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Conserved domains on  [gi|1907113833|ref|XP_036015436|]
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elongation factor 1-delta isoform X5 [Mus musculus]

Protein Classification

elongation factor 1-beta family protein( domain architecture ID 10465137)

elongation factor 1-beta family protein stimulates the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome, may be either EF-1 beta or EF-1 delta

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 ...
 217-300 2.05e-45

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: 148.34  E-value: 2.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113833 217 ILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFeEHVQSVDIAA 296
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEI-DGVQSVDIEA 79


                  ....
gi 1907113833 297 FNKI 300
Cdd:pfam00736  80 FNKL 83
 
Name Accession Description Interval E-value
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 217-300 2.05e-45

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: 148.34  E-value: 2.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113833 217 ILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFeEHVQSVDIAA 296
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEI-DGVQSVDIEA 79


                  ....
gi 1907113833 297 FNKI 300
Cdd:pfam00736  80 FNKL 83
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 212-300 1.05e-42

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: 141.58  E-value: 1.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113833 212 VAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKfEEHVQS 291
Cdd:cd00292     1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79


                  ....*....
gi 1907113833 292 VDIAAFNKI 300
Cdd:cd00292    80 VDVEAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
 214-300 4.31e-32

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: 114.15  E-value: 4.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113833  214 KSSILLDVKPWDDETDMAQLETCVRSI-QLDGLVWGAS-KLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEhVQS 291
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG-VQS 79


                   ....*....
gi 1907113833  292 VDIAAFNKI 300
Cdd:smart00888  80 VEVEAVSRL 88
 
Name Accession Description Interval E-value
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 217-300 2.05e-45

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: 148.34  E-value: 2.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113833 217 ILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFeEHVQSVDIAA 296
Cdd:pfam00736   1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEI-DGVQSVDIEA 79


                  ....
gi 1907113833 297 FNKI 300
Cdd:pfam00736  80 FNKL 83
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 212-300 1.05e-42

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: 141.58  E-value: 1.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113833 212 VAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKfEEHVQS 291
Cdd:cd00292     1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79


                  ....*....
gi 1907113833 292 VDIAAFNKI 300
Cdd:cd00292    80 VDVEAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
 214-300 4.31e-32

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: 114.15  E-value: 4.31e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907113833  214 KSSILLDVKPWDDETDMAQLETCVRSI-QLDGLVWGAS-KLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEhVQS 291
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG-VQS 79


                   ....*....
gi 1907113833  292 VDIAAFNKI 300
Cdd:smart00888  80 VEVEAVSRL 88
 
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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