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Conserved domains on  [gi|30691619|ref|NP_174314|]
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elongation factor 1B beta [Arabidopsis thaliana]

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List of domain hits

Name Accession Description Interval E-value
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
140-231 2.07e-37

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.


:

Pssm-ID: 238181  Cd Length: 88  Bit Score: 127.71  E-value: 2.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619 140 SGKSSVLIDIKPWDDETDMKKLEEAVKSIQMEGLFWGASKLVPVGYGIKKLQILCTIVDDLVSIDtMIEEQLTVEpinEY 219
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTD-ELEEAISEE---DG 76
                        90
                ....*....|..
gi 30691619 220 VQSCDIVAFNKI 231
Cdd:cd00292  77 VQSVDVEAFNKL 88
GST_C_family super family cl02776
C-terminal, alpha helical domain of the Glutathione S-transferase family; Glutathione ...
1-63 1.47e-21

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


The actual alignment was detected with superfamily member cd10308:

Pssm-ID: 261442  Cd Length: 82  Bit Score: 85.55  E-value: 1.47e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30691619   1 MAAFPNLNSDAGLKKLDEHLLTRSYITGYQASKDDITVFAALAKPPTS-QYVNASRWYNHIDAL 63
Cdd:cd10308  19 DGSFADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDAtKFPHLARWYRHIASF 82
 
Name Accession Description Interval E-value
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
140-231 2.07e-37

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.


Pssm-ID: 238181  Cd Length: 88  Bit Score: 127.71  E-value: 2.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619 140 SGKSSVLIDIKPWDDETDMKKLEEAVKSIQMEGLFWGASKLVPVGYGIKKLQILCTIVDDLVSIDtMIEEQLTVEpinEY 219
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTD-ELEEAISEE---DG 76
                        90
                ....*....|..
gi 30691619 220 VQSCDIVAFNKI 231
Cdd:cd00292  77 VQSVDVEAFNKL 88
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
142-231 5.81e-33

EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.


Pssm-ID: 250097  Cd Length: 88  Bit Score: 116.08  E-value: 5.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619   142 KSSVLIDIKPWDDETDMKKLEEAVK-SIQMEGLFWG-ASKLVPVGYGIKKLQILCTIVDDLVSIDtMIEEQLTVEpinEY 219
Cdd:pfam00736   1 KSSVVLKVKPWDDETDLEELEKKVKrKIPMDGLVWGkASKLEPIAFGLKKLQISCVVEDDKVGTD-ELEEAIAFE---DG 76
                          90
                  ....*....|..
gi 30691619   220 VQSCDIVAFNKI 231
Cdd:pfam00736  77 VQSVDIVAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
142-231 9.05e-29

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).


Pssm-ID: 214886  Cd Length: 88  Bit Score: 104.90  E-value: 9.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619    142 KSSVLIDIKPWDDETDMKKLEEAVKSI-QMEGLFWGAS-KLVPVGYGIKKLQILCTIVDDLVSIDTmIEEQLTVepiNEY 219
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDE-LEEAIEE---VEG 76
                           90
                   ....*....|..
gi 30691619    220 VQSCDIVAFNKI 231
Cdd:smart00888  77 VQSVEVEAVSRL 88
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
1-63 1.47e-21

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: 85.55  E-value: 1.47e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30691619   1 MAAFPNLNSDAGLKKLDEHLLTRSYITGYQASKDDITVFAALAKPPTS-QYVNASRWYNHIDAL 63
Cdd:cd10308  19 DGSFADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDAtKFPHLARWYRHIASF 82
EFB1 COG2092
Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]
141-231 1.90e-17

Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]


Pssm-ID: 225003  Cd Length: 88  Bit Score: 74.26  E-value: 1.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619 141 GKSSVLIDIKPWDDETDMKKLEEAVKSIQMEGLFWGASKLVPVGYGIKKLQILCtIVDDLVSIDTMIEEQLtvEPInEYV 220
Cdd:COG2092   2 ADVLVVLKVMPDDPEVDLEELEEKIKEKLPEGYELIKIEEEPIAFGLKALKLYV-VVEDKEGGTDALEEAL--EEV-EGV 77
                        90
                ....*....|.
gi 30691619 221 QSCDIVAFNKI 231
Cdd:COG2092  78 ESVEVENVSRL 88
PLN02907 PLN02907
glutamate-tRNA ligase
16-62 3.00e-04

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 40.09  E-value: 3.00e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30691619   16 LDEHLLTRSYITGYQASKDDITVFAALAKPP--------TSQYVNASRWYNHIDA 62
Cdd:PLN02907 102 VDGYLASRTFLVGYSLTIADIAIWSGLAGSGqrweslrkSKKYQNLVRWFNSISA 156
 
Name Accession Description Interval E-value
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
140-231 2.07e-37

Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the exchange of GDP bound to the G-protein, EF1A, for GTP, an important step in the elongation cycle of the protein biosynthesis. EF1A binds to and delivers the aminoacyl tRNA to the ribosome. The guanine nucleotide exchange domain of EF1B, which is the alpha subunit in yeast, is responsible for the catalysis of this exchange reaction.


Pssm-ID: 238181  Cd Length: 88  Bit Score: 127.71  E-value: 2.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619 140 SGKSSVLIDIKPWDDETDMKKLEEAVKSIQMEGLFWGASKLVPVGYGIKKLQILCTIVDDLVSIDtMIEEQLTVEpinEY 219
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTD-ELEEAISEE---DG 76
                        90
                ....*....|..
gi 30691619 220 VQSCDIVAFNKI 231
Cdd:cd00292  77 VQSVDVEAFNKL 88
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
142-231 5.81e-33

EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain of EF-1 beta and EF-1 delta chains.


Pssm-ID: 250097  Cd Length: 88  Bit Score: 116.08  E-value: 5.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619   142 KSSVLIDIKPWDDETDMKKLEEAVK-SIQMEGLFWG-ASKLVPVGYGIKKLQILCTIVDDLVSIDtMIEEQLTVEpinEY 219
Cdd:pfam00736   1 KSSVVLKVKPWDDETDLEELEKKVKrKIPMDGLVWGkASKLEPIAFGLKKLQISCVVEDDKVGTD-ELEEAIAFE---DG 76
                          90
                  ....*....|..
gi 30691619   220 VQSCDIVAFNKI 231
Cdd:pfam00736  77 VQSVDIVAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
142-231 9.05e-29

EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for two main processes during protein synthesis on the ribosome. EF1A (or EF-Tu) is responsible for the selection and binding of the cognate aminoacyl-tRNA to the A-site (acceptor site) of the ribosome. EF2 (or EF-G) is responsible for the translocation of the peptidyl-tRNA from the A-site to the P-site (peptidyl-tRNA site) of the ribosome, thereby freeing the A-site for the next aminoacyl-tRNA to bind. Elongation factors are responsible for achieving accuracy of translation and both EF1A and EF2 are remarkably conserved throughout evolution. Elongation factor EF1B (also known as EF-Ts or EF-1beta/gamma/delta) is a nucleotide exchange factor that is required to regenerate EF1A from its inactive form (EF1A-GDP) to its active form (EF1A-GTP). EF1A is then ready to interact with a new aminoacyl-tRNA to begin the cycle again. EF1B is more complex in eukaryotes than in bacteria, and can consist of three subunits: EF1B-alpha (or EF-1beta), EF1B-gamma (or EF-1gamma) and EF1B-beta (or EF-1delta). This entry represents the guanine nucleotide exchange domain of the beta (EF-1beta, also known as EF1B-alpha) and delta (EF-1delta, also known as EF1B-beta) chains of EF1B proteins from eukaryotes and archaea. The beta and delta chains have exchange activity, which mainly resides in their homologous guanine nucleotide exchange domains, found in the C-terminal region of the peptides. Their N-terminal regions may be involved in interactions with the gamma chain (EF-1gamma).


Pssm-ID: 214886  Cd Length: 88  Bit Score: 104.90  E-value: 9.05e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619    142 KSSVLIDIKPWDDETDMKKLEEAVKSI-QMEGLFWGAS-KLVPVGYGIKKLQILCTIVDDLVSIDTmIEEQLTVepiNEY 219
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDE-LEEAIEE---VEG 76
                           90
                   ....*....|..
gi 30691619    220 VQSCDIVAFNKI 231
Cdd:smart00888  77 VQSVEVEAVSRL 88
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
1-63 1.47e-21

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: 85.55  E-value: 1.47e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 30691619   1 MAAFPNLNSDAGLKKLDEHLLTRSYITGYQASKDDITVFAALAKPPTS-QYVNASRWYNHIDAL 63
Cdd:cd10308  19 DGSFADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDAtKFPHLARWYRHIASF 82
EFB1 COG2092
Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]
141-231 1.90e-17

Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]


Pssm-ID: 225003  Cd Length: 88  Bit Score: 74.26  E-value: 1.90e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619 141 GKSSVLIDIKPWDDETDMKKLEEAVKSIQMEGLFWGASKLVPVGYGIKKLQILCtIVDDLVSIDTMIEEQLtvEPInEYV 220
Cdd:COG2092   2 ADVLVVLKVMPDDPEVDLEELEEKIKEKLPEGYELIKIEEEPIAFGLKALKLYV-VVEDKEGGTDALEEAL--EEV-EGV 77
                        90
                ....*....|.
gi 30691619 221 QSCDIVAFNKI 231
Cdd:COG2092  78 ESVEVENVSRL 88
GST_C_CysRS_N cd10310
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase ...
16-63 2.47e-14

Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase from higher eukaryotes; Glutathione S-transferase (GST) C-terminal domain family, Cysteinyl-tRNA synthetase (CysRS) subfamily; This model characterizes the GST_C-like domain found in the N-terminal region of CysRS 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 CysRS 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. CysRSs from prokaryotes and lower eukaryotes do not appear to contain this GST_C-like domain.


Pssm-ID: 198343  Cd Length: 73  Bit Score: 65.30  E-value: 2.47e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 30691619  16 LDEHLLTRSYITGYQASKDDITVFAALAKPPTSQYVNASRWYNHIDAL 63
Cdd:cd10310  26 LNEYLSTRSYLQGFGPSQADVEVFRLLSRPPADRLVHVLRWYRHIEAL 73
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
4-63 2.02e-10

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  Cd Length: 82  Bit Score: 54.63  E-value: 2.02e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30691619   4 FPNLNSDAGLKKLDEHLLTRSYITGYQASKDDITVFAALA----KPPTSQ---YVNASRWYNHIDAL 63
Cdd:cd10289  16 LKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYpsgqKLSDKEkkkFPHVTRWFNHIQNL 82
GST_C_GluRS_N cd10306
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ...
2-63 4.60e-10

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  Cd Length: 87  Bit Score: 53.89  E-value: 4.60e-10
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 30691619   2 AAFPNLnsDAGLKKLDEHLLTRSYITGYQASKDDITVFAAL--AKPPTS-----QYVNASRWYNHIDAL 63
Cdd:cd10306  21 KDFKAL--SQALEELDSHLTLRTFIVGYSLSLADIAVWGALrgNGVAGSliknkVYVNLSRWFSFLESL 87
GST_C_AIMP3 cd10305
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
13-66 1.69e-07

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  Cd Length: 101  Bit Score: 46.90  E-value: 1.69e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 30691619  13 LKKLDEHLLTRSYITGYQASKDDITVFAALAKPPTS-------QYVNASRWYNHIDALLRI 66
Cdd:cd10305  31 LKELNSYLQDRTYLVGHKLTLADVVLYYGLHPIMKDlspqekeQYLNVSRWFDHVQHLPGI 91
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
10-60 1.06e-06

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  Cd Length: 123  Bit Score: 45.24  E-value: 1.06e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30691619  10 DAGLKKLDEHLLTRSYITGYQASKDDITVFAALA--------KPPTSQYVNASRWYNHI 60
Cdd:cd03181  46 KRALGVLEEHLLTRTYLVGERITLADIFVASALLrgfetvldPEFRKKYPNVTRWFNTV 104
GST_C_GluProRS_N cd10309
Glutathione S-transferase C-terminal-like, alpha helical domain of bifunctional ...
12-63 1.95e-06

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  Cd Length: 81  Bit Score: 43.85  E-value: 1.95e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 30691619  12 GLKKLDEHLLTRSYITGYQASKDDITVFAAL---AKPPTSQ--YVNASRWYNHIDAL 63
Cdd:cd10309  25 ALSYLDKALSLRTYLVGNSLTLADFAVWAALrgnGEWLASKekYVNVTRWFKFISSQ 81
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
11-62 1.95e-03

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: 35.76  E-value: 1.95e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 30691619  11 AGLKKLDEHLLTRSYITGYQASKDDITVFAAL--AK----PPTSQYVNASRWYNHIDA 62
Cdd:cd03182  55 DFLPVLDKRLAESPYVAGDRFSIADITAFVALdfAKnlklPVPEELTALRRWYERMAA 112
GST_C_ValRS_N cd10294
Glutathione S-transferase C-terminal-like, alpha helical domain of vertebrate Valyl-tRNA ...
13-58 6.81e-03

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  Cd Length: 123  Bit Score: 34.43  E-value: 6.81e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 30691619  13 LKKLDEHLLTRSYITGYQASKDDITVFAALAKP------PT--SQYVNASRWYN 58
Cdd:cd10294  49 LKVLDCYLKLRTYLVGEAITLADIAVACALLLPfkyvldPArrESLLNVTRWFL 102
GST_C_Arc1p_N_like cd10304
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ...
13-55 7.07e-03

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  Cd Length: 100  Bit Score: 33.88  E-value: 7.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 30691619  13 LKKLDEHLLTRSYITG-YQASKDDITVFAALAkPPTSQYVNASR 55
Cdd:cd10304  27 LGQLNLHLRTRTFLLGtGKPSVADVAVFEAVL-PVVKEWSDEVK 69
GST_C_7 cd03206
C-terminal, alpha helical domain of an unknown subfamily 7 of Glutathione S-transferases; ...
9-63 7.25e-03

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  Cd Length: 100  Bit Score: 33.74  E-value: 7.25e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 30691619   9 SDAGLKKLDEHLLTRSYITGYQASKDDITVFAALAKPPT-----SQYVNASRWYNHIDAL 63
Cdd:cd03206  38 SHRLLRLLDQHLAGRDWLAGDRPTIADVACYPYIALAPEggvslEPYPAIRAWLARVEAL 97
PLN02907 PLN02907
glutamate-tRNA ligase
16-62 3.00e-04

glutamate-tRNA ligase


Pssm-ID: 215492 [Multi-domain]  Cd Length: 722  Bit Score: 40.09  E-value: 3.00e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 30691619   16 LDEHLLTRSYITGYQASKDDITVFAALAKPP--------TSQYVNASRWYNHIDA 62
Cdd:PLN02907 102 VDGYLASRTFLVGYSLTIADIAIWSGLAGSGqrweslrkSKKYQNLVRWFNSISA 156
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.11
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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