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Conserved domains on  [gi|766281589|gb|AJR53007|]
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Gtt1p [Saccharomyces cerevisiae YJM1527]

Protein Classification

glutathione S-transferase( domain architecture ID 10122657)

glutathione S-transferase catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 93-218 3.26e-44

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


:

Pssm-ID: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 144.37  E-value: 3.26e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589  93 MSEDADIADQINYYLFYVEGSLQPPLMIEFILSKVKDSGMPFPIsYLARKVADKISQAYSSGEVKNQFDFVEGEISKnNG 172
Cdd:cd03189    1 PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFFR-PISRKIADKPLQAFINPELKRHLDFLEDHLAK-HP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 766281589 173 YLVDGKLSGADILMSFPLQMAFERKFAApEDYPAISKWLKTITSEE 218
Cdd:cd03189   79 YFAGDELTAADIMMSFPLEAALARGPLL-EQYPNIAAYLERIEARP 123
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 6-87 3.45e-21

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: 83.71  E-value: 3.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589   6 IKVHWLDHSRAFRLLWLLDHLNLEYEIVPYKRDANFRAPPELKKIHPLGRSPLLEVQDRetgkkkILAESGFIFQYVLQH 85
Cdd:cd03046    1 ITLYHLPRSRSFRILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDL------VLTESAAIILYLAEK 74


                 ..
gi 766281589  86 FD 87
Cdd:cd03046   75 YG 76
 
Name Accession Description Interval E-value
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 93-218 3.26e-44

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


Pssm-ID: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 144.37  E-value: 3.26e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589  93 MSEDADIADQINYYLFYVEGSLQPPLMIEFILSKVKDSGMPFPIsYLARKVADKISQAYSSGEVKNQFDFVEGEISKnNG 172
Cdd:cd03189    1 PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFFR-PISRKIADKPLQAFINPELKRHLDFLEDHLAK-HP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 766281589 173 YLVDGKLSGADILMSFPLQMAFERKFAApEDYPAISKWLKTITSEE 218
Cdd:cd03189   79 YFAGDELTAADIMMSFPLEAALARGPLL-EQYPNIAAYLERIEARP 123
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 6-87 3.45e-21

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: 83.71  E-value: 3.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589   6 IKVHWLDHSRAFRLLWLLDHLNLEYEIVPYKRDANFRAPPELKKIHPLGRSPLLEVQDRetgkkkILAESGFIFQYVLQH 85
Cdd:cd03046    1 ITLYHLPRSRSFRILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDL------VLTESAAIILYLAEK 74


                 ..
gi 766281589  86 FD 87
Cdd:cd03046   75 YG 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
29-230 2.98e-19

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 82.25  E-value: 2.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589  29 EYEIVPYKRDANFRAPPELKKIHPLGRSPLLEVQDRetgkkkILAESGFIFQYVLQHFDHSHvLMSEDADIADQINYYLF 108
Cdd:COG0625   26 PYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGL------VLTESLAILEYLAERYPEPP-LLPADPAARARVRQWLA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589 109 YVEGSLQPPLMIEFilskvkDSGMPFPISYLARKVADKISQAyssgevknqFDFVEGEISKnNGYLVDGKLSGADILMSF 188
Cdd:COG0625   99 WADGDLHPALRNLL------ERLAPEKDPAAIARARAELARL---------LAVLEARLAG-GPYLAGDRFSIADIALAP 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 766281589 189 PLQMAFERKFAApEDYPAISKWLKTITSEESYAASKEKARAL 230
Cdd:COG0625  163 VLRRLDRLGLDL-ADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 4-84 2.95e-14

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: 65.40  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589    4 PIIKVHWLDHSRAFRLLWLLDHLNLEYEIVPYKRDANFRAPPELKKIHPLGRSPLLEVQDretgkkKILAESGFIFQYVL 83
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGG------KKLTESRAILEYIA 75


                  .
gi 766281589   84 Q 84
Cdd:pfam02798  76 R 76
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 137-218 2.82e-13

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: 63.46  E-value: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589  137 SYLARKVADKISQAYSSGEVKNQFDFVEGEIsKNNGYLVDGKLSGADILMSFPLQMAFERKFAAP-EDYPAISKWLKTIT 215
Cdd:pfam00043  12 PYVPPEEKKEPEVDEALEKVARVLSALEEVL-KGQTYLVGDKLTLADIALAPALLWLYELDPACLrEKFPNLKAWFERVA 90


                  ...
gi 766281589  216 SEE 218
Cdd:pfam00043  91 ARP 93
 
Name Accession Description Interval E-value
GST_C_GTT1_like cd03189
C-terminal, alpha helical domain of GTT1-like Glutathione S-transferases; Glutathione ...
 93-218 3.26e-44

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


Pssm-ID: 198298 [Multi-domain]  Cd Length: 123  Bit Score: 144.37  E-value: 3.26e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589  93 MSEDADIADQINYYLFYVEGSLQPPLMIEFILSKVKDSGMPFPIsYLARKVADKISQAYSSGEVKNQFDFVEGEISKnNG 172
Cdd:cd03189    1 PPPDTAEYADYLYWLHFAEGSLMPPLLLKLVFGKIGEAPPPFFR-PISRKIADKPLQAFINPELKRHLDFLEDHLAK-HP 78

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 766281589 173 YLVDGKLSGADILMSFPLQMAFERKFAApEDYPAISKWLKTITSEE 218
Cdd:cd03189   79 YFAGDELTAADIMMSFPLEAALARGPLL-EQYPNIAAYLERIEARP 123
GST_N_GTT1_like cd03046
GST_N family, Saccharomyces cerevisiae GTT1-like subfamily; composed of predominantly ...
 6-87 3.45e-21

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: 83.71  E-value: 3.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589   6 IKVHWLDHSRAFRLLWLLDHLNLEYEIVPYKRDANFRAPPELKKIHPLGRSPLLEVQDRetgkkkILAESGFIFQYVLQH 85
Cdd:cd03046    1 ITLYHLPRSRSFRILWLLEELGLPYELVLYDRGPGEQAPPEYLAINPLGKVPVLVDGDL------VLTESAAIILYLAEK 74


                 ..
gi 766281589  86 FD 87
Cdd:cd03046   75 YG 76
GstA COG0625
Glutathione S-transferase [Posttranslational modification, protein turnover, chaperones];
29-230 2.98e-19

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


Pssm-ID: 440390 [Multi-domain]  Cd Length: 205  Bit Score: 82.25  E-value: 2.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589  29 EYEIVPYKRDANFRAPPELKKIHPLGRSPLLEVQDRetgkkkILAESGFIFQYVLQHFDHSHvLMSEDADIADQINYYLF 108
Cdd:COG0625   26 PYELVPVDLAKGEQKSPEFLALNPLGKVPVLVDDGL------VLTESLAILEYLAERYPEPP-LLPADPAARARVRQWLA 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589 109 YVEGSLQPPLMIEFilskvkDSGMPFPISYLARKVADKISQAyssgevknqFDFVEGEISKnNGYLVDGKLSGADILMSF 188
Cdd:COG0625   99 WADGDLHPALRNLL------ERLAPEKDPAAIARARAELARL---------LAVLEARLAG-GPYLAGDRFSIADIALAP 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 766281589 189 PLQMAFERKFAApEDYPAISKWLKTITSEESYAASKEKARAL 230
Cdd:COG0625  163 VLRRLDRLGLDL-ADYPNLAAWLARLAARPAFQRALAAAEPD 203
GST_N pfam02798
Glutathione S-transferase, N-terminal domain; Function: conjugation of reduced glutathione to ...
 4-84 2.95e-14

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: 65.40  E-value: 2.95e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589    4 PIIKVHWLDHSRAFRLLWLLDHLNLEYEIVPYKRDANFRAPPELKKIHPLGRSPLLEVQDretgkkKILAESGFIFQYVL 83
Cdd:pfam02798   2 VLTLYGIRGSPRAHRIRWLLAEKGVEYEIVPLDFGAGPEKSPELLKLNPLGKVPALEDGG------KKLTESRAILEYIA 75


                  .
gi 766281589   84 Q 84
Cdd:pfam02798  76 R 76
GST_C pfam00043
Glutathione S-transferase, C-terminal domain; GST conjugates reduced glutathione to a variety ...
 137-218 2.82e-13

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: 63.46  E-value: 2.82e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589  137 SYLARKVADKISQAYSSGEVKNQFDFVEGEIsKNNGYLVDGKLSGADILMSFPLQMAFERKFAAP-EDYPAISKWLKTIT 215
Cdd:pfam00043  12 PYVPPEEKKEPEVDEALEKVARVLSALEEVL-KGQTYLVGDKLTLADIALAPALLWLYELDPACLrEKFPNLKAWFERVA 90


                  ...
gi 766281589  216 SEE 218
Cdd:pfam00043  91 ARP 93
GST_C_family cd00299
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
 118-214 3.43e-04

C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione S-transferase (GST) family, C-terminal alpha helical domain; a large, diverse group of cytosolic dimeric proteins involved in cellular detoxification by catalyzing the conjugation of glutathione (GSH) with a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress. In addition, GSTs also show GSH peroxidase activity and are involved in the synthesis of prostaglandins and leukotrienes. This family, also referred to as soluble GSTs, is the largest family of GSH transferases and is only distantly related to the mitochondrial GSTs (GSTK). Soluble GSTs bear no structural similarity to microsomal GSTs (MAPEG family) and display additional activities unique to their group, such as catalyzing thiolysis, reduction and isomerization of certain compounds. The GST fold contains an N-terminal thioredoxin-fold domain and a C-terminal alpha helical domain, with an active site located in a cleft between the two domains. GSH binds to the N-terminal domain while the hydrophobic substrate occupies a pocket in the C-terminal domain. Based on sequence similarity, different classes of GSTs have been identified, which display varying tissue distribution, substrate specificities and additional specific activities. In humans, GSTs display polymorphisms which may influence individual susceptibility to diseases such as cancer, arthritis, allergy and sclerosis. Some GST family members with non-GST functions include glutaredoxin 2, the CLIC subfamily of anion channels, prion protein Ure2p, crystallins, metaxins, stringent starvation protein A, and aminoacyl-tRNA synthetases.


Pssm-ID: 198286 [Multi-domain]  Cd Length: 100  Bit Score: 38.63  E-value: 3.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281589 118 LMIEFILSKVKDSGMPFPISYLARKVADKISQAYSSGEVKNQFDFVEGEISKNnGYLVDGKLSGADILMsFPLQMAFER- 196
Cdd:cd00299    3 ALEDWADATLAPPLVRLLYLEKVPLPKDEAAVEAAREELPALLAALEQLLAGR-PYLAGDQFSLADVAL-APVLARLEAl 80

                         90       100
                 ....*....|....*....|
gi 766281589 197 --KFAAPEDYPAISKWLKTI 214
Cdd:cd00299   81 gpYYDLLDEYPRLKAWYDRL 100
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 155-214 4.80e-04

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: 38.70  E-value: 4.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766281589 155 EVKNQFDFVEGEISKNNgYLVDGKLSGADI----LMSFPLQMAFERKFAAPedYPAISKWLKTI 214
Cdd:cd03181   44 DLKRALGVLEEHLLTRT-YLVGERITLADIfvasALLRGFETVLDPEFRKK--YPNVTRWFNTV 104
 
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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