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Conserved domains on  [gi|330686713|gb|AEC32333|]
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eukaryotic translation elongation factor 2, partial [Zanda latirostris]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13351 super family cl46912
elongation factor G-like protein;
1-41 2.31e-27

elongation factor G-like protein;


The actual alignment was detected with superfamily member PTZ00416:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 836  Bit Score: 100.89  E-value: 2.31e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 330686713   1 LYEGPPDDEAAIGIKNCDPKGPLMMYISKMVPTSDKGRFYA 41
Cdd:PTZ00416 350 LYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTSDKGRFYA 390
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 1-41 2.31e-27

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 100.89  E-value: 2.31e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 330686713   1 LYEGPPDDEAAIGIKNCDPKGPLMMYISKMVPTSDKGRFYA 41
Cdd:PTZ00416 350 LYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTSDKGRFYA 390
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 23-41 1.09e-07

Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein; This subfamily represents domain II of elongation factor (EF) EF-2 found in eukaryotes and archaea, and the C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of U5-116 kD/Snu114p.


Pssm-ID: 293901 [Multi-domain]  Cd Length: 95  Bit Score: 43.37  E-value: 1.09e-07
                        10
                ....*....|....*....
gi 330686713 23 LMMYISKMVPTSDKGRFYA 41
Cdd:cd03700   1 LMVYSSKMVPTSDKGRFYA 19
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 1-41 2.31e-27

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 100.89  E-value: 2.31e-27
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 330686713   1 LYEGPPDDEAAIGIKNCDPKGPLMMYISKMVPTSDKGRFYA 41
Cdd:PTZ00416 350 LYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTSDKGRFYA 390
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 1-41 7.93e-24

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 90.94  E-value: 7.93e-24
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 330686713   1 LYEGPPDDEAAIGIKNCDPKGPLMMYISKMVPTSDKGRFYA 41
Cdd:PLN00116 354 LYEGPLDDKYATAIRNCDPNGPLMLYVSKMIPASDKGRFFA 394
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 23-41 1.09e-07

Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein; This subfamily represents domain II of elongation factor (EF) EF-2 found in eukaryotes and archaea, and the C-terminal portion of the spliceosomal human 116kD U5 small nuclear ribonucleoprotein (snRNP) protein (U5-116 kD) and its yeast counterpart Snu114p. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site. Yeast Snu114p is essential for cell viability and for splicing in vivo. U5-116 kD binds GTP. Experiments suggest that GTP binding and probably GTP hydrolysis is important for the function of U5-116 kD/Snu114p.


Pssm-ID: 293901 [Multi-domain]  Cd Length: 95  Bit Score: 43.37  E-value: 1.09e-07
                        10
                ....*....|....*....
gi 330686713 23 LMMYISKMVPTSDKGRFYA 41
Cdd:cd03700   1 LMVYSSKMVPTSDKGRFYA 19
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 22-41 2.84e-04

Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site.


Pssm-ID: 293913 [Multi-domain]  Cd Length: 96  Bit Score: 34.50  E-value: 2.84e-04
                        10        20
                ....*....|....*....|
gi 330686713 22 PLMMYISKMVPTSDKGRFYA 41
Cdd:cd16268   1 PLVMYVSKMVPTDKGAGFVA 20
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-31 4.20e-03

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 32.14  E-value: 4.20e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 330686713   1 LYEGPPDDEAAIGIKNCDPKGPLMMYISKMV 31
Cdd:PRK07560 269 IWKGDLNSEVGKAMLNCDPNGPLVMMVTDII 299
 
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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