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Conserved domains on  [gi|56699438|ref|NP_083939|]
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elongation factor 1-delta isoform a [Mus musculus]

Protein Classification

similar to elongation factor 1-delta isoform X1 (domain architecture ID 10465137)

protein similar to elongation factor 1-delta isoform X1

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 ...
577-660 9.45e-47

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: 307058  Cd Length: 83  Bit Score: 161.04  E-value: 9.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438   577 ILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFeEHVQSVDIAA 656
Cdd:pfam00736   1 VVLDVKPWDDETDLEELEEKIRSIKLDGLVWGKSKLEPIAFGLKKLQITCVVEDDKVGTDDLEEAIEEI-EGVQSVDIEA 79

                  ....
gi 56699438   657 FNKI 660
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 ...
577-660 9.45e-47

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: 307058  Cd Length: 83  Bit Score: 161.04  E-value: 9.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438   577 ILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFeEHVQSVDIAA 656
Cdd:pfam00736   1 VVLDVKPWDDETDLEELEEKIRSIKLDGLVWGKSKLEPIAFGLKKLQITCVVEDDKVGTDDLEEAIEEI-EGVQSVDIEA 79

                  ....
gi 56699438   657 FNKI 660
Cdd:pfam00736  80 FNKL 83
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
572-660 9.33e-44

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: 152.75  E-value: 9.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438 572 VAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKfEEHVQS 651
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79

                ....*....
gi 56699438 652 VDIAAFNKI 660
Cdd:cd00292  80 VDVEAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
574-660 5.51e-34

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: 126.09  E-value: 5.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438    574 KSSILLDVKPWDDETDMAQLETCVRSI-QLDGLVWGAS-KLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEhVQS 651
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG-VQS 79

                   ....*....
gi 56699438    652 VDIAAFNKI 660
Cdd:smart00888  80 VEVEAVSRL 88
EFB1 COG2092
Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis];
572-660 5.59e-23

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


Pssm-ID: 225003  Cd Length: 88  Bit Score: 95.45  E-value: 5.59e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438 572 VAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEhVQS 651
Cdd:COG2092   1 MADVLVVLKVMPDDPEVDLEELEEKIKEKLPEGYELIKIEEEPIAFGLKALKLYVVVEDKEGGTDALEEALEEVEG-VES 79

                ....*....
gi 56699438 652 VDIAAFNKI 660
Cdd:COG2092  80 VEVENVSRL 88
aEF-1_beta TIGR00489
translation elongation factor aEF-1 beta; This model describes the archaeal translation ...
570-654 1.32e-03

translation elongation factor aEF-1 beta; This model describes the archaeal translation elongation factor aEF-1 beta. The member from Sulfolobus solfataricus was demonstrated experimentally. It is a dimer that catalyzes the exchange of GDP for GTP on aEF-1 alpha. [Protein synthesis, Translation factors]


Pssm-ID: 129580  Cd Length: 88  Bit Score: 38.71  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438   570 TLVAKssilLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEhV 649
Cdd:TIGR00489   3 DVVAK----IKVMPESPDVDLEALKEKIKERIPEGVEIRKIDEEPIAFGLVAINVMVVMGDAEGGTEAAEESLSGIEG-V 77

                  ....*
gi 56699438   650 QSVDI 654
Cdd:TIGR00489  78 ESVEV 82
 
Name Accession Description Interval E-value
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
577-660 9.45e-47

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: 307058  Cd Length: 83  Bit Score: 161.04  E-value: 9.45e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438   577 ILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFeEHVQSVDIAA 656
Cdd:pfam00736   1 VVLDVKPWDDETDLEELEEKIRSIKLDGLVWGKSKLEPIAFGLKKLQITCVVEDDKVGTDDLEEAIEEI-EGVQSVDIEA 79

                  ....
gi 56699438   657 FNKI 660
Cdd:pfam00736  80 FNKL 83
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
572-660 9.33e-44

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: 152.75  E-value: 9.33e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438 572 VAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKfEEHVQS 651
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISE-EDGVQS 79

                ....*....
gi 56699438 652 VDIAAFNKI 660
Cdd:cd00292  80 VDVEAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
574-660 5.51e-34

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: 126.09  E-value: 5.51e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438    574 KSSILLDVKPWDDETDMAQLETCVRSI-QLDGLVWGAS-KLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEhVQS 651
Cdd:smart00888   1 KVLVVLKVMPESDEVDLEELEEKVKSIlPMDGLLWGAGiELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEG-VQS 79

                   ....*....
gi 56699438    652 VDIAAFNKI 660
Cdd:smart00888  80 VEVEAVSRL 88
EFB1 COG2092
Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis];
572-660 5.59e-23

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


Pssm-ID: 225003  Cd Length: 88  Bit Score: 95.45  E-value: 5.59e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438 572 VAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEhVQS 651
Cdd:COG2092   1 MADVLVVLKVMPDDPEVDLEELEEKIKEKLPEGYELIKIEEEPIAFGLKALKLYVVVEDKEGGTDALEEALEEVEG-VES 79

                ....*....
gi 56699438 652 VDIAAFNKI 660
Cdd:COG2092  80 VEVENVSRL 88
aEF-1_beta TIGR00489
translation elongation factor aEF-1 beta; This model describes the archaeal translation ...
570-654 1.32e-03

translation elongation factor aEF-1 beta; This model describes the archaeal translation elongation factor aEF-1 beta. The member from Sulfolobus solfataricus was demonstrated experimentally. It is a dimer that catalyzes the exchange of GDP for GTP on aEF-1 alpha. [Protein synthesis, Translation factors]


Pssm-ID: 129580  Cd Length: 88  Bit Score: 38.71  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56699438   570 TLVAKssilLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEhV 649
Cdd:TIGR00489   3 DVVAK----IKVMPESPDVDLEALKEKIKERIPEGVEIRKIDEEPIAFGLVAINVMVVMGDAEGGTEAAEESLSGIEG-V 77

                  ....*
gi 56699438   650 QSVDI 654
Cdd:TIGR00489  78 ESVEV 82
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • 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, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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