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Conserved domains on  [gi|1185245801|gb|ARK08609|]
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eukaryotic elongation factor 2, partial [Upupa epops]

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;
1-154 4.80e-90

elongation factor G-like protein;


The actual alignment was detected with superfamily member PTZ00416:

Pssm-ID: 481252 [Multi-domain]  Cd Length: 836  Bit Score: 278.86  E-value: 4.80e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185245801   1 KLWGDRYFDPATGKFSKSATSPDGKKLPRTFCQLILDPIFKVFDAIMNFKKEEAAKLIEKLDIKLDSEDKDKEGKPLLKA 80
Cdd:PTZ00416  237 RLWGDNFFDAKTKKWIKDETNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTGEDKELTGKPLLKA 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1185245801  81 VMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAIGIKNCDPKGPLMMYISKMVPTSDKGRFYA 154
Cdd:PTZ00416  317 VMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTSDKGRFYA 390
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 1-154 4.80e-90

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 278.86  E-value: 4.80e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185245801   1 KLWGDRYFDPATGKFSKSATSPDGKKLPRTFCQLILDPIFKVFDAIMNFKKEEAAKLIEKLDIKLDSEDKDKEGKPLLKA 80
Cdd:PTZ00416  237 RLWGDNFFDAKTKKWIKDETNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTGEDKELTGKPLLKA 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1185245801  81 VMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAIGIKNCDPKGPLMMYISKMVPTSDKGRFYA 154
Cdd:PTZ00416  317 VMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTSDKGRFYA 390
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
 63-144 1.30e-11

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 61.07  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185245801  63 IKLDSEDKDKEgkpLLKAVmrrwlPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAIGIKNCDPKGPLMMYISK 142
Cdd:TIGR00490 225 YKYCKEDKQKE---LAKKS-----PLHQVVLDMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKAMLNCDPKGPLALMITK 296


                  ..
gi 1185245801 143 MV 144
Cdd:TIGR00490 297 IV 298
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 136-154 1.70e-06

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: 43.76  E-value: 1.70e-06
                          10
                  ....*....|....*....
gi 1185245801 136 LMMYISKMVPTSDKGRFYA 154
Cdd:cd03700     1 LMVYSSKMVPTSDKGRFYA 19
 
Name Accession Description Interval E-value
PTZ00416 PTZ00416
elongation factor 2; Provisional
 1-154 4.80e-90

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 278.86  E-value: 4.80e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185245801   1 KLWGDRYFDPATGKFSKSATSPDGKKLPRTFCQLILDPIFKVFDAIMNFKKEEAAKLIEKLDIKLDSEDKDKEGKPLLKA 80
Cdd:PTZ00416  237 RLWGDNFFDAKTKKWIKDETNAQGKKLKRAFCQFILDPICQLFDAVMNEDKEKYDKMLKSLNISLTGEDKELTGKPLLKA 316

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1185245801  81 VMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAIGIKNCDPKGPLMMYISKMVPTSDKGRFYA 154
Cdd:PTZ00416  317 VMQKWLPAADTLLEMIVDHLPSPKEAQKYRVENLYEGPMDDEAANAIRNCDPNGPLMMYISKMVPTSDKGRFYA 390
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
 1-154 1.48e-74

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 237.70  E-value: 1.48e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185245801   1 KLWGDRYFDPATGKFSKSATspDGKKLPRTFCQLILDPIFKVFDAIMNFKKEEAAKLIEKLDIKLDSEDKDKEGKPLLKA 80
Cdd:PLN00116  243 RLWGENFFDPATKKWTTKNT--GSPTCKRGFVQFCYEPIKQIINTCMNDQKDKLWPMLEKLGVTLKSDEKELMGKALMKR 320

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1185245801  81 VMRRWLPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAIGIKNCDPKGPLMMYISKMVPTSDKGRFYA 154
Cdd:PLN00116  321 VMQTWLPASDALLEMIIFHLPSPAKAQRYRVENLYEGPLDDKYATAIRNCDPNGPLMLYVSKMIPASDKGRFFA 394
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 87-144 2.08e-13

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 66.43  E-value: 2.08e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1185245801  87 PAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAIGIKNCDPKGPLMMYISKMV 144
Cdd:PRK07560  242 PLHEVVLDMVVKHLPNPIEAQKYRIPKIWKGDLNSEVGKAMLNCDPNGPLVMMVTDII 299
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
 63-144 1.30e-11

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 61.07  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1185245801  63 IKLDSEDKDKEgkpLLKAVmrrwlPAGDALLQMITIHLPSPVTAQKYRCELLYEGPPDDEAAIGIKNCDPKGPLMMYISK 142
Cdd:TIGR00490 225 YKYCKEDKQKE---LAKKS-----PLHQVVLDMVIRHLPSPIEAQKYRIPVIWKGDLNSEVGKAMLNCDPKGPLALMITK 296


                  ..
gi 1185245801 143 MV 144
Cdd:TIGR00490 297 IV 298
EF2_snRNP_like_II cd03700
Domain II of elongation factor 2 and C-terminal domain of the spliceosomal human 116kD U5 ...
 136-154 1.70e-06

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: 43.76  E-value: 1.70e-06
                          10
                  ....*....|....*....
gi 1185245801 136 LMMYISKMVPTSDKGRFYA 154
Cdd:cd03700     1 LMVYSSKMVPTSDKGRFYA 19
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 135-154 1.39e-03

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: 36.04  E-value: 1.39e-03
                          10        20
                  ....*....|....*....|
gi 1185245801 135 PLMMYISKMVPTSDKGRFYA 154
Cdd:cd16268     1 PLVMYVSKMVPTDKGAGFVA 20
 
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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