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Conserved domains on  [gi|1123899909|ref|WP_074422566|]
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MULTISPECIES: EF-Tu/IF-2/RF-3 family GTPase, partial [Klebsiella]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK00049 super family cl35051
elongation factor Tu; Reviewed
 1-213 8.89e-173

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 479.68  E-value: 8.89e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEG--DAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 78
Cdd:PRK00049  169 PIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  79 GIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKG 158
Cdd:PRK00049  249 GIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNG 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1123899909 159 YRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:PRK00049  329 YRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGG 383
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-213 8.89e-173

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 479.68  E-value: 8.89e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEG--DAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 78
Cdd:PRK00049  169 PIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  79 GIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKG 158
Cdd:PRK00049  249 GIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNG 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1123899909 159 YRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:PRK00049  329 YRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGG 383
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-213 2.19e-167

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: 466.16  E-value: 2.19e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEGD--AEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 78
Cdd:COG0050   169 PIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIV 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  79 GIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKG 158
Cdd:COG0050   249 GIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNG 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1123899909 159 YRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:COG0050   329 YRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGG 383
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-213 1.98e-147

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: 415.72  E-value: 1.98e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEGDAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI 80
Cdd:TIGR00485 169 PIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGL 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  81 KETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYR 160
Cdd:TIGR00485 249 KDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYR 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1123899909 161 PQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:TIGR00485 329 PQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGG 381
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 132-213 1.74e-58

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: 178.86  E-value: 1.74e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909 132 NPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIRE 211
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80


                  ..
gi 1123899909 212 GG 213
Cdd:cd03707    81 GG 82
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 130-213 3.91e-41

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: 135.47  E-value: 3.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909 130 TINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIE------LPEGV----EMVMPGDNIKMVVTLIHPI 199
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80

                          90
                  ....*....|....
gi 1123899909 200 AMDDGLRFAIREGG 213
Cdd:pfam03143  81 ALEKGQRFAIREGG 94
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-213 8.89e-173

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 479.68  E-value: 8.89e-173
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEG--DAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 78
Cdd:PRK00049  169 PIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  79 GIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKG 158
Cdd:PRK00049  249 GIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNG 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1123899909 159 YRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:PRK00049  329 YRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGG 383
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-213 2.19e-167

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: 466.16  E-value: 2.19e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEGD--AEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 78
Cdd:COG0050   169 PIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIV 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  79 GIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKG 158
Cdd:COG0050   249 GIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNG 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1123899909 159 YRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:COG0050   329 YRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGG 383
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-213 7.00e-167

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 464.70  E-value: 7.00e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEGD--AEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 78
Cdd:PRK12735  169 PIIRGSALKALEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIV 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  79 GIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKG 158
Cdd:PRK12735  249 GIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNG 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1123899909 159 YRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:PRK12735  329 YRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGG 383
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-213 1.60e-155

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 435.91  E-value: 1.60e-155
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEGDAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI 80
Cdd:PRK12736  169 PVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGI 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  81 KETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYR 160
Cdd:PRK12736  249 KETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYR 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1123899909 161 PQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:PRK12736  329 PQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGG 381
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-213 1.98e-147

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: 415.72  E-value: 1.98e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEGDAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI 80
Cdd:TIGR00485 169 PIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGL 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  81 KETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFFKGYR 160
Cdd:TIGR00485 249 KDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYR 328

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1123899909 161 PQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:TIGR00485 329 PQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGG 381
tufA CHL00071
elongation factor Tu
 1-213 4.93e-130

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 371.98  E-value: 4.93e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALE----------GDAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK 70
Cdd:CHL00071  169 PIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVK 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  71 VGEEVEIVGIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGG 150
Cdd:CHL00071  249 VGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGG 328

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123899909 151 RHTPFFKGYRPQFYFRTTDVTGTIEL-----PEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:CHL00071  329 RHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGG 396
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-213 4.08e-124

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 358.37  E-value: 4.08e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEG--DAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 78
Cdd:PLN03127  218 PIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIV 297

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  79 GIKE--TAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGGRHTPFF 156
Cdd:PLN03127  298 GLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFF 377

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1123899909 157 KGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:PLN03127  378 SNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGG 434
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-213 2.18e-106

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 314.25  E-value: 2.18e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALE----------GDAEWEAKIIELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK 70
Cdd:PLN03126  238 PIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVK 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  71 VGEEVEIVGIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSKDEGG 150
Cdd:PLN03126  318 VGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGG 397

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123899909 151 RHTPFFKGYRPQFYFRTTDVTGTI-----ELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:PLN03126  398 RHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGG 465
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 132-213 1.74e-58

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: 178.86  E-value: 1.74e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909 132 NPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIRE 211
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80


                  ..
gi 1123899909 212 GG 213
Cdd:cd03707    81 GG 82
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 43-129 4.73e-52

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: 162.30  E-value: 4.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  43 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERG 122
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80


                  ....*..
gi 1123899909 123 QVLAKPG 129
Cdd:cd03697    81 MVLAKPG 87
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 130-213 3.91e-41

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: 135.47  E-value: 3.91e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909 130 TINPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIE------LPEGV----EMVMPGDNIKMVVTLIHPI 199
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80

                          90
                  ....*....|....
gi 1123899909 200 AMDDGLRFAIREGG 213
Cdd:pfam03143  81 ALEKGQRFAIREGG 94
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 133-213 1.76e-30

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: 107.70  E-value: 1.76e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909 133 PHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREG 212
Cdd:cd03706     2 MHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81


                  .
gi 1123899909 213 G 213
Cdd:cd03706    82 G 82
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 32-175 1.15e-23

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: 97.31  E-value: 1.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  32 IPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV--GIKETAKTtctgVEMFRKLLDEGRAGENVGV 109
Cdd:COG5256   214 LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFMpaGVVGEVKS----IEMHHEELEQAEPGDNIGF 289

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909 110 LLRGIKREEIERGQVLAKPGtiNPHT---KFESEVYILskdeggRH-TPFFKGYRPQFYFRTTDVTGTIE 175
Cdd:COG5256   290 NVRGVEKNDIKRGDVAGHPD--NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVACTFV 351
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 23-213 1.25e-22

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: 94.98  E-value: 1.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  23 ELAGHLDTYIPE-PERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDEG 101
Cdd:COG3276   156 ELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGKPVRV--RGIQVHGQPVEEA 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909 102 RAGENVGVLLRGIKREEIERGQVLAKPGTINPHTKFESEVYILSkdegGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVE 181
Cdd:COG3276   234 YAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQRVHLHHGTAEVLARVVLLDREE 309

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1123899909 182 MVmPGDNIKMVVTLIHPIAMDDGLRFAIREGG 213
Cdd:COG3276   310 LA-PGEEALAQLRLEEPLVAARGDRFILRDYS 340
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 28-175 1.63e-22

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 93.84  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  28 LDTyIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEV--EIVGIKETAKTtctgVEMFRKLLDEGRAGE 105
Cdd:PRK12317  212 LDN-LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGD 286

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123899909 106 NVGVLLRGIKREEIERGQVLAKPGtiNPHT---KFESEVYILskdeggRH-TPFFKGYRPQFYFRTTDVTGTIE 175
Cdd:PRK12317  287 NIGFNVRGVGKKDIKRGDVCGHPD--NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVACTFE 352
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 43-127 2.00e-21

Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor SelB that is homologous to domain II of EF-Tu. SelB may function by replacing EF-Tu. In prokaryotes, the incorporation of selenocysteine as the 21st amino acid, encoded by TGA, requires several elements: SelC is the tRNA itself, SelD acts as a donor of reduced selenium, SelA modifies a serine residue on SelC into selenocysteine, and SelB is a selenocysteine-specific translation elongation factor. 3' or 5' non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation.


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 84.12  E-value: 2.00e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  43 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERG 122
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRV--RSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78


                  ....*
gi 1123899909 123 QVLAK 127
Cdd:cd03696    79 FVLSE 83
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 39-124 4.53e-21

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: 83.39  E-value: 4.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  39 IDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIvgiketAKTTCTG----VEMFRKLLDEGRAGENVGVLLRGI 114
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTF------APAGVTGevksVEMHHEPLEEAIPGDNVGFNVKGV 74

                          90
                  ....*....|
gi 1123899909 115 KREEIERGQV 124
Cdd:cd03693    75 SVKDIKRGDV 84
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 24-124 2.43e-18

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 82.49  E-value: 2.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  24 LAGHLDTYIPePERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETakTTCTGVEMFRKLLDEGRA 103
Cdd:PTZ00141  216 LLEALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVT--TEVKSVEMHHEQLAEAVP 292

                          90       100
                  ....*....|....*....|.
gi 1123899909 104 GENVGVLLRGIKREEIERGQV 124
Cdd:PTZ00141  293 GDNVGFNVKNVSVKDIKRGYV 313
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 57-126 3.71e-18

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: 75.38  E-value: 3.71e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1123899909  57 GTVVTGRVERGIIKVGEEVEIVG---IKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLA 126
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 43-126 1.42e-13

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: 63.44  E-value: 1.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  43 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDEGRAGENVGVLLRGIKreEIERG 122
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGRV--TSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76


                  ....
gi 1123899909 123 QVLA 126
Cdd:cd01342    77 DTLT 80
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 8-145 4.05e-13

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 67.42  E-value: 4.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   8 LKALEGDaeweaKIIELAGHLDTY-----------IPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGeevE 76
Cdd:PLN00043  193 ISGFEGD-----NMIERSTNLDWYkgptllealdqINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---M 264

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1123899909  77 IVGIKETAKTT-CTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVL--AKPGTINPHTKFESEVYILS 145
Cdd:PLN00043  265 VVTFGPTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYVAsnSKDDPAKEAANFTSQVIIMN 336
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 42-126 1.26e-10

Domain II of the eukaryotic class II release factor-like proteins; This model represents the domain similar to domain II of the eukaryotic class II release factor (eRF3). In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. 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. This group also contains proteins similar to S. cerevisiae Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 293899 [Multi-domain]  Cd Length: 84  Bit Score: 55.97  E-value: 1.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  42 PFLLPIEDVFSiSGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEMFRKlLDEGRAGENVGVLLRGIKREEIER 121
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78


                  ....*
gi 1123899909 122 GQVLA 126
Cdd:cd03698    79 GDILS 83
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 43-126 1.65e-10

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 55.69  E-value: 1.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  43 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI----VGikETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGIKREE 118
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdaDG--KFRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRES 78


                  ....*...
gi 1123899909 119 IERGQVLA 126
Cdd:cd03694    79 LRKGMVLV 86
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-35 8.47e-10

Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes orthologs of translation elongation factor EF-Tu in bacteria, mitochondria, and chloroplasts. It is one of several GTP-binding translation factors found in the larger family of GTP-binding elongation factors. The eukaryotic counterpart, eukaryotic translation elongation factor 1 (eEF-1 alpha), is excluded from this family. 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.


Pssm-ID: 206671 [Multi-domain]  Cd Length: 195  Bit Score: 56.05  E-value: 8.47e-10
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1123899909   1 PIVRGSALKALEGD--AEWEAKIIELAGHLDTYIPEP 35
Cdd:cd01884   159 PIVRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 42-125 1.30e-09

Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 52.90  E-value: 1.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  42 PFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAktTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIER 121
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETA--TVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78


                  ....
gi 1123899909 122 GQVL 125
Cdd:cd16267    79 GSIL 82
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 42-125 4.09e-09

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. 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: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 51.72  E-value: 4.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  42 PFLLPIEDVFSisGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTT---CTGVEMfrkllDEGRAGENVGVLLRGIKREE 118
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNKTKVEVTgiyIDEEEV-----DSAKPGENVKLKLKGVEEED 73


                  ....*..
gi 1123899909 119 IERGQVL 125
Cdd:cd04089    74 ISPGFVL 80
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 133-213 4.18e-09

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: 52.01  E-value: 4.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909 133 PHTKFESEVYILSKDEggrhtPFFKGYRPQFYFRTTDVTGTIELPEGVE-----------MVMPGDNIKMVVTLIHPIAM 201
Cdd:cd01513     2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVVL 76

                          90
                  ....*....|....*...
gi 1123899909 202 DDG------LRFAIREGG 213
Cdd:cd01513    77 ERGkefptlGRFALRDGG 94
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-146 4.45e-08

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 52.55  E-value: 4.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909   1 PIVRGSALKALEGDAeweakiieLAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGT--------VVTGRVERGIIKVG 72
Cdd:PRK04000  177 PIIPVSALHKVNIDA--------LIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVG 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  73 EEVEIV-GIKETAK---------TTCTGVEMFRKLLDEGRAGENVGV---LLRGIKREEIERGQVLAKPGTINP-HTKFE 138
Cdd:PRK04000  249 DEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPGGLVGVgtkLDPSLTKADALAGSVAGKPGTLPPvWESLT 328


                  ....*...
gi 1123899909 139 SEVYILSK 146
Cdd:PRK04000  329 IEVHLLER 336
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 21-122 8.17e-06

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 45.81  E-value: 8.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  21 IIELAGHLDTyIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETAKTtcTGVEMFRKLLDE 100
Cdd:PRK10512  154 IDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMRV--RGLHAQNQPTEQ 230

                          90       100
                  ....*....|....*....|...
gi 1123899909 101 GRAGENVGVLLRG-IKREEIERG 122
Cdd:PRK10512  231 AQAGQRIALNIAGdAEKEQINRG 253
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 47-126 1.65e-05

Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 41.90  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  47 IEDVFSISGRgTVVTGRVERGIIKVGEEVeivgIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLRGikREEIERGQVLA 126
Cdd:cd16265     5 VEKVFKILGR-QVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 43-127 6.45e-05

Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 40.24  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  43 FLLPIEDV--FSISGRGtvVTGRVERGIIKVGEEVEIvgIKETAKTTCTGVEMFRKLLDEGRAGENVGVLLrgiKRE-EI 119
Cdd:cd03695     1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73


                  ....*...
gi 1123899909 120 ERGQVLAK 127
Cdd:cd03695    74 SRGDLIVR 81
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 57-143 7.12e-03

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 36.76  E-value: 7.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123899909  57 GTVVTGRVERGIIKVGEEVEIVGIKETAKTTCTGVEM--FRKLLDEGRAGENVGVLlrGIKreEIERGQVLAKPGTINPh 134
Cdd:PRK07560  305 GEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMgpEREEVEEIPAGNIAAVT--GLK--DARAGETVVSVEDMTP- 379


                  ....*....
gi 1123899909 135 tkFESEVYI 143
Cdd:PRK07560  380 --FESLKHI 386
 
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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