-value: 4.31e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1484499003  40 VGEEKKKEwaqhwITRGFRAVEKLLSTSagKYCVGDEITLADCCLIPQVFNARRFHVDLRPFPIILR 106
Cdd:cd03177    35 PPEEKLDK-----LEEALEFLETFLEGS--DYVAGDQLTIADLSLVATVSTLEVVGFDLSKYPNVAA 94
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 55-119 5.94e-03

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 33.45  E-value: 5.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1484499003  55 RGFRAVEKLLSTSAgkYCVGDEITLADCCLIPQVFnarRFHVDLRPFPIilridreLETHPAFRA 119
Cdd:pfam13410  11 AALDALEARLADGP--GLLGDRPTLADIALAPVLA---RLDAAYPGLDL-------REGYPRLRA 63
GST_C_CLIC cd03198
C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase ...
 64-86 7.78e-03

C-terminal, alpha helical domain of Chloride Intracellular Channels; Glutathione S-transferase (GST) C-terminal domain family, Chloride Intracellular Channel (CLIC) subfamily; composed of CLICs (CLIC1-6 in vertebrates), p64, parchorin, and similar proteins. They are auto-inserting, self-assembling intracellular anion channels involved in a wide variety of functions including regulated secretion, cell division, and apoptosis. They can exist in both water-soluble and membrane-bound states and are found in various vesicles and membranes, and they may play roles in the maintenance of these intracellular membranes. Biochemical studies of the Caenorhabditis elegans homolog, EXC-4, show that the membrane localization domain is present in the N-terminal part of the protein. CLICs display structural plasticity, with CLIC1 adopting two soluble conformations. The structure of soluble human CLIC1 reveals that it is monomeric and adopts a fold similar to GSTs, containing an N-terminal domain with a thioredoxin fold and a C-terminal alpha helical domain. Upon oxidation, the N-terminal domain of CLIC1 undergoes a structural change to form a non-covalent dimer stabilized by the formation of an intramolecular disulfide bond between two cysteines that are far apart in the reduced form. The CLIC1 dimer bears no similarity to GST dimers. The redox-controlled structural rearrangement exposes a large hydrophobic surface, which is masked by dimerization in vitro. In vivo, this surface may represent the docking interface of CLIC1 in its membrane-bound state. The two cysteines in CLIC1 that form the disulfide bond in oxidizing conditions are essential for dimerization and chloride channel activity, however, in other subfamily members, the second cysteine is not conserved.


Pssm-ID: 198307  Cd Length: 119  Bit Score: 34.12  E-value: 7.78e-03
                          10        20
                  ....*....|....*....|...
gi 1484499003  64 LSTSAGKYCVGDEITLADCCLIP 86
Cdd:cd03198    45 LSSSSRKFLDGDTLTLADCNLLP 67
 
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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