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Conserved domains on  [gi|403063075|gb|AFR12065|]
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elongation factor 1 gamma, partial [Drosophila nr. medialis 3 KNM-2012]

Protein Classification

elongation factor 1-gamma family protein( domain architecture ID 10123605)

elongation factor 1-gamma family protein similar to elongation factor 1-gamma, a subunit of eukaryotic elongation factor 1 complex (eEF1), which plays a role in anchoring eEF1 to other cellular components

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 27-146 5.09e-58

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) 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 thioredoxin-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 to 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. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.


:

Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 181.22  E-value: 5.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISFADNEILPASCAWVFPLLGIMPQQKnPNV---KQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLH 103
Cdd:cd03181    2 AAQVLQWISFANSELLPAAATWVLPLLGIAPYNK-KAVdkaKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 403063075 104 LYEHVLDSSARSAYGNLNRWFVTILNQPQVKAVIKDFKLCEKA 146
Cdd:cd03181   81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123
EF1G pfam00647
Elongation factor 1 gamma, conserved domain;
210-277 8.71e-37

Elongation factor 1 gamma, conserved domain;


:

Pssm-ID: 459888  Cd Length: 105  Bit Score: 126.11  E-value: 8.71e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 403063075  210 KDPFDAMPKGTFNFDDFKRVYSNEEE-AKSIPYFFEKFDAENYSIWFGEYKYNEELTKTFMSCNLIGGM 277
Cdd:pfam00647   1 KHPLDALPKSSFNLDEWKRQYSNEDTrPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGF 69
 
Name Accession Description Interval E-value
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 27-146 5.09e-58

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) 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 thioredoxin-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 to 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. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 181.22  E-value: 5.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISFADNEILPASCAWVFPLLGIMPQQKnPNV---KQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLH 103
Cdd:cd03181    2 AAQVLQWISFANSELLPAAATWVLPLLGIAPYNK-KAVdkaKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 403063075 104 LYEHVLDSSARSAYGNLNRWFVTILNQPQVKAVIKDFKLCEKA 146
Cdd:cd03181   81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123
EF1G pfam00647
Elongation factor 1 gamma, conserved domain;
210-277 8.71e-37

Elongation factor 1 gamma, conserved domain;


Pssm-ID: 459888  Cd Length: 105  Bit Score: 126.11  E-value: 8.71e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 403063075  210 KDPFDAMPKGTFNFDDFKRVYSNEEE-AKSIPYFFEKFDAENYSIWFGEYKYNEELTKTFMSCNLIGGM 277
Cdd:pfam00647   1 KHPLDALPKSSFNLDEWKRQYSNEDTrPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGF 69
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
3-139 2.00e-16

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 75.70  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075   3 LTESNAIAYFLAneQLRGGKC-----PLVQAQVQQWISFADNEILPASCAWVFPLLGIMPQQKNPNVKQDAEVVLQQLNK 77
Cdd:COG0625   63 LTESLAILEYLA--ERYPEPPllpadPAARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEA 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 403063075  78 KLLDATYLAGERITLADIVVFSTLLHLYEHVLDssaRSAYGNLNRWFVTILNQPQVKAVIKD 139
Cdd:COG0625  141 RLAGGPYLAGDRFSIADIALAPVLRRLDRLGLD---LADYPNLAAWLARLAARPAFQRALAA 199
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 41-131 4.40e-11

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: 58.07  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075   41 ILPASCAWVFPLLGIMPQQKNP---NVKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYEHVLDSSaRSAY 117
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPevdEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79

                          90
                  ....*....|....
gi 403063075  118 GNLNRWFVTILNQP 131
Cdd:pfam00043  80 PNLKAWFERVAARP 93
PLN02473 PLN02473
glutathione S-transferase
 3-137 1.70e-05

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 44.59  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075   3 LTESNAIAYFLANEQL-RG----GKCPLVQAQVQQWISFADNEILPASCAWVFPLLgIMPQQKNP-------NVKQDAEV 70
Cdd:PLN02473  64 LFESRAIARYYATKYAdQGtdllGKTLEHRAIVDQWVEVENNYFYAVALPLVINLV-FKPRLGEPcdvalveELKVKFDK 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 403063075  71 VLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYEHVLDSSARSAYGNLNRWFVTILNQPQVKAVI 137
Cdd:PLN02473 143 VLDVYENRLATNRYLGGDEFTLADLTHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLM 209
 
Name Accession Description Interval E-value
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 27-146 5.09e-58

Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of Elongation Factor 1B and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Gamma subunit of Elongation Factor 1B (EF1Bgamma) 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 thioredoxin-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 to 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. Also included in this subfamily is the GST_C-like domain at the N-terminus of human valyl-tRNA synthetase (ValRS) and its homologs. Metazoan ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF.


Pssm-ID: 198290 [Multi-domain]  Cd Length: 123  Bit Score: 181.22  E-value: 5.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISFADNEILPASCAWVFPLLGIMPQQKnPNV---KQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLH 103
Cdd:cd03181    2 AAQVLQWISFANSELLPAAATWVLPLLGIAPYNK-KAVdkaKEDLKRALGVLEEHLLTRTYLVGERITLADIFVASALLR 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 403063075 104 LYEHVLDSSARSAYGNLNRWFVTILNQPQVKAVIKDFKLCEKA 146
Cdd:cd03181   81 GFETVLDPEFRKKYPNVTRWFNTVVNQPKFKAVFGEVKLCEKP 123
GST_C_ValRS_N cd10294
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ...
 27-146 1.48e-37

Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Valyl-tRNA synthetase (ValRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of human ValRS and its homologs from other vertebrates such as frog and zebrafish. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. They typically form large stable complexes with other proteins. ValRS forms a stable complex with Elongation Factor-1H (EF-1H), and together, they catalyze consecutive steps in protein biosynthesis, tRNA aminoacylation and its transfer to EF. The GST_C-like domain of ValRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. ValRSs from prokaryotes and lower eukaryotes, such as fungi and plants, do not appear to contain this GST_C-like domain.


Pssm-ID: 198327 [Multi-domain]  Cd Length: 123  Bit Score: 128.80  E-value: 1.48e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISFADNEILPASCAWVFPLLGIMPQQKNPNVKQDAEV--VLQQLNKKLLDATYLAGERITLADIVVFSTLLHL 104
Cdd:cd10294    2 CALVWQWVSFADNELTPAACAAAFPLLGLSGSDKQNQQRSLAELqrVLKVLDCYLKLRTYLVGEAITLADIAVACALLLP 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 403063075 105 YEHVLDSSARSAYGNLNRWFVTILNQPQVKAVIKDFKLCEKA 146
Cdd:cd10294   82 FKYVLDPARRESLLNVTRWFLTCVNQPEFLAVLGEVSLCEKA 123
EF1G pfam00647
Elongation factor 1 gamma, conserved domain;
210-277 8.71e-37

Elongation factor 1 gamma, conserved domain;


Pssm-ID: 459888  Cd Length: 105  Bit Score: 126.11  E-value: 8.71e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 403063075  210 KDPFDAMPKGTFNFDDFKRVYSNEEE-AKSIPYFFEKFDAENYSIWFGEYKYNEELTKTFMSCNLIGGM 277
Cdd:pfam00647   1 KHPLDALPKSSFNLDEWKRQYSNEDTrPVALPWFWENFDPEGYSLWKVDYKYNDELTLTFMSSNLIGGF 69
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
3-139 2.00e-16

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 75.70  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075   3 LTESNAIAYFLAneQLRGGKC-----PLVQAQVQQWISFADNEILPASCAWVFPLLGIMPQQKNPNVKQDAEVVLQQLNK 77
Cdd:COG0625   63 LTESLAILEYLA--ERYPEPPllpadPAARARVRQWLAWADGDLHPALRNLLERLAPEKDPAAIARARAELARLLAVLEA 140

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 403063075  78 KLLDATYLAGERITLADIVVFSTLLHLYEHVLDssaRSAYGNLNRWFVTILNQPQVKAVIKD 139
Cdd:COG0625  141 RLAGGPYLAGDRFSIADIALAPVLRRLDRLGLD---LADYPNLAAWLARLAARPAFQRALAA 199
GST_C_AIMP3 cd10305
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
 24-134 1.80e-14

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 3; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 3 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP3, also called p18 or eukaryotic translation elongation factor 1 epsilon-1 (EEF1E1), contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It specifically interacts with methionyl-tRNA synthetase (MetRS) and is translocated to the nucleus during DNA synthesis or in response to DNA damage and oncogenic stress. In the nucleus, it interacts with ATM and ATR, which are upstream kinase regulators of p53. It appears to work against DNA damage in cooperation with AIMP2, and similar to AIMP2, AIMP3 is also a haploinsufficient tumor suppressor. AIMP3 transgenic mice have shorter lifespans than wild-type mice and they show characteristics of progeria, suggesting that AIMP3 may also be involved in cellular and organismal aging.


Pssm-ID: 198338 [Multi-domain]  Cd Length: 101  Bit Score: 67.70  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  24 PLVQAQVQQWISFADNEILPAScawvfpllgimpqqknpnVKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTllh 103
Cdd:cd10305    1 AEERAQVDQWLEYRVTQVAPAS------------------DKADAKSLLKELNSYLQDRTYLVGHKLTLADVVLYYG--- 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 403063075 104 LYEHVLDSSA--RSAYGNLNRWFVTILNQPQVK 134
Cdd:cd10305   60 LHPIMKDLSPqeKEQYLNVSRWFDHVQHLPGIR 92
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
 27-130 1.00e-12

Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA synthetases and similar domains; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl-tRNA synthetase (AaRS)-like subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of some eukaryotic AaRSs, as well as similar domains found in proteins involved in protein synthesis including Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2 (AIMP2), AIMP3, and eukaryotic translation Elongation Factor 1 beta (eEF1b). AaRSs comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. AaRSs in this subfamily include GluRS from lower eukaryotes, as well as GluProRS, MetRS, and CysRS from higher eukaryotes. AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex found in higher eukaryotes. The GST_C-like domain is involved in protein-protein interactions, mediating the formation of aaRS complexes such as the MetRS-Arc1p-GluRS ternary complex in lower eukaryotes and the multi-aaRS complex in higher eukaryotes, that act as molecular hubs for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198322 [Multi-domain]  Cd Length: 82  Bit Score: 62.33  E-value: 1.00e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISFADNEilpascawvfpllgimpqqknpNVKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYE 106
Cdd:cd10289    2 AAQVDQWLDLAGSL----------------------LKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQ 59

                         90       100
                 ....*....|....*....|....
gi 403063075 107 hVLDSSARSAYGNLNRWFVTILNQ 130
Cdd:cd10289   60 -KLSDKEKKKFPHVTRWFNHIQNL 82
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 30-124 7.42e-12

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: 60.59  E-value: 7.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  30 VQQWISFADNEILPASCAWVFPLLGIMP--QQKNPNVKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYEH 107
Cdd:cd00299    1 VRALEDWADATLAPPLVRLLYLEKVPLPkdEAAVEAAREELPALLAALEQLLAGRPYLAGDQFSLADVALAPVLARLEAL 80

                         90
                 ....*....|....*..
gi 403063075 108 VLDSSARSAYGNLNRWF 124
Cdd:cd00299   81 GPYYDLLDEYPRLKAWY 97
GST_C_GluProRS_N cd10309
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ...
 27-130 3.10e-11

Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional Glutamyl-Prolyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, bifunctional GluRS-Prolyl-tRNA synthetase (GluProRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluProRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluProRS may be involved in protein-protein interactions, mediating the formation of the multi-aaRS complex in higher eukaryotes. The multi-aaRS complex acts as a molecular hub for protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198342 [Multi-domain]  Cd Length: 81  Bit Score: 58.10  E-value: 3.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISFAdneILPASCawvfpllgimpqqknpnvKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYE 106
Cdd:cd10309    2 QTEVDHWISFS---AGRLSC------------------DQDFSSALSYLDKALSLRTYLVGNSLTLADFAVWAALRGNGE 60

                         90       100
                 ....*....|....*....|....
gi 403063075 107 HvldSSARSAYGNLNRWFVTILNQ 130
Cdd:cd10309   61 W---LASKEKYVNVTRWFKFISSQ 81
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 41-131 4.40e-11

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: 58.07  E-value: 4.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075   41 ILPASCAWVFPLLGIMPQQKNP---NVKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYEHVLDSSaRSAY 117
Cdd:pfam00043   1 LMDLRMQIALLPYVPPEEKKEPevdEALEKVARVLSALEEVLKGQTYLVGDKLTLADIALAPALLWLYELDPACL-REKF 79

                          90
                  ....*....|....
gi 403063075  118 GNLNRWFVTILNQP 131
Cdd:pfam00043  80 PNLKAWFERVAARP 93
GST_C_7 cd03206
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ...
 30-124 9.76e-10

C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 7; composed of uncharacterized 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: 198315 [Multi-domain]  Cd Length: 100  Bit Score: 54.54  E-value: 9.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  30 VQQWISFADNEIL--PAScAWVFPLLGiMPqqKNP-NVKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYE 106
Cdd:cd03206    1 VQRWLSFAAGEIAhgPAA-ARLIHLFG-AP--LDPeRARAISHRLLRLLDQHLAGRDWLAGDRPTIADVACYPYIALAPE 76

                         90
                 ....*....|....*...
gi 403063075 107 HVLDssaRSAYGNLNRWF 124
Cdd:cd03206   77 GGVS---LEPYPAIRAWL 91
GST_C_Beta cd03188
C-terminal, alpha helical domain of Class Beta Glutathione S-transferases; Glutathione ...
 28-137 5.47e-07

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: 47.24  E-value: 5.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  28 AQVQQWISFADNEILPASCAWVFP-LLGIMPQQknPNVKQDA----EVVLQQLNKKLLDATYLAGERITLADIVVFsTLL 102
Cdd:cd03188    4 ARLLEWLNFIASELHKAFGPLFYPaRWADDALA--EEVKAAArerlERRLAYLDAQLAGGPYLLGDQFSVADAYLF-VVL 80

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 403063075 103 HLYEHV-LDssaRSAYGNLNRWFVTILNQPQVKAVI 137
Cdd:cd03188   81 RWARAVgLD---LSDWPHLAAYLARVAARPAVQAAL 113
GST_C_8 cd03207
C-terminal, alpha helical domain of an unknown subfamily 8 of Glutathione S-transferases; ...
 32-124 6.69e-07

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: 46.90  E-value: 6.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  32 QWISFADNEILPASCAWV--FPLLGIMPQQKNPNVKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYEHVL 109
Cdd:cd03207    3 RWLFFAAGTVEPPLLNKAlgRFFEPPWGEPAIAAAYGDLDERLAALEAALAGRPYLVGERFSAADLLLASVLRWARAFGL 82

                         90
                 ....*....|....*
gi 403063075 110 dssaRSAYGNLNRWF 124
Cdd:cd03207   83 ----LPEYPALRAYV 93
GST_C_Arc1p_N_like cd10304
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ...
 24-133 8.76e-07

Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA synthetase cofactor 1 and similar proteins; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase cofactor 1 (Arc1p)-like subfamily; Arc1p, also called GU4 nucleic binding protein 1 (G4p1) or p42, is a tRNA-aminoacylation and nuclear-export cofactor. It contains a domain in the N-terminal region with similarity to the C-terminal alpha helical domain of GSTs. This domain mediates the association of the aminoacyl tRNA synthetases (aaRSs), MetRS and GluRS, in yeast to form a stable stoichiometric ternany complex. The GST_C-like domain of Arc1p is a protein-protein interaction domain containing two binding sites which enable it to bind the two aaRSs simultaneously and independently. The MetRS-Arc1p-GluRS complex selectively recruits and aminoacylates its cognate tRNAs without additional cofactors. Arc1p also plays a role in the transport of tRNA from the nucleus to the cytoplasm. It may also control the subcellular distribution of GluRS in the cytoplasm, nucleoplasm, and the mitochondrial matrix.


Pssm-ID: 198337 [Multi-domain]  Cd Length: 100  Bit Score: 46.21  E-value: 8.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  24 PLVQAQVQQWISFADNeiLPASCAWvfpllgimpqqknpnvkqdaEVVLQQLNKKLLDATYLAG-ERITLADIVVFSTLL 102
Cdd:cd10304    1 PEQSAEVAQWLSVAKS--GPVSKDV--------------------QETLGQLNLHLRTRTFLLGtGKPSVADVAVFEAVL 58

                         90       100       110
                 ....*....|....*....|....*....|...
gi 403063075 103 HLYEHVLDSSA--RSAYGNLNRWFVTILNQPQV 133
Cdd:cd10304   59 PVVKEWSDEVKtgYAKYRHILRWVDYVQNLLLF 91
GST_C_2 cd03180
C-terminal, alpha helical domain of an unknown subfamily 2 of Glutathione S-transferases; ...
 27-124 3.82e-06

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: 44.96  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISFADNEILPAscaWVFPLLGIMpqqKNPNVKQDAEVV---LQQLNK--KLLDAT-----YLAGERITLADIV 96
Cdd:cd03180    3 RALADRWMDWQTSTLNPA---FRYAFWGLV---RTPPEQRDPAAIaasLAACNKlmAILDAQlarqaYLAGDRFTLADIA 76

                         90       100
                 ....*....|....*....|....*...
gi 403063075  97 VFSTLLHLYEHVLDssaRSAYGNLNRWF 124
Cdd:cd03180   77 LGCSVYRWLELPIE---RPALPHLERWY 101
GST_C_Ure2p_like cd03178
C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; ...
 27-134 5.39e-06

C-terminal, alpha helical domain of Ure2p and related Glutathione S-transferase-like proteins; Glutathione S-transferase (GST) C-terminal domain family, Ure2p-like subfamily; composed of the Saccharomyces cerevisiae Ure2p, YfcG and YghU from Escherichia coli, and related GST-like proteins. Ure2p is a regulator for nitrogen catabolism in yeast. It represses the expression of several gene products involved in the use of poor nitrogen sources when rich sources are available. A transmissible conformational change of Ure2p results in a prion called [Ure3], an inactive, self-propagating and infectious amyloid. Ure2p displays a GST fold containing an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain. The N-terminal thioredoxin-fold domain is sufficient to induce the [Ure3] phenotype and is also called the prion domain of Ure2p. In addition to its role in nitrogen regulation, Ure2p confers protection to cells against heavy metal ion and oxidant toxicity, and shows glutathione (GSH) peroxidase activity. YfcG and YghU are two of the nine GST homologs in the genome of Escherichia coli. They display very low or no GSH transferase, but show very good disulfide bond oxidoreductase activity. YghU also shows modest organic hydroperoxide reductase activity. GSTs are cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of GSH with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain.


Pssm-ID: 198288 [Multi-domain]  Cd Length: 110  Bit Score: 44.55  E-value: 5.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISFADNEILPASCAWVFPLLgiMPQQKNPNV----KQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLL 102
Cdd:cd03178    2 RAEVLQWLFFQMSGLGPMFGQAGHFLY--FAPEKIPYAieryTDEVKRLYGVLDKRLSDRPYLAGEEYSIADIALYPWTH 79

                         90       100       110
                 ....*....|....*....|....*....|..
gi 403063075 103 HLYEHVLDSsaRSAYGNLNRWFVTILNQPQVK 134
Cdd:cd03178   80 YADLGGFAD--LSEYPNVKRWLERIAARPAVQ 109
GST_C_Delta_Epsilon cd03177
C-terminal, alpha helical domain of Class Delta and Epsilon Glutathione S-transferases; ...
 25-147 1.67e-05

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: 43.29  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  25 LVQAQVQQWISFaDNEILPASCAWVFPLLGIMPQQKNPNVKQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTLLHL 104
Cdd:cd03177    1 KKRAIVNQRLFF-DSGTLYQRLRDYYYPILFGGAEPPEEKLDKLEEALEFLETFLEGSDYVAGDQLTIADLSLVATVSTL 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 403063075 105 YEHVLDssaRSAYGNLNRWFvtilnqPQVKAVIKDFKLCEKAL 147
Cdd:cd03177   80 EVVGFD---LSKYPNVAAWY------ERLKALPPGEEENGEGA 113
PLN02473 PLN02473
glutathione S-transferase
 3-137 1.70e-05

glutathione S-transferase


Pssm-ID: 166114 [Multi-domain]  Cd Length: 214  Bit Score: 44.59  E-value: 1.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075   3 LTESNAIAYFLANEQL-RG----GKCPLVQAQVQQWISFADNEILPASCAWVFPLLgIMPQQKNP-------NVKQDAEV 70
Cdd:PLN02473  64 LFESRAIARYYATKYAdQGtdllGKTLEHRAIVDQWVEVENNYFYAVALPLVINLV-FKPRLGEPcdvalveELKVKFDK 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 403063075  71 VLQQLNKKLLDATYLAGERITLADIVVFSTLLHLYEHVLDSSARSAYGNLNRWFVTILNQPQVKAVI 137
Cdd:PLN02473 143 VLDVYENRLATNRYLGGDEFTLADLTHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLM 209
PRK10542 PRK10542
glutathionine S-transferase; Provisional
 3-138 1.92e-05

glutathionine S-transferase; Provisional


Pssm-ID: 182533 [Multi-domain]  Cd Length: 201  Bit Score: 44.29  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075   3 LTESNAIAYFLANE----QLRGGKCPLVQAQVQQWISFADNEILPASCAWVFPllgIMPQQKNPNVKQDAEVVLQQLNKK 78
Cdd:PRK10542  63 LTEGVAIMQYLADSvpdrQLLAPVGSLSRYHTIEWLNYIATELHKGFTPLFRP---DTPEEYKPTVRAQLEKKFQYVDEA 139

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  79 LLDATYLAGERITLADIVVFSTLLHLYEHVLDSSARSAygnLNRWFVTILNQPQVKAVIK 138
Cdd:PRK10542 140 LADEQWICGQRFTIADAYLFTVLRWAYAVKLNLEGLEH---IAAYMQRVAERPAVAAALK 196
PLN02907 PLN02907
glutamate-tRNA ligase
 3-135 2.48e-05

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 45.49  E-value: 2.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075   3 LTESNAIAYFLANEQLR---GGKCPLVQAQVQQWISFAdNEILPAScawvfpllgimpqqknpnvkqDAEVVLQQLNKKL 79
Cdd:PLN02907  49 LTGTNVLLRYIARSASLpgfYGQDAFESSQVDEWLDYA-PTFSSGS---------------------EFENACEYVDGYL 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 403063075  80 LDATYLAGERITLADIVVFSTLL---HLYEHVLDSsarSAYGNLNRWFVTILNQPQVKA 135
Cdd:PLN02907 107 ASRTFLVGYSLTIADIAIWSGLAgsgQRWESLRKS---KKYQNLVRWFNSISAEYSDIL 162
GST_C_3 pfam14497
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 72-138 3.19e-05

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


Pssm-ID: 464190 [Multi-domain]  Cd Length: 104  Bit Score: 42.16  E-value: 3.19e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 403063075   72 LQQLNKKLLDA--TYLAGERITLADIVVFSTLLHLyEHVLDSSARSAYGNLNRWFVTILNQPQVKAVIK 138
Cdd:pfam14497  35 LGYFEKVLNKNggGYLVGDKLTYADLALFQVLDGL-LYPKAPDALDKYPKLKALHERVAARPNIKAYLA 102
GST_C_2 pfam13410
Glutathione S-transferase, C-terminal domain; This domain is closely related to pfam00043.
 72-124 3.32e-05

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


Pssm-ID: 433185 [Multi-domain]  Cd Length: 67  Bit Score: 41.15  E-value: 3.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 403063075   72 LQQLNKKLLDATYLAGERITLADIVVFSTL--LHLYEHVLDSsaRSAYGNLNRWF 124
Cdd:pfam13410  13 LDALEARLADGPGLLGDRPTLADIALAPVLarLDAAYPGLDL--REGYPRLRAWL 65
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 24-133 4.96e-05

C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae GTT2-like subfamily; composed of predominantly uncharacterized proteins with similarity to the Saccharomyces 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 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. 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: 198291 [Multi-domain]  Cd Length: 116  Bit Score: 41.92  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  24 PLVQAQVQQWISFADNEIL-PASCAWVFpllgIMPQQKNPNVKQDAEVVLQQ----------LNKKLLDATYLAGERITL 92
Cdd:cd03182    2 PLEKALIEMWQRRAELQGLaPVFQAFRH----ATPGLKPDREVQVPEWGERNkkrvidflpvLDKRLAESPYVAGDRFSI 77

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 403063075  93 ADIVVFSTLlhLYEHVLDSSARSAYGNLNRWFVTILNQPQV 133
Cdd:cd03182   78 ADITAFVAL--DFAKNLKLPVPEELTALRRWYERMAARPSA 116
GST_C_Phi cd03187
C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione ...
 28-137 5.23e-05

C-terminal, alpha helical domain of Class Phi Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain 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 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 Phi GST subfamily has experience extensive gene duplication. The Arabidopsis and Oryza genomes contain 13 and 16 Tau 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: 198296 [Multi-domain]  Cd Length: 118  Bit Score: 41.83  E-value: 5.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  28 AQVQQWISFADNEILPASCAWVFPLL--GIMPQQKNPNV----KQDAEVVLQQLNKKLLDATYLAGERITLADIVVFSTL 101
Cdd:cd03187    4 ALVEQWLEVEAHQFDPPASKLVFELVfkPMLGLKTDEAVveenEAKLKKVLDVYEARLSKSKYLAGDSFTLADLSHLPNL 83

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 403063075 102 LHL----YEHVLDSsarsaYGNLNRWFVTILNQPQVKAVI 137
Cdd:cd03187   84 HYLmatpSKKLFDS-----RPHVKAWWEDISARPAWKKVL 118
GST_C_GluRS_N cd10306
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ...
 28-127 1.02e-04

Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; Glutathione S-transferase (GST) C-terminal domain family, Glutamyl-tRNA synthetase (GluRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of GluRS from lower eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. The GST_C-like domain of GluRS is involved in protein-protein interactions. This domain mediates the formation of the MetRS-Arc1p-GluRS ternary complex found in lower eukaryotes, which is considered an evolutionary intermediate between prokaryotic aaRS and the multi-aaRS complex found in higher eukaryotes. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198339 [Multi-domain]  Cd Length: 87  Bit Score: 40.03  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  28 AQVQQWISFADNEILPAScawvFPLLgimpqqknpnvkqdaEVVLQQLNKKLLDATYLAGERITLADIVVFSTllhlyeh 107
Cdd:cd10306    5 EQVAEWIDFATTLLVLKD----FKAL---------------SQALEELDSHLTLRTFIVGYSLSLADIAVWGA------- 58

                         90       100
                 ....*....|....*....|....*..
gi 403063075 108 vLDSSA-------RSAYGNLNRWFVTI 127
Cdd:cd10306   59 -LRGNGvagslikNKVYVNLSRWFSFL 84
GST_C_Theta cd03183
C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione ...
 27-124 1.27e-04

C-terminal, alpha helical domain of Class Theta Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Class Theta subfamily; composed of eukaryotic class Theta GSTs and bacterial dichloromethane (DCM) dehalogenase. 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. Mammalian class Theta GSTs show poor GSH conjugating activity towards the standard substrates, CDNB and ethacrynic acid, differentiating them from other mammalian GSTs. GSTT1-1 shows similar cataytic activity as bacterial DCM dehalogenase, catalyzing the GSH-dependent hydrolytic dehalogenation of dihalomethanes. This is an essential process in methylotrophic bacteria to enable them to use chloromethane and DCM as sole carbon and energy sources. The presence of polymorphisms in human GSTT1-1 and its relationship to the onset of diseases including cancer is the subject of many studies. Human GSTT2-2 exhibits a highly specific sulfatase activity, catalyzing the cleavage of sulfate ions from aralkyl sufate esters, but not from the aryl or alkyl sulfate esters.


Pssm-ID: 198292 [Multi-domain]  Cd Length: 126  Bit Score: 40.66  E-value: 1.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  27 QAQVQQWISF-ADNEILPAS----CAWVFPLLGI--MPQQKNPNVKQDAEVVLQQLNKKLL-DATYLAGERITLADIVVF 98
Cdd:cd03183    2 RARVDEYLAWqHTNLRLGCAayfwQKVLLPLFGGtpVSPEKVKKAEENLEESLDLLENKFLkDKPFLAGDEISIADLSAI 81

                         90       100
                 ....*....|....*....|....*.
gi 403063075  99 STLLHLyeHVLDSSARSAYGNLNRWF 124
Cdd:cd03183   82 CEIMQP--EAAGYDVFEGRPKLAAWR 105
GST_C_MetRS_N cd10307
Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase ...
 72-127 2.35e-04

Glutathione S-transferase C-terminal-like, alpha helical domain of Methionyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Methionyl-tRNA synthetase (MetRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of MetRS from higher eukaryotes. Aminoacyl-tRNA synthetases (aaRSs) comprise a family of enzymes that catalyze the coupling of amino acids with their matching tRNAs. This involves the formation of an aminoacyl adenylate using ATP, followed by the transfer of the activated amino acid to the 3'-adenosine moiety of the tRNA. AaRSs may also be involved in translational and transcriptional regulation, as well as in tRNA processing. MetRS is a class I aaRS, containing a Rossman fold catalytic core. It recognizes the initiator tRNA as well as the Met-tRNA for protein chain elongation. The GST_C-like domain of MetRS from higher eukaryotes is likely involved in protein-protein interactions, to mediate the formation of the multi-aaRS complex that acts as a molecular hub to coordinate protein synthesis. AaRSs from prokaryotes, which are active as dimers, do not contain this GST_C-like domain.


Pssm-ID: 198340 [Multi-domain]  Cd Length: 102  Bit Score: 39.40  E-value: 2.35e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 403063075  72 LQQLNKKLLDA-TYLAGERITLADIVVFSTLLHLYehVLDSSARSAYGNLNRWFVTI 127
Cdd:cd10307   45 LVHLDQSLLKKsTPLLGDKLSSADVVVWSALYPLG--TDKSALPENLDNLRRWFQNV 99
GST_C_5 cd03196
C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; ...
 66-136 6.08e-04

C-terminal, alpha helical domain of an unknown subfamily 5 of Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, unknown subfamily 5; 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: 198305 [Multi-domain]  Cd Length: 115  Bit Score: 38.67  E-value: 6.08e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 403063075  66 QDAEVVLQQLNKKLLDATYLAGERITLADIVVF-------STLLHLYEHvldssarSAYGNLNRWFVTILNQPQVKAV 136
Cdd:cd03196   44 AQAEEFLAELEARLSQHAYLFGDRPSLADYAIFpfvrqfaHVDRDWFDA-------SPYPNLRRWLNRFLQSPLFSKI 114
GST_C_AIMP2 cd03200
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
 71-130 1.42e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein 2; Glutathione S-transferase (GST) C-terminal domain family, Aminoacyl tRNA synthetase complex-Interacting Multifunctional Protein (AIMP) 2 subfamily; AIMPs are non-enzymatic cofactors that play critical roles in the assembly and formation of a macromolecular multi-tRNA synthetase protein complex that functions as a molecular hub to coordinate protein synthesis. There are three AIMPs, named AIMP1-3, which play diverse regulatory roles. AIMP2, also called p38 or JTV-1, contains a C-terminal domain with similarity to the C-terminal alpha helical domain of GSTs. It plays an important role in the control of cell fate via antiproliferative (by enhancing the TGF-beta signal) and proapoptotic (activation of p53 and TNF-alpha) activities. Its roles in the control of cell proliferation and death suggest that it is a potent tumor suppressor. AIMP2 heterozygous mice with lower than normal expression of AIMP2 show high susceptibility to tumorigenesis. AIMP2 is also a substrate of Parkin, an E3 ubiquitin ligase that is involved in the ubiquitylation and proteasomal degradation of its substrates. Mutations in the Parkin gene is found in 50% of patients with autosomal-recessive early-onset parkinsonism. The accumulation of AIMP2, due to impaired Parkin function, may play a role in the pathogenesis of Parkinson's disease.


Pssm-ID: 198309 [Multi-domain]  Cd Length: 96  Bit Score: 37.11  E-value: 1.42e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 403063075  71 VLQQLNKKLLDATYLAGERITLADIVVFSTLLHLyehvldSSARSAYGNLNRWFVTILNQ 130
Cdd:cd03200   43 VLRALNSALGRSPWLVGSEPTVADIALWSAVLQT------GLASGAPANVQRWMKSCENL 96
PRK11752 PRK11752
putative S-transferase; Provisional
 75-134 1.63e-03

putative S-transferase; Provisional


Pssm-ID: 183298 [Multi-domain]  Cd Length: 264  Bit Score: 39.14  E-value: 1.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 403063075  75 LNKKLLDATYLAGERITLADIVVFSTLLHLYEHVLDSSAR----SAYGNLNRWFVTILNQPQVK 134
Cdd:PRK11752 190 LDKQLAEHEYIAGDEYTIADIAIWPWYGNLVLGNLYDAAEfldvGSYKHVQRWAKEIAERPAVK 253
GST_C_YfcG_like cd10291
C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and ...
 75-135 1.73e-03

C-terminal, alpha helical domain of Escherichia coli YfcG Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YfcG-like subfamily; composed of the Escherichia coli YfcG and related 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YfcG is one of nine GST homologs in Escherichia coli. It is expressed predominantly during the late stationary phase where the predominant form of GSH is glutathionylspermidine (GspSH), suggesting that YfcG might interact with GspSH. It has very low or no GSH transferase or peroxidase activity, but displays a unique disulfide bond reductase activity that is comparable to thioredoxins (TRXs) and glutaredoxins (GRXs). However, unlike TRXs and GRXs, YfcG does not contain a redox active cysteine residue and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YcfG reveals a bound GSSG molecule in its active site. The actual physiological substrates for YfcG are yet to be identified.


Pssm-ID: 198324 [Multi-domain]  Cd Length: 110  Bit Score: 37.25  E-value: 1.73e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 403063075  75 LNKKLLDATYLAGERITLADIVVFS--TLLHLYEHVLDSsarsaYGNLNRWFVTILNQPQVKA 135
Cdd:cd10291   52 LDRRLAKSKYLAGDEYSIADIAIWPwvARHEWQGIDLAD-----FPNLKRWFERLAARPAVQK 109
GST_C_YghU_like cd10292
C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and ...
 72-134 1.96e-03

C-terminal, alpha helical domain of Escherichia coli Yghu Glutathione S-transferases and related uncharacterized proteins; Glutathione S-transferase (GST) C-terminal domain family, YghU-like subfamily; composed of the Escherichia coli YghU and related 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. GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. The GST active site is located in a cleft between the N- and C-terminal domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. YghU is one of nine GST homologs in the genome of Escherichia coli. It is similar to Escherichia coli YfcG in that it has poor GSH transferase activity towards typical substrates. It shows modest reductase activity towards some organic hydroperoxides. Like YfcG, YghU also shows good disulfide bond oxidoreductase activity comparable to the activities of glutaredoxins and thioredoxins. YghU does not contain a redox active cysteine residue, and may use a bound thiol disulfide couple such as 2GSH/GSSG for activity. The crystal structure of YghU reveals two GSH molecules bound in its active site.


Pssm-ID: 198325 [Multi-domain]  Cd Length: 118  Bit Score: 37.44  E-value: 1.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 403063075  72 LQQLNKKLLDATYLAGERITLADIVVFSTLLHLYEHVLDSSAR----SAYGNLNRWFVTILNQPQVK 134
Cdd:cd10292   49 LDVLDRQLATHKYLAGDEYTIADMAIWPWYGGLALGSLYDAAEfldvDEYKHVQRWAKDIAARPAVK 115
GST_C_Omega_like cd03190
C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione ...
 72-134 2.08e-03

C-terminal, alpha helical domain of Class Omega-like Glutathione S-transferases; Glutathione S-transferase (GST) C-terminal domain family, Saccharomyces cerevisiae Omega-like subfamily; composed of three Saccharomyces cerevisiae GST omega-like (Gto) proteins, Gto1p, Gto2p (also known as Extracellular mutant protein 4 or ECM4p), and Gto3p, as well as similar uncharacterized proteins from fungi and bacteria. The three Saccharomyces cerevisiae Gto proteins are omega-class GSTs with low or no GST activity against standard substrates, but have glutaredoxin/thiol oxidoreductase and dehydroascorbate reductase activity through a single cysteine residue in the active site. Gto1p is located in the peroxisomes while Gto2p and Gto3p are cytosolic. The gene encoding Gto2p, called ECM4, is involved in cell surface biosynthesis and architecture. S. cerevisiae ECM4 mutants show increased amounts of the cell wall hexose, N-acetylglucosamine. More recently, global gene expression analysis shows that ECM4 is upregulated during genotoxic conditions and together with the expression profiles of 18 other genes could potentially differentiate between genotoxic and cytotoxic insults in yeast.


Pssm-ID: 198299 [Multi-domain]  Cd Length: 142  Bit Score: 37.55  E-value: 2.08e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 403063075  72 LQQLNKKLLDATYLAGERITLADIVVFSTLLHL---YEHVLDSSAR--SAYGNLNRWFVTILNQPQVK 134
Cdd:cd03190   46 LDKLEKRLSKQPYLLGDRLTEADIRLFTTLIRFdpvYHQHFKCNLKtiRDYPNLWRYLRRLYQNPGVF 113
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
 52-127 2.61e-03

Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation Elongation Factor 1 beta; Glutathione S-transferase (GST) C-terminal domain family, eukaryotic translation Elongation Factor 1 beta (eEF1b) subfamily; eEF1b is a component 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. eEF1b contains a GST_C-like alpha helical domain at the N-terminal region and a C-terminal guanine nucleotide exchange domain. The GST_C-like domain likely functions as a protein-protein interaction domain, similar to the function of the GST_C-like domains of EF1Bgamma and various aminoacyl-tRNA synthetases (aaRSs) from higher eukaryotes.


Pssm-ID: 198341  Cd Length: 82  Bit Score: 36.25  E-value: 2.61e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 403063075  52 LLGIMPQQKNPNVKQDAevVLQQLNKKLLDATYLAGERITLADIVVFSTLlhlyeHVLDSSARsaYGNLNRWFVTI 127
Cdd:cd10308   13 LLGVSLDGSFADLKTDK--GLEALNEYLADRSYISGYSPSQADVEVFDKL-----KKAPDATK--FPHLARWYRHI 79
 
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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