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Conserved domains on  [gi|499179767|ref|WP_010877307|]
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MULTISPECIES: elongation factor 1-beta [Methanothermobacter]

Protein Classification

elongation factor 1-beta( domain architecture ID 10011438)

elongation factor 1-beta promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus allowing the regeneration of EF-1-alpha/GTP that could then be used to form the ternary complex EF-1-alpha/GTP/AAtRNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ef1B PRK00435
elongation factor 1-beta; Validated
 1-88 5.61e-39

elongation factor 1-beta; Validated


:

Pssm-ID: 179023  Cd Length: 88  Bit Score: 124.20  E-value: 5.61e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767  1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:PRK00435  1 MGDVLAVLKVMPESPEVDLDELKEKIKEVLPEGYKINGIEEEPIAFGLKALKLYVIMPDEEGGTEPVEEAFANVEGVESV 80


                ....*...
gi 499179767 81 EVTDVRRL 88
Cdd:PRK00435 81 EVEEVSRI 88
 
Name Accession Description Interval E-value
ef1B PRK00435
elongation factor 1-beta; Validated
 1-88 5.61e-39

elongation factor 1-beta; Validated


Pssm-ID: 179023  Cd Length: 88  Bit Score: 124.20  E-value: 5.61e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767  1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:PRK00435  1 MGDVLAVLKVMPESPEVDLDELKEKIKEVLPEGYKINGIEEEPIAFGLKALKLYVIMPDEEGGTEPVEEAFANVEGVESV 80


                ....*...
gi 499179767 81 EVTDVRRL 88
Cdd:PRK00435 81 EVEEVSRI 88
EFB1 COG2092
Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]; ...
 1-89 1.03e-38

Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1beta is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 441695  Cd Length: 89  Bit Score: 123.75  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767  1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:COG2092   1 MGDVAAVIKVMPESPEVDLEELKEKIKKKLPEGYEIKGIEEEPIAFGLKALKLYVVMPDTEGGTDALEEALSSVEGVESV 80


                ....*....
gi 499179767 81 EVTDVRRLM 89
Cdd:COG2092  81 EVESVSRLS 89
aEF-1_beta TIGR00489
translation elongation factor aEF-1 beta; This model describes the archaeal translation ...
 1-88 2.22e-33

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: 110.36  E-value: 2.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767   1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:TIGR00489  1 MGTVLAKIKVMPTSPDVDLEKLKEKIKEVLEEGVEIRGLFDEPIAFGLYAIYTMIVMEDREGGTEPIEEALAEIEGVESV 80


                 ....*...
gi 499179767  81 EVTDVRRL 88
Cdd:TIGR00489 81 ETVDVSLL 88
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 1-88 6.40e-29

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: 98.82  E-value: 6.40e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767  1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISEEDGVQSV 80


                ....*...
gi 499179767 81 EVTDVRRL 88
Cdd:cd00292  81 DVEAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
 3-88 1.31e-27

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: 95.66  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767    3 DVVATIKVMPESPDVDLEALKKEIQERIPEGTELH--KIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:smart00888  1 KVLVVLKVMPESDEVDLEELEEKVKSILPMDGLLWgaGIELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEGVQSV 80


                  ....*...
gi 499179767   81 EVTDVRRL 88
Cdd:smart00888 81 EVEAVSRL 88
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 6-88 3.64e-25

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: 89.41  E-value: 3.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767   6 ATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNIEVTDV 85
Cdd:pfam00736  1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEIDGVQSVDIEAF 80


                 ...
gi 499179767  86 RRL 88
Cdd:pfam00736 81 NKL 83
 
Name Accession Description Interval E-value
ef1B PRK00435
elongation factor 1-beta; Validated
 1-88 5.61e-39

elongation factor 1-beta; Validated


Pssm-ID: 179023  Cd Length: 88  Bit Score: 124.20  E-value: 5.61e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767  1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:PRK00435  1 MGDVLAVLKVMPESPEVDLDELKEKIKEVLPEGYKINGIEEEPIAFGLKALKLYVIMPDEEGGTEPVEEAFANVEGVESV 80


                ....*...
gi 499179767 81 EVTDVRRL 88
Cdd:PRK00435 81 EVEEVSRI 88
EFB1 COG2092
Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]; ...
 1-89 1.03e-38

Translation elongation factor EF-1beta [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-1beta is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 441695  Cd Length: 89  Bit Score: 123.75  E-value: 1.03e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767  1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:COG2092   1 MGDVAAVIKVMPESPEVDLEELKEKIKKKLPEGYEIKGIEEEPIAFGLKALKLYVVMPDTEGGTDALEEALSSVEGVESV 80


                ....*....
gi 499179767 81 EVTDVRRLM 89
Cdd:COG2092  81 EVESVSRLS 89
aEF-1_beta TIGR00489
translation elongation factor aEF-1 beta; This model describes the archaeal translation ...
 1-88 2.22e-33

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: 110.36  E-value: 2.22e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767   1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:TIGR00489  1 MGTVLAKIKVMPTSPDVDLEKLKEKIKEVLEEGVEIRGLFDEPIAFGLYAIYTMIVMEDREGGTEPIEEALAEIEGVESV 80


                 ....*...
gi 499179767  81 EVTDVRRL 88
Cdd:TIGR00489 81 ETVDVSLL 88
EF1B cd00292
Elongation factor 1 beta (EF1B) guanine nucleotide exchange domain. EF1B catalyzes the ...
 1-88 6.40e-29

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: 98.82  E-value: 6.40e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767  1 MGDVVATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:cd00292   1 MAKSLVVLKVKPWDDEVDLDELEEKIRAILMDGLLWGKSKLEPIAFGLKALQIYCVVEDDEGGTDELEEAISEEDGVQSV 80


                ....*...
gi 499179767 81 EVTDVRRL 88
Cdd:cd00292  81 DVEAFNKL 88
EF1_GNE smart00888
EF-1 guanine nucleotide exchange domain; Translation elongation factors are responsible for ...
 3-88 1.31e-27

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: 95.66  E-value: 1.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767    3 DVVATIKVMPESPDVDLEALKKEIQERIPEGTELH--KIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNI 80
Cdd:smart00888  1 KVLVVLKVMPESDEVDLEELEEKVKSILPMDGLLWgaGIELEPIAFGLKALQIYVVVEDDEGGTDELEEAIEEVEGVQSV 80


                  ....*...
gi 499179767   81 EVTDVRRL 88
Cdd:smart00888 81 EVEAVSRL 88
EF1_GNE pfam00736
EF-1 guanine nucleotide exchange domain; This family is the guanine nucleotide exchange domain ...
 6-88 3.64e-25

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: 89.41  E-value: 3.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499179767   6 ATIKVMPESPDVDLEALKKEIQERIPEGTELHKIDEEPIAFGLVALNVMVVVGDAEGGTEAAEESLSGIEGVSNIEVTDV 85
Cdd:pfam00736  1 VVLKVKPWDDETDLEELEEKIRSIKLDGLVWGASKLEPIAFGLKALQIYCVVEDDEGGTDELEEAIEEIDGVQSVDIEAF 80


                 ...
gi 499179767  86 RRL 88
Cdd:pfam00736 81 NKL 83
 
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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