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Conserved domains on  [gi|4503477|ref|NP_001950|]
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elongation factor 1-beta [Homo sapiens]

Protein Classification

GST_C_eEF1b_like and EF1B domain-containing protein( domain architecture ID 10875120)

protein containing domains GST_C_eEF1b_like, EF-1_beta_acid, and EF1B

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 142-225 4.14e-46

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: 459919  Cd Length: 83  Bit Score: 147.57  E-value: 4.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503477    142 ILLDVKPWDDETDMAKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFeDYVQSMDVAA 221
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEI-DGVQSVDIEA 79


                  ....
gi 4503477    222 FNKI 225
Cdd:pfam00736  80 FNKL 83
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
 3-62 4.54e-30

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: 106.74  E-value: 4.54e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503477    3 FGDLKSPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPAD-LCHALRWYNHIKSY 62
Cdd:cd10308  22 FADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATkFPHLARWYRHIASF 82
EF-1_beta_acid pfam10587
Eukaryotic elongation factor 1 beta central acidic region;
103-130 8.86e-03

Eukaryotic elongation factor 1 beta central acidic region;


:

Pssm-ID: 463158  Cd Length: 28  Bit Score: 32.89  E-value: 8.86e-03
                          10        20
                  ....*....|....*....|....*...
gi 4503477    103 LFGSDDEEESEEAKRLREERLAQYESKK 130
Cdd:pfam10587   1 LFGSDDEEEDEEAERLREERLAAYAAKK 28
 
Name Accession Description Interval E-value
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 142-225 4.14e-46

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: 459919  Cd Length: 83  Bit Score: 147.57  E-value: 4.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503477    142 ILLDVKPWDDETDMAKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFeDYVQSMDVAA 221
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEI-DGVQSVDIEA 79


                  ....
gi 4503477    222 FNKI 225
Cdd:pfam00736  80 FNKL 83
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 137-225 2.16e-45

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: 146.20  E-value: 2.16e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503477  137 VAKSSILLDVKPWDDETDMAKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAfEDYVQS 216
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79


                ....*....
gi 4503477  217 MDVAAFNKI 225
Cdd:cd00292  80 VDVEAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
 139-225 3.27e-35

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: 119.93  E-value: 3.27e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503477     139 KSSILLDVKPWDDETDMAKLEECVRSI-QADGLVWG-SSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFEDyVQS 216
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGaGIELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG-VQS 79


                   ....*....
gi 4503477     217 MDVAAFNKI 225
Cdd:smart00888  80 VEVEAVSRL 88
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
 3-62 4.54e-30

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: 106.74  E-value: 4.54e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503477    3 FGDLKSPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPAD-LCHALRWYNHIKSY 62
Cdd:cd10308  22 FADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATkFPHLARWYRHIASF 82
ef1B PRK00435
elongation factor 1-beta; Validated
 144-219 1.86e-03

elongation factor 1-beta; Validated


Pssm-ID: 179023  Cd Length: 88  Bit Score: 36.38  E-value: 1.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503477   144 LDVKPWDDETDMAKLEECVR-SIQADGLVWGSSKlVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFEDyVQSMDV 219
Cdd:PRK00435   8 LKVMPESPEVDLDELKEKIKeVLPEGYKINGIEE-EPIAFGLKALKLYVIMPDEEGGTEPVEEAFANVEG-VESVEV 82
EF-1_beta_acid pfam10587
Eukaryotic elongation factor 1 beta central acidic region;
103-130 8.86e-03

Eukaryotic elongation factor 1 beta central acidic region;


Pssm-ID: 463158  Cd Length: 28  Bit Score: 32.89  E-value: 8.86e-03
                          10        20
                  ....*....|....*....|....*...
gi 4503477    103 LFGSDDEEESEEAKRLREERLAQYESKK 130
Cdd:pfam10587   1 LFGSDDEEEDEEAERLREERLAAYAAKK 28
 
Name Accession Description Interval E-value
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 142-225 4.14e-46

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: 459919  Cd Length: 83  Bit Score: 147.57  E-value: 4.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503477    142 ILLDVKPWDDETDMAKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFeDYVQSMDVAA 221
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEI-DGVQSVDIEA 79


                  ....
gi 4503477    222 FNKI 225
Cdd:pfam00736  80 FNKL 83
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 137-225 2.16e-45

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: 146.20  E-value: 2.16e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503477  137 VAKSSILLDVKPWDDETDMAKLEECVRSIQADGLVWGSSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAfEDYVQS 216
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79


                ....*....
gi 4503477  217 MDVAAFNKI 225
Cdd:cd00292  80 VDVEAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
 139-225 3.27e-35

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: 119.93  E-value: 3.27e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503477     139 KSSILLDVKPWDDETDMAKLEECVRSI-QADGLVWG-SSKLVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFEDyVQS 216
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGaGIELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG-VQS 79


                   ....*....
gi 4503477     217 MDVAAFNKI 225
Cdd:smart00888  80 VEVEAVSRL 88
GST_C_eEF1b_like cd10308
Glutathione S-transferase C-terminal-like, alpha helical domain of eukaryotic translation ...
 3-62 4.54e-30

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: 106.74  E-value: 4.54e-30
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 4503477    3 FGDLKSPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPAD-LCHALRWYNHIKSY 62
Cdd:cd10308  22 FADLKTDKGLEALNEYLADRSYISGYSPSQADVEVFDKLKKAPDATkFPHLARWYRHIASF 82
GST_C_CysRS_N cd10310
Glutathione S-transferase C-terminal-like, alpha helical domain of Cysteinyl-tRNA synthetase ...
 10-59 1.14e-16

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: 71.85  E-value: 1.14e-16
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 4503477   10 AGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPADLCHALRWYNHI 59
Cdd:cd10310  21 ARAEALNEYLSTRSYLQGFGPSQADVEVFRLLSRPPADRLVHVLRWYRHI 70
GST_C_AaRS_like cd10289
Glutathione S-transferase C-terminal-like, alpha helical domain of various Aminoacyl-tRNA ...
 1-62 3.06e-15

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: 68.11  E-value: 3.06e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 4503477    1 MGFGDLKSPAGLQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPA-------DLCHALRWYNHIKSY 62
Cdd:cd10289  14 SLLKGKELEALLKSLNSYLASRTFLVGYSLTLADVAVFSALYPSGQKlsdkekkKFPHVTRWFNHIQNL 82
GST_C_AIMP3 cd10305
Glutathione S-transferase C-terminal-like, alpha helical domain of Aminoacyl tRNA synthetase ...
 12-72 1.55e-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 [Multi-domain]  Cd Length: 101  Bit Score: 48.06  E-value: 1.55e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4503477   12 LQVLNDYLADKSYIEGYVPSQADVAVF----EAVSSPPPAD---LCHALRWYNHIKSYEKEKASLPGV 72
Cdd:cd10305  31 LKELNSYLQDRTYLVGHKLTLADVVLYyglhPIMKDLSPQEkeqYLNVSRWFDHVQHLPGIRQHLPLI 98
GST_C_GluRS_N cd10306
Glutathione S-transferase C-terminal-like, alpha helical domain of Glutamyl-tRNA synthetase; ...
 12-61 6.81e-06

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: 43.11  E-value: 6.81e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 4503477   12 LQVLNDYLADKSYIEGYVPSQADVAVFEAVSSPPPA-------DLCHALRWYNHIKS 61
Cdd:cd10306  30 LEELDSHLTLRTFIVGYSLSLADIAVWGALRGNGVAgsliknkVYVNLSRWFSFLES 86
GST_C_Arc1p_N_like cd10304
Glutathione S-transferase C-terminal-like, alpha helical domain of the Aminoacyl tRNA ...
 9-61 9.19e-06

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: 43.13  E-value: 9.19e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4503477    9 PAGLQVLNDYLADKSYIEG-YVPSQADVAVFEAVS------SPPPADLC----HALRWYNHIKS 61
Cdd:cd10304  24 QETLGQLNLHLRTRTFLLGtGKPSVADVAVFEAVLpvvkewSDEVKTGYakyrHILRWVDYVQN 87
GST_C_EF1Bgamma_like cd03181
Glutathione S-transferase C-terminal-like, alpha helical domain of the Gamma subunit of ...
 12-85 1.61e-03

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: 37.16  E-value: 1.61e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4503477   12 LQVLNDYLADKSYIEGYVPSQADVAV-------FEAVSSPP-PADLCHALRWYNHIksyekekASLPGVKKALGKYGPAD 83
Cdd:cd03181  49 LGVLEEHLLTRTYLVGERITLADIFVasallrgFETVLDPEfRKKYPNVTRWFNTV-------VNQPKFKAVFGEVKLCE 121


                ..
gi 4503477   84 VE 85
Cdd:cd03181 122 KP 123
GST_C_GTT2_like cd03182
C-terminal, alpha helical domain of GTT2-like Glutathione S-transferases; Glutathione ...
 10-61 1.75e-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: 36.92  E-value: 1.75e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4503477   10 AGLQVLNDYLADKSYIEGYVPSQADVAVFEAV------SSPPPADLCHALRWYNHIKS 61
Cdd:cd03182  55 DFLPVLDKRLAESPYVAGDRFSIADITAFVALdfaknlKLPVPEELTALRRWYERMAA 112
ef1B PRK00435
elongation factor 1-beta; Validated
 144-219 1.86e-03

elongation factor 1-beta; Validated


Pssm-ID: 179023  Cd Length: 88  Bit Score: 36.38  E-value: 1.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4503477   144 LDVKPWDDETDMAKLEECVR-SIQADGLVWGSSKlVPVGYGIKKLQIQCVVEDDKVGTDMLEEQITAFEDyVQSMDV 219
Cdd:PRK00435   8 LKVMPESPEVDLDELKEKIKeVLPEGYKINGIEE-EPIAFGLKALKLYVIMPDEEGGTEPVEEAFANVEG-VESVEV 82
EF-1_beta_acid pfam10587
Eukaryotic elongation factor 1 beta central acidic region;
103-130 8.86e-03

Eukaryotic elongation factor 1 beta central acidic region;


Pssm-ID: 463158  Cd Length: 28  Bit Score: 32.89  E-value: 8.86e-03
                          10        20
                  ....*....|....*....|....*...
gi 4503477    103 LFGSDDEEESEEAKRLREERLAQYESKK 130
Cdd:pfam10587   1 LFGSDDEEEDEEAERLREERLAAYAAKK 28
 
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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