NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1831517661|ref|NP_001367276|]
View 

Translation elongation factor EFTu/EF1A C-terminal domain-containing protein [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Translation_factor_III super family cl02786
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 1-40 1.66e-19

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


The actual alignment was detected with superfamily member cd03704:

Pssm-ID: 470675 [Multi-domain]  Cd Length: 108  Bit Score: 73.36  E-value: 1.66e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1831517661   1 MRLESPEPFVLEPFKEYPYLGRFTLRDEGKTIAIGKVLKV 40
Cdd:cd03704    69 ARLETARPICLETFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
 
Name Accession Description Interval E-value
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 1-40 1.66e-19

C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 73.36  E-value: 1.66e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1831517661   1 MRLESPEPFVLEPFKEYPYLGRFTLRDEGKTIAIGKVLKV 40
Cdd:cd03704    69 ARLETARPICLETFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 8-42 1.10e-11

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 56.47  E-value: 1.10e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1831517661   8 PFVLEPFKEYPYLGRFTLRDEGKTIAIGKVLKVVE 42
Cdd:PRK12317  388 PLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKP 422
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 8-42 2.88e-11

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


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 54.94  E-value: 2.88e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1831517661   8 PFVLEPFKEYPYLGRFTLRDEGKTIAIGKVLKVVE 42
Cdd:COG5256   387 PLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKP 421
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 1-40 8.15e-07

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 41.10  E-value: 8.15e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1831517661   1 MRLESPEPFVLEPFKeypylgRFTLRDEGKTIAIGKVLKV 40
Cdd:pfam03143  72 VTVELIKPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
 
Name Accession Description Interval E-value
eRF3_C_III cd03704
C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, ...
 1-40 1.66e-19

C-terminal domain of eRF3; This model represents the eEF1alpha-like C-terminal region of eRF3, which is homologous to the domain III of EF-Tu. eRF3 is a GTPase which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. The C-terminal region is responsible for translation termination activity and is essential for viability. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions: N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 294003 [Multi-domain]  Cd Length: 108  Bit Score: 73.36  E-value: 1.66e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1831517661   1 MRLESPEPFVLEPFKEYPYLGRFTLRDEGKTIAIGKVLKV 40
Cdd:cd03704    69 ARLETARPICLETFKDFPQLGRFTLRDEGKTIAIGKVLKL 108
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 8-42 1.10e-11

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 56.47  E-value: 1.10e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1831517661   8 PFVLEPFKEYPYLGRFTLRDEGKTIAIGKVLKVVE 42
Cdd:PRK12317  388 PLVIEKVKEIPQLGRFAIRDMGQTIAAGMVIDVKP 422
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 8-42 2.88e-11

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


Pssm-ID: 444074 [Multi-domain]  Cd Length: 423  Bit Score: 54.94  E-value: 2.88e-11
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1831517661   8 PFVLEPFKEYPYLGRFTLRDEGKTIAIGKVLKVVE 42
Cdd:COG5256   387 PLVIEKFKEFPQLGRFAIRDMGQTVAAGVVLDVKP 421
EF1_alpha_III cd03705
Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for ...
 7-37 1.31e-09

Domain III of Elongation Factor 1; Eukaryotic elongation factor 1 (EF-1) is responsible for the GTP-dependent binding of aminoacyl-tRNAs to ribosomes. EF-1 is composed of four subunits: the alpha chain, which binds GTP and aminoacyl-tRNAs; the gamma chain that probably plays a role in anchoring the complex to other cellular components; and the beta and delta (or beta') chains. This model represents the alpha subunit, which is the counterpart of bacterial EF-Tu for archaea (aEF-1 alpha) and eukaryotes (eEF-1 alpha).


Pssm-ID: 294004 [Multi-domain]  Cd Length: 104  Bit Score: 48.34  E-value: 1.31e-09
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1831517661   7 EPFVLEPFKEYPYLGRFTLRDEGKTIAIGKV 37
Cdd:cd03705    74 KPLCVETFSEYPPLGRFAVRDMRQTVAVGVI 104
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 7-40 1.76e-09

C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1), which is homologous to the domain III of EF-1alpha. This group contains proteins similar to yeast Hbs1, which together with Dom34, promotes the No-go decay (NGD) of mRNA. The NGD targets mRNAs whose elongation stalled for degradation initiated by endonucleolytic cleavage in the vicinity of the stalled ribosome.


Pssm-ID: 294008 [Multi-domain]  Cd Length: 109  Bit Score: 47.92  E-value: 1.76e-09
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1831517661   7 EPFVLEPFKEYPYLGRFTLRDEGKTIAIGKVLKV 40
Cdd:cd04093    76 RPIPLETFKDNKELGRFVLRRGGETIAAGIVTEI 109
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-42 5.86e-08

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 45.89  E-value: 5.86e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1831517661   2 RLESPEPFVLEPFKEYPYLGRFTLRDEGKTIAIGkVLKVVE 42
Cdd:PTZ00141  391 KMVPTKPMCVEVFNEYPPLGRFAVRDMKQTVAVG-VIKSVE 430
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 2-37 7.40e-08

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 43.92  E-value: 7.40e-08
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1831517661   2 RLESPEPFVLEPFKEYPYLGRFTLRDEGKTIAIGKV 37
Cdd:cd01513    67 EVELQKPVVLERGKEFPTLGRFALRDGGRTVGAGLI 102
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 1-40 8.15e-07

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 41.10  E-value: 8.15e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1831517661   1 MRLESPEPFVLEPFKeypylgRFTLRDEGKTIAIGKVLKV 40
Cdd:pfam03143  72 VTVELIKPIALEKGQ------RFAIREGGRTVAAGVVTEI 105
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-42 7.05e-06

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 40.07  E-value: 7.05e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1831517661   1 MRLESPEPFVLEPFKEYPYLGRFTLRDEGKTIAIGkVLKVVE 42
Cdd:PLN00043  390 VKMIPTKPMVVETFSEYPPLGRFAVRDMRQTVAVG-VIKSVE 430
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH