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Conserved domains on  [gi|2278206478|ref|WP_255364275|]
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EF-Tu/IF-2/RF-3 family GTPase, partial [Alcanivorax sp. HI0044]

Protein Classification

elongation factor Tu( domain architecture ID 1000100)

elongation factor Tu promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis

Gene Ontology:  GO:0005525|GO:0003746|GO:0003924
PubMed:  31708880|17446867|8073502

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK00049 super family cl35051
elongation factor Tu; Reviewed
 1-164 5.96e-135

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 381.84  E-value: 5.96e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:PRK00049  233 RVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVY 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:PRK00049  313 VLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVT 392


                  ....
gi 2278206478 161 KITE 164
Cdd:PRK00049  393 KIIE 396
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-164 5.96e-135

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 381.84  E-value: 5.96e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:PRK00049  233 RVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVY 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:PRK00049  313 VLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVT 392


                  ....
gi 2278206478 161 KITE 164
Cdd:PRK00049  393 KIIE 396
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-164 3.97e-129

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


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 366.78  E-value: 3.97e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:COG0050   233 RVERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVY 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:COG0050   313 VLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVT 392


                  ....
gi 2278206478 161 KITE 164
Cdd:COG0050   393 KIIE 396
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-164 4.88e-107

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 310.94  E-value: 4.88e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:TIGR00485 231 RVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVY 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:TIGR00485 311 VLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVS 390


                  ....
gi 2278206478 161 KITE 164
Cdd:TIGR00485 391 KILE 394
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 70-159 9.53e-64

Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their 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. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


Pssm-ID: 294006 [Multi-domain]  Cd Length: 90  Bit Score: 190.42  E-value: 9.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  70 KPHTKFVAEVYVLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIRE 149
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80

                          90
                  ....*....|
gi 2278206478 150 GGRTVGAGVV 159
Cdd:cd03707    81 GGRTVGAGVV 90
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 68-162 2.62e-50

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: 156.66  E-value: 2.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  68 SIKPHTKFVAEVYVLSKDEGGRHTPFFNGYRPQFYFRTTDVTG------ACTLPEGT----EMVMPGDNVQMDVELIAPI 137
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkfvellHKLDPGGVsenpEFVMPGDNVIVTVELIKPI 80

                          90       100
                  ....*....|....*....|....*
gi 2278206478 138 AMEDGLRFAIREGGRTVGAGVVAKI 162
Cdd:pfam03143  81 ALEKGQRFAIREGGRTVAAGVVTEI 105
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-164 5.96e-135

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 381.84  E-value: 5.96e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:PRK00049  233 RVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVY 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:PRK00049  313 VLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVGAGVVT 392


                  ....
gi 2278206478 161 KITE 164
Cdd:PRK00049  393 KIIE 396
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-164 5.14e-131

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 371.86  E-value: 5.14e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:PRK12735  233 RVERGIVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVY 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:PRK12735  313 VLSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVGAGVVA 392


                  ....
gi 2278206478 161 KITE 164
Cdd:PRK12735  393 KIIE 396
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-164 3.97e-129

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


Pssm-ID: 439820 [Multi-domain]  Cd Length: 396  Bit Score: 366.78  E-value: 3.97e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:COG0050   233 RVERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVY 312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:COG0050   313 VLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVGAGVVT 392


                  ....
gi 2278206478 161 KITE 164
Cdd:COG0050   393 KIIE 396
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-164 5.59e-119

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 341.15  E-value: 5.59e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:PRK12736  231 RVERGTVKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVY 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:PRK12736  311 ILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVGAGTVT 390


                  ....
gi 2278206478 161 KITE 164
Cdd:PRK12736  391 EILD 394
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-164 4.88e-107

translation elongation factor TU; This model models orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts, one of several GTP-binding translation factors found by the more general pfam model GTP_EFTU. The eukaryotic conterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this model. EF-Tu is one of the most abundant proteins in bacteria, as well as one of the most highly conserved, and in a number of species the gene is duplicated with identical function. When bound to GTP, EF-Tu can form a complex with any (correctly) aminoacylated tRNA except those for initiation and for selenocysteine, in which case EF-Tu is replaced by other factors. Transfer RNA is carried to the ribosome in these complexes for protein translation. [Protein synthesis, Translation factors]


Pssm-ID: 129576 [Multi-domain]  Cd Length: 394  Bit Score: 310.94  E-value: 4.88e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:TIGR00485 231 RVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVY 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGVVA 160
Cdd:TIGR00485 311 VLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVGAGVVS 390


                  ....
gi 2278206478 161 KITE 164
Cdd:TIGR00485 391 KILE 394
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-164 7.34e-97

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 286.72  E-value: 7.34e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGIND--TTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAE 78
Cdd:PLN03127  282 RVEQGTIKVGEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAE 361

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  79 VYVLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVGAGV 158
Cdd:PLN03127  362 IYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVGAGV 441


                  ....*.
gi 2278206478 159 VAKITE 164
Cdd:PLN03127  442 VSKVLS 447
tufA CHL00071
elongation factor Tu
 1-164 1.25e-96

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 284.93  E-value: 1.25e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:CHL00071  241 RIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTL-----PEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVG 155
Cdd:CHL00071  321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400


                  ....*....
gi 2278206478 156 AGVVAKITE 164
Cdd:CHL00071  401 AGVVSKILK 409
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-164 5.65e-81

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 247.22  E-value: 5.65e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVY 80
Cdd:PLN03126  310 RVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVY 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  81 VLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTL-----PEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIREGGRTVG 155
Cdd:PLN03126  390 VLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVTSimndkDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469


                  ....*....
gi 2278206478 156 AGVVAKITE 164
Cdd:PLN03126  470 AGVIQSIIE 478
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 70-159 9.53e-64

Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their 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. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


Pssm-ID: 294006 [Multi-domain]  Cd Length: 90  Bit Score: 190.42  E-value: 9.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  70 KPHTKFVAEVYVLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIRE 149
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80

                          90
                  ....*....|
gi 2278206478 150 GGRTVGAGVV 159
Cdd:cd03707    81 GGRTVGAGVV 90
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 68-162 2.62e-50

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: 156.66  E-value: 2.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  68 SIKPHTKFVAEVYVLSKDEGGRHTPFFNGYRPQFYFRTTDVTG------ACTLPEGT----EMVMPGDNVQMDVELIAPI 137
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGkfvellHKLDPGGVsenpEFVMPGDNVIVTVELIKPI 80

                          90       100
                  ....*....|....*....|....*
gi 2278206478 138 AMEDGLRFAIREGGRTVGAGVVAKI 162
Cdd:pfam03143  81 ALEKGQRFAIREGGRTVAAGVVTEI 105
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 70-162 2.45e-35

Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.


Pssm-ID: 294005 [Multi-domain]  Cd Length: 93  Bit Score: 118.49  E-value: 2.45e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  70 KPHTKFVAEVYVLSKDEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVMPGDNVQMDVELIAPIAMEDGLRFAIRE 149
Cdd:cd03706     1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80

                          90
                  ....*....|...
gi 2278206478 150 GGRTVGAGVVAKI 162
Cdd:cd03706    81 GGRTIGTGVVTKL 93
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 1-67 7.16e-35

Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with an essential function in the elongation phase of mRNA translation. The GTPase center of EF-Tu is in the N-terminal domain (domain I), also known as the catalytic or G-domain. The G-domain is composed of about 200 amino acid residues, arranged into a predominantly parallel six-stranded beta-sheet core surrounded by seven alpha helices. Non-catalytic domains II and III are beta-barrels of seven and six, respectively, antiparallel beta-strands that share an extended interface. Both non-catalytic domains are composed of about 100 amino acid residues. EF-Tu proteins exist in two principal conformations: a compact one, EF-Tu*GTP, with tight interfaces between all three domains and a high affinity for aminoacyl-tRNA; and an open one, EF-Tu*GDP, with essentially no G-domain-domain II interactions and a low affinity for aminoacyl-tRNA. EF-Tu has approximately a 100-fold higher affinity for GDP than for GTP.


Pssm-ID: 293898 [Multi-domain]  Cd Length: 87  Bit Score: 116.85  E-value: 7.16e-35
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPG 67
Cdd:cd03697    21 RIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGMVLAKPG 87
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 70-159 1.78e-15

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: 67.80  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  70 KPHTKFVAEVYVLSKDEggrhtPFFNGYRPQFYFRTTDVTGACTLPEGTEM-----------VMPGDNVQMDVELIAPIA 138
Cdd:cd01513     1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVV 75

                          90       100
                  ....*....|....*....|....*..
gi 2278206478 139 MEDG------LRFAIREGGRTVGAGVV 159
Cdd:cd01513    76 LERGkefptlGRFALRDGGRTVGAGLI 102
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 5-159 5.98e-15

Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure and biogenesis]; Selenocysteine-specific translation elongation factor SelB is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 442507 [Multi-domain]  Cd Length: 630  Bit Score: 71.10  E-value: 5.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   5 GIIKVGEELEIVGINDTTKTTctGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGSIKPHTKFVAEVYVLSk 84
Cdd:COG3276   201 GTVRVGDELELLPSGKPVRVR--GIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP- 277

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2278206478  85 degGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEMVmPGDNVQMDVELIAPIAMEDGLRFAIREGG--RTVGAGVV 159
Cdd:COG3276   278 ---SAPRPLKHWQRVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARGDRFILRDYSprRTIGGGRV 350
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-164 6.60e-13

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: 64.95  E-value: 6.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEEleIVGINDTTKTTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGsiKPHT---KFVA 77
Cdd:COG5256   245 RVETGVLKVGDK--VVFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD--NPPTvaeEFTA 320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  78 EVYVLskdeggRH-TPFFNGYRPQFYFRTTDVtgACTLPEGTEMVMP---------------GDNVQMDVELIAPIAMED 141
Cdd:COG5256   321 QIVVL------QHpSAITVGYTPVFHVHTAQV--ACTFVELVSKLDPrtgqvkeenpqflktGDAAIVKIKPTKPLVIEK 392

                         170       180       190
                  ....*....|....*....|....*....|
gi 2278206478 142 -------GlRFAIREGGRTVGAGVVAKITE 164
Cdd:COG5256   393 fkefpqlG-RFAIRDMGQTVAAGVVLDVKP 421
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 1-64 1.80e-12

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 59.20  E-value: 1.80e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTK---TTCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLA 64
Cdd:pfam03144   7 RVESGTLKKGDKVRILPNGTGKKkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-164 5.97e-12

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 62.25  E-value: 5.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEEL--EIVGINDTTKTtctgVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVLAKPGsiKPHT---KF 75
Cdd:PRK12317  246 RVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPD--NPPTvaeEF 319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  76 VAEVYVLskdeggRH-TPFFNGYRPQFYFRTTDVtgACTLPEGTEMVMP---------------GDNVQMDVELIAPIAM 139
Cdd:PRK12317  320 TAQIVVL------QHpSAITVGYTPVFHAHTAQV--ACTFEELVKKLDPrtgqvaeenpqfiktGDAAIVKIKPTKPLVI 391

                         170       180       190
                  ....*....|....*....|....*....|..
gi 2278206478 140 ED-------GlRFAIREGGRTVGAGVVAKITE 164
Cdd:PRK12317  392 EKvkeipqlG-RFAIRDMGQTIAAGMVIDVKP 422
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-163 7.48e-08

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 50.52  E-value: 7.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKttCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVL--AKPGSIKPHTKFVAE 78
Cdd:PTZ00141  254 RVETGILKPGMVVTFAPSGVTTE--VKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVAsdSKNDPAKECADFTAQ 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  79 VYVLSKDEGGRhtpffNGYRPQFYFRTTDVtgAC---------------TLPEGTEMVMPGDNVQMDVELIAPIAMED-- 141
Cdd:PTZ00141  332 VIVLNHPGQIK-----NGYTPVLDCHTAHI--ACkfaeieskidrrsgkVLEENPKAIKSGDAAIVKMVPTKPMCVEVfn 404

                         170       180
                  ....*....|....*....|....*..
gi 2278206478 142 -----GlRFAIREGGRTVGAGVVAKIT 163
Cdd:PTZ00141  405 eypplG-RFAVRDMKQTVAVGVIKSVE 430
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 1-62 2.52e-07

Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor 1-alpha (EF-1A) that is found in archaea and all eukaryotic lineages. EF-1A is very abundant in the cytosol, where it is involved in the GTP-dependent binding of aminoacyl-tRNAs to the A site of the ribosomes in the second step of translation from mRNAs to proteins. Both domain II of EF-1A and domain IV of IF2/eIF5B have been implicated in recognition of the 3'-ends of tRNA. More than 61% of eukaryotic elongation factor 1A (eEF-1A) in cells is estimated to be associated with actin cytoskeleton. The binding of eEF-1A to actin is a noncanonical function that may link two distinct cellular processes, cytoskeleton organization and gene expression.


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 46.03  E-value: 2.52e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKttCTGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQV 62
Cdd:cd03693    25 RVETGILKPGMVVTFAPAGVTGE--VKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRGDV 84
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 1-64 5.72e-07

Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of three structural domains. Domain II adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is found in other proteins such as elongation factor G and translation initiation factor IF-2. This group also includes the C2 subdomain of domain IV of IF-2 that has the same fold as domain II of (EF-Tu). Like IF-2 from certain prokaryotes such as Thermus thermophilus, mitochondrial IF-2 lacks domain II, which is thought to be involved in binding of E. coli IF-2 to 30S subunits.


Pssm-ID: 293888 [Multi-domain]  Cd Length: 80  Bit Score: 44.95  E-value: 5.72e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTctGVEMFRKLLDEGRAGENVGVLLRGTKrdEVERGQVLA 64
Cdd:cd01342    21 RVESGTLKVGDEIRILPKGITGRVT--SIERFHEEVDEAKAGDIVGIGILGVK--DILTGDTLT 80
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-162 7.23e-03

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 35.84  E-value: 7.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   1 RVERGIIKVGEELEIVGINDTTKTTctGVEMFRKLLDEGRAGENVGVLLRGTKRDEVERGQVL--AKPGSIKPHTKFVAE 78
Cdd:PLN00043  254 RVETGVIKPGMVVTFGPTGLTTEVK--SVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnSKDDPAKEAANFTSQ 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  79 VYVLSK--DEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEM------VMPGDNVQMDVELIAPIAMEDGL------R 144
Cdd:PLN00043  332 VIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAGFVKMIPTKPMVVETFSeypplgR 411

                         170
                  ....*....|....*...
gi 2278206478 145 FAIREGGRTVGAGVVAKI 162
Cdd:PLN00043  412 FAVRDMRQTVAVGVIKSV 429
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 4-159 7.79e-03

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 35.60  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478   4 RGIIKVGEELEIV-GINDTTK---------TTCTGVEMFRKLLDEGRAGENVGVllrGTKRD------EVERGQVLAKPG 67
Cdd:PRK04000  242 QGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPGGLVGV---GTKLDpsltkaDALAGSVAGKPG 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2278206478  68 SIKP-HTKFVAEVYVLSK----DEGGRHTPFFNGYRPQFYFRTTDVTGACTLPEGTEmvmpgdnvqMDVELIAPIAMEDG 142
Cdd:PRK04000  319 TLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVVTSARKDE---------AEVKLKRPVCAEEG 389

                         170       180
                  ....*....|....*....|.
gi 2278206478 143 LRFAI--REGGR--TVGAGVV 159
Cdd:PRK04000  390 DRVAIsrRVGGRwrLIGYGII 410
HBS1_C_III cd04093
C-terminal domain of Hsp70 subfamily B suppressor 1 (HBS1); This model represents the ...
 131-162 9.28e-03

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: 34.06  E-value: 9.28e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2278206478 131 VELIAPIAMED-------GlRFAIREGGRTVGAGVVAKI 162
Cdd:cd04093    72 IELERPIPLETfkdnkelG-RFVLRRGGETIAAGIVTEI 109
 
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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