MULTISPECIES: glutathione S-transferase N-terminal domain-containing protein [Klebsiella]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| GST_C_6 | cd03205 | C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ... |
95-202 | 1.49e-43 | ||||
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization. : Pssm-ID: 198314 [Multi-domain] Cd Length: 109 Bit Score: 141.19 E-value: 1.49e-43
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| PRK10357 super family | cl32504 | putative glutathione S-transferase; Provisional |
2-182 | 5.89e-28 | ||||
putative glutathione S-transferase; Provisional The actual alignment was detected with superfamily member PRK10357: Pssm-ID: 182405 [Multi-domain] Cd Length: 202 Bit Score: 104.42 E-value: 5.89e-28
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| Name | Accession | Description | Interval | E-value | ||||
| GST_C_6 | cd03205 | C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ... |
95-202 | 1.49e-43 | ||||
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization. Pssm-ID: 198314 [Multi-domain] Cd Length: 109 Bit Score: 141.19 E-value: 1.49e-43
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
1-202 | 8.30e-31 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 111.53 E-value: 8.30e-31
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| PRK10357 | PRK10357 | putative glutathione S-transferase; Provisional |
2-182 | 5.89e-28 | ||||
putative glutathione S-transferase; Provisional Pssm-ID: 182405 [Multi-domain] Cd Length: 202 Bit Score: 104.42 E-value: 5.89e-28
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| GST_N_3 | cd03049 | GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ... |
2-76 | 2.92e-26 | ||||
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Pssm-ID: 239347 [Multi-domain] Cd Length: 73 Bit Score: 95.79 E-value: 2.92e-26
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| GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
9-78 | 1.39e-13 | ||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 63.03 E-value: 1.39e-13
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| GST_C_2 | pfam13410 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
127-190 | 9.18e-04 | ||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 433185 [Multi-domain] Cd Length: 67 Bit Score: 36.53 E-value: 9.18e-04
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| Name | Accession | Description | Interval | E-value | ||||
| GST_C_6 | cd03205 | C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; ... |
95-202 | 1.49e-43 | ||||
C-terminal, alpha helical domain of an unknown subfamily 6 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 6; composed of uncharacterized bacterial proteins with similarity to GSTs, including Pseudomonas fluorescens GST with a known three-dimensional structure. 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. Though the three-dimensional structure of Pseudomonas fluorescens GST has been determined, there is no information on its functional characterization. Pssm-ID: 198314 [Multi-domain] Cd Length: 109 Bit Score: 141.19 E-value: 1.49e-43
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| GstA | COG0625 | Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; |
1-202 | 8.30e-31 | ||||
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440390 [Multi-domain] Cd Length: 205 Bit Score: 111.53 E-value: 8.30e-31
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| PRK10357 | PRK10357 | putative glutathione S-transferase; Provisional |
2-182 | 5.89e-28 | ||||
putative glutathione S-transferase; Provisional Pssm-ID: 182405 [Multi-domain] Cd Length: 202 Bit Score: 104.42 E-value: 5.89e-28
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| GST_N_3 | cd03049 | GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with ... |
2-76 | 2.92e-26 | ||||
GST_N family, unknown subfamily 3; composed of uncharacterized bacterial proteins with similarity to GSTs. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Pssm-ID: 239347 [Multi-domain] Cd Length: 73 Bit Score: 95.79 E-value: 2.92e-26
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| GST_N_2 | pfam13409 | Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. |
9-78 | 1.39e-13 | ||||
Glutathione S-transferase, N-terminal domain; This family is closely related to pfam02798. Pssm-ID: 433184 [Multi-domain] Cd Length: 68 Bit Score: 63.03 E-value: 1.39e-13
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| GST_N_family | cd00570 | Glutathione S-transferase (GST) family, N-terminal domain; a large, diverse group of cytosolic ... |
2-75 | 5.86e-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: 58.74 E-value: 5.86e-12
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| GST_N_3 | pfam13417 | Glutathione S-transferase, N-terminal domain; |
4-81 | 6.56e-12 | ||||
Glutathione S-transferase, N-terminal domain; Pssm-ID: 433190 [Multi-domain] Cd Length: 75 Bit Score: 58.78 E-value: 6.56e-12
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| GST_N_Phi | cd03053 | GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related ... |
2-78 | 2.07e-09 | ||||
GST_N family, Class Phi subfamily; composed of plant-specific class Phi GSTs and related fungal and bacterial proteins. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The class Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Phi GSTs, respectively. They are primarily responsible for herbicide detoxification together with class Tau GSTs, showing class specificity in substrate preference. Phi enzymes are highly reactive toward chloroacetanilide and thiocarbamate herbicides. Some Phi GSTs have other functions including transport of flavonoid pigments to the vacuole, shoot regeneration and GSH peroxidase activity. Pssm-ID: 239351 [Multi-domain] Cd Length: 76 Bit Score: 52.27 E-value: 2.07e-09
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| GST_N_Delta_Epsilon | cd03045 | GST_N family, Class Delta and Epsilon subfamily; GSTs are cytosolic dimeric proteins involved ... |
2-75 | 2.76e-07 | ||||
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: 46.45 E-value: 2.76e-07
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| GST_N_EF1Bgamma | cd03044 | GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part ... |
4-75 | 3.46e-07 | ||||
GST_N family, Gamma subunit of Elongation Factor 1B (EFB1gamma) subfamily; EF1Bgamma is part of the eukaryotic translation elongation factor-1 (EF1) complex which plays a central role in the elongation cycle during protein biosynthesis. EF1 consists of two functionally distinct units, EF1A and EF1B. EF1A catalyzes the GTP-dependent binding of aminoacyl-tRNA to the ribosomal A site concomitant with the hydrolysis of GTP. The resulting inactive EF1A:GDP complex is recycled to the active GTP form by the guanine-nucleotide exchange factor EF1B, a complex composed of at least two subunits, alpha and gamma. Metazoan EFB1 contain a third subunit, beta. The EF1B gamma subunit contains a GST fold consisting of an N-terminal TRX-fold domain and a C-terminal alpha helical domain. The GST-like domain of EF1Bgamma is believed to mediate the dimerization of the EF1 complex, which in yeast is a dimer of the heterotrimer EF1A:EF1Balpha:EF1Bgamma. In addition to its role in protein biosynthesis, EF1Bgamma may also display other functions. The recombinant rice protein has been shown to possess GSH conjugating activity. The yeast EF1Bgamma binds membranes in a calcium dependent manner and is also part of a complex that binds to the msrA (methionine sulfoxide reductase) promoter suggesting a function in the regulation of its gene expression. Pssm-ID: 239342 [Multi-domain] Cd Length: 75 Bit Score: 46.09 E-value: 3.46e-07
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| GST_N_SspA | cd03059 | GST_N family, Stringent starvation protein A (SspA) subfamily; SspA is a RNA polymerase (RNAP) ... |
2-78 | 1.92e-06 | ||||
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: 43.86 E-value: 1.92e-06
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| GST_N_GTT2_like | cd03051 | GST_N family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly ... |
2-75 | 2.41e-06 | ||||
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: 43.83 E-value: 2.41e-06
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| GST_N | pfam02798 | Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ... |
2-75 | 3.47e-06 | ||||
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to a variety of targets. Also included in the alignment, but not GSTs: S-crystallins from squid (similarity to GST previously noted); eukaryotic elongation factors 1-gamma (not known to have GST activity and similarity not previously recognized); HSP26 family of stress-related proteins including auxin-regulated proteins in plants and stringent starvation proteins in E. coli (not known to have GST activity and similarity not previously recognized). The glutathione molecule binds in a cleft between the N- and C-terminal domains - the catalytically important residues are proposed to reside in the N-terminal domain. Pssm-ID: 460698 [Multi-domain] Cd Length: 76 Bit Score: 43.45 E-value: 3.47e-06
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| GST_N_2 | cd03047 | GST_N family, unknown subfamily 2; composed of uncharacterized bacterial proteins with ... |
2-75 | 2.07e-05 | ||||
GST_N 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 TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. The sequence from Burkholderia cepacia was identified as part of a gene cluster involved in the degradation of 2,4,5-trichlorophenoxyacetic acid. Some GSTs (e.g. Class Zeta and Delta) are known to catalyze dechlorination reactions. Pssm-ID: 239345 [Multi-domain] Cd Length: 73 Bit Score: 41.15 E-value: 2.07e-05
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| GST_N_Omega | cd03055 | GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
49-76 | 1.23e-04 | ||||
GST_N family, Class Omega subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Class Omega GSTs show little or no GSH-conjugating activity towards standard GST substrates. Instead, they catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins. They contain a conserved cysteine equivalent to the first cysteine in the CXXC motif of glutaredoxins, which is a redox active residue capable of reducing GSH mixed disulfides in a monothiol mechanism. Polymorphisms of the class Omega GST genes may be associated with the development of some types of cancer and the age-at-onset of both Alzheimer's and Parkinson's diseases. Pssm-ID: 239353 [Multi-domain] Cd Length: 89 Bit Score: 39.64 E-value: 1.23e-04
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| sspA | PRK09481 | stringent starvation protein A; Provisional |
2-85 | 1.52e-04 | ||||
stringent starvation protein A; Provisional Pssm-ID: 236537 [Multi-domain] Cd Length: 211 Bit Score: 41.23 E-value: 1.52e-04
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| GST_N_Beta | cd03057 | GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
2-79 | 3.94e-04 | ||||
GST_N family, Class Beta subfamily; GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. Unlike mammalian GSTs which detoxify a broad range of compounds, the bacterial class Beta GSTs exhibit limited GSH conjugating activity with a narrow range of substrates. In addition to GSH conjugation, they also bind antibiotics and reduce the antimicrobial activity of beta-lactam drugs. The structure of the Proteus mirabilis enzyme reveals that the cysteine in the active site forms a covalent bond with GSH. Pssm-ID: 239355 [Multi-domain] Cd Length: 77 Bit Score: 37.90 E-value: 3.94e-04
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| GST_N_1 | cd03043 | GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from ... |
27-76 | 5.55e-04 | ||||
GST_N family, unknown subfamily 1; composed of uncharacterized proteins, predominantly from bacteria, 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: 239341 [Multi-domain] Cd Length: 73 Bit Score: 37.19 E-value: 5.55e-04
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| GST_C_2 | pfam13410 | Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. |
127-190 | 9.18e-04 | ||||
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043. Pssm-ID: 433185 [Multi-domain] Cd Length: 67 Bit Score: 36.53 E-value: 9.18e-04
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| GST_N_Zeta | cd03042 | GST_N family, Class Zeta subfamily; GSTs are cytosolic dimeric proteins involved in cellular ... |
2-75 | 3.43e-03 | ||||
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: 34.85 E-value: 3.43e-03
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| GST_N_GTT1_like | cd03046 | GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ... |
23-78 | 4.40e-03 | ||||
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly uncharacterized proteins with similarity to the S. cerevisiae GST protein, GTT1, and the Schizosaccharomyces pombe GST-III. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST fold contains an N-terminal TRX-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GTT1, a homodimer, exhibits GST activity with standard substrates and associates with the endoplasmic reticulum. Its expression is induced after diauxic shift and remains high throughout the stationary phase. S. pombe GST-III is implicated in the detoxification of various metals. Pssm-ID: 239344 [Multi-domain] Cd Length: 76 Bit Score: 34.78 E-value: 4.40e-03
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| Blast search parameters | ||||
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