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Conserved domains on  [gi|655576748|ref|WP_028928105|]
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EF-Tu/IF-2/RF-3 family GTPase, partial [Pseudoxanthomonas suwonensis]

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
 1-183 1.55e-152

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 427.30  E-value: 1.55e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PRK00049 214 LMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQ 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:PRK00049 294 VLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEE 373

                        170       180
                 ....*....|....*....|...
gi 655576748 161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:PRK00049 374 GLRFAIREGGRTVGAGVVTKIIE 396
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-183 1.55e-152

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 427.30  E-value: 1.55e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PRK00049 214 LMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQ 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:PRK00049 294 VLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEE 373

                        170       180
                 ....*....|....*....|...
gi 655576748 161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:PRK00049 374 GLRFAIREGGRTVGAGVVTKIIE 396
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-183 1.56e-147

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: 414.55  E-value: 1.56e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:COG0050  214 LMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQ 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:COG0050  294 VLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEE 373

                        170       180
                 ....*....|....*....|...
gi 655576748 161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:COG0050  374 GLRFAIREGGRTVGAGVVTKIIE 396
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-183 2.83e-123

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: 352.93  E-value: 2.83e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748    1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:TIGR00485 212 LLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGM 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:TIGR00485 292 VLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQ 371

                         170       180
                  ....*....|....*....|...
gi 655576748  161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:TIGR00485 372 GMRFAIREGGRTVGAGVVSKILE 394
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 89-178 1.22e-62

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: 188.10  E-value: 1.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  89 TPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDEGLRFAIRE 168
Cdd:cd03707    1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80

                         90
                 ....*....|
gi 655576748 169 GGRTVGAGVV 178
Cdd:cd03707   81 GGRTVGAGVV 90
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 87-181 4.23e-48

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: 152.03  E-value: 4.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   87 TITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAV------QLPEGV----EMVMPGDNVKMVVSLINPV 156
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkLDPGGVsenpEFVMPGDNVIVTVELIKPI 80

                          90       100
                  ....*....|....*....|....*
gi 655576748  157 AMDEGLRFAIREGGRTVGAGVVAKI 181
Cdd:pfam03143  81 ALEKGQRFAIREGGRTVAAGVVTEI 105
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-183 1.55e-152

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 427.30  E-value: 1.55e-152
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PRK00049 214 LMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQ 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:PRK00049 294 VLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEE 373

                        170       180
                 ....*....|....*....|...
gi 655576748 161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:PRK00049 374 GLRFAIREGGRTVGAGVVTKIIE 396
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-183 1.56e-147

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: 414.55  E-value: 1.56e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:COG0050  214 LMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQ 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:COG0050  294 VLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEE 373

                        170       180
                 ....*....|....*....|...
gi 655576748 161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:COG0050  374 GLRFAIREGGRTVGAGVVTKIIE 396
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-183 8.34e-147

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 412.69  E-value: 8.34e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PRK12735 214 LMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQ 293

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:PRK12735 294 VLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEE 373

                        170       180
                 ....*....|....*....|...
gi 655576748 161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:PRK12735 374 GLRFAIREGGRTVGAGVVAKIIE 396
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-183 1.26e-134

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 381.60  E-value: 1.26e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PRK12736 212 LMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQ 291

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:PRK12736 292 VLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQ 371

                        170       180
                 ....*....|....*....|...
gi 655576748 161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:PRK12736 372 GLKFAIREGGRTVGAGTVTEILD 394
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-183 2.83e-123

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: 352.93  E-value: 2.83e-123
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748    1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:TIGR00485 212 LLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGM 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDE 160
Cdd:TIGR00485 292 VLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQ 371

                         170       180
                  ....*....|....*....|...
gi 655576748  161 GLRFAIREGGRTVGAGVVAKIIK 183
Cdd:TIGR00485 372 GMRFAIREGGRTVGAGVVSKILE 394
tufA CHL00071
elongation factor Tu
 1-183 4.52e-115

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 332.69  E-value: 4.52e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:CHL00071 222 LMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGM 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQL-----PEGVEMVMPGDNVKMVVSLINP 155
Cdd:CHL00071 302 VLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYP 381

                        170       180
                 ....*....|....*....|....*...
gi 655576748 156 VAMDEGLRFAIREGGRTVGAGVVAKIIK 183
Cdd:CHL00071 382 IAIEKGMRFAIREGGRTVGAGVVSKILK 409
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-182 7.77e-113

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 328.32  E-value: 7.77e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRP--TTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VER 78
Cdd:PLN03127 263 LMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQR 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  79 GQVLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAM 158
Cdd:PLN03127 343 GQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPL 422

                        170       180
                 ....*....|....*....|....
gi 655576748 159 DEGLRFAIREGGRTVGAGVVAKII 182
Cdd:PLN03127 423 EPGQRFALREGGRTVGAGVVSKVL 446
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-183 9.17e-95

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 283.43  E-value: 9.17e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PLN03126 291 LLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGM 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAV-----QLPEGVEMVMPGDNVKMVVSLINP 155
Cdd:PLN03126 371 VLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVP 450

                        170       180
                 ....*....|....*....|....*...
gi 655576748 156 VAMDEGLRFAIREGGRTVGAGVVAKIIK 183
Cdd:PLN03126 451 VACEQGMRFAIREGGKTVGAGVIQSIIE 478
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 89-178 1.22e-62

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: 188.10  E-value: 1.22e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  89 TPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDEGLRFAIRE 168
Cdd:cd03707    1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80

                         90
                 ....*....|
gi 655576748 169 GGRTVGAGVV 178
Cdd:cd03707   81 GGRTVGAGVV 90
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 1-86 2.57e-50

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: 156.91  E-value: 2.57e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:cd03697    2 LMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERGM 81


                 ....*.
gi 655576748  81 VLAKPG 86
Cdd:cd03697   82 VLAKPG 87
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 87-181 4.23e-48

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: 152.03  E-value: 4.23e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   87 TITPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAV------QLPEGV----EMVMPGDNVKMVVSLINPV 156
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFvellhkLDPGGVsenpEFVMPGDNVIVTVELIKPI 80

                          90       100
                  ....*....|....*....|....*
gi 655576748  157 AMDEGLRFAIREGGRTVGAGVVAKI 181
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% ...
 89-181 3.02e-36

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: 121.57  E-value: 3.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  89 TPHTDFEAEVYVLSKDEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVMPGDNVKMVVSLINPVAMDEGLRFAIRE 168
Cdd:cd03706    1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80

                         90
                 ....*....|...
gi 655576748 169 GGRTVGAGVVAKI 181
Cdd:cd03706   81 GGRTIGTGVVTKL 93
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-181 1.06e-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: 96.16  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDVFSISGRGTVVTGRIERGVIKVGDEVeiVGIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQV 81
Cdd:COG5256  227 IPIQDVYSISGIGTVPVGRVETGVLKVGDKV--VFMPAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDV 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  82 LAKPGT-ITPHTDFEAEVYVLskdeggRH-TPFFKGYRPQFYFRTTDItgAVQLPEGVEMVMP---------------GD 144
Cdd:COG5256  305 AGHPDNpPTVAEEFTAQIVVL------QHpSAITVGYTPVFHVHTAQV--ACTFVELVSKLDPrtgqvkeenpqflktGD 376

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 655576748 145 NVKMVVSLINPVAMD------EGLRFAIREGGRTVGAGVVAKI 181
Cdd:COG5256  377 AAIVKIKPTKPLVIEkfkefpQLGRFAIRDMGQTVAAGVVLDV 419
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-181 1.27e-20

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 87.67  E-value: 1.27e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDVFSISGRGTVVTGRIERGVIKVGDEVEivgIRPTTKT-TVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PRK12317 228 IPIQDVYSISGVGTVPVGRVETGVLKVGDKVV---FMPAGVVgEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGD 304

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VLAKPGTI-TPHTDFEAEVYVLskdeggRH-TPFFKGYRPQFYFRTTDI--------------TGAVqLPEGVEMVMPGD 144
Cdd:PRK12317 305 VCGHPDNPpTVAEEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVactfeelvkkldprTGQV-AEENPQFIKTGD 377

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 655576748 145 NVKMVVSLINPVAMDE-------GlRFAIREGGRTVGAGVVAKI 181
Cdd:PRK12317 378 AAIVKIKPTKPLVIEKvkeipqlG-RFAIRDMGQTIAAGMVIDV 420
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-178 2.23e-20

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: 87.28  E-value: 2.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRptTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQV 81
Cdd:COG3276  179 LPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG--KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDV 256

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  82 LAKPGTITPHTDFEAEVYVLSkdegGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEMVmPGDNVKMVVSLINPVAMDEG 161
Cdd:COG3276  257 LAAPGALRPTDRIDVRLRLLP----SAPRPLKHWQRVHLHHGTAEVLARVVLLDREELA-PGEEALAQLRLEEPLVAARG 331

                        170
                 ....*....|....*....
gi 655576748 162 LRFAIREGG--RTVGAGVV 178
Cdd:COG3276  332 DRFILRDYSprRTIGGGRV 350
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 1-84 1.43e-17

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: 73.33  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKttVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:cd03696    2 RLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERGF 79


                 ....
gi 655576748  81 VLAK 84
Cdd:cd03696   80 VLSE 83
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 2-81 1.21e-16

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: 71.06  E-value: 1.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVgirPTTKTT-VTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:cd03693    7 LPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA---PAGVTGeVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKDIKRGD 83


                 .
gi 655576748  81 V 81
Cdd:cd03693   84 V 84
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 14-83 2.09e-16

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: 69.99  E-value: 2.09e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 655576748   14 GTVVTGRIERGVIKVGDEVEIVGIRPTTK---TTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQVLA 83
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 90-178 3.58e-14

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: 65.11  E-value: 3.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  90 PHTDFEAEVYVLSKDEggrhtPFFKGYRPQFYFRTTDITGAVQLPEGVEM-----------VMPGDNVKMVVSLINPVAM 158
Cdd:cd01513    2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEDgktkekkppdsLQPGENGTVEVELQKPVVL 76

                         90       100
                 ....*....|....*....|....*.
gi 655576748 159 DEG------LRFAIREGGRTVGAGVV 178
Cdd:cd01513   77 ERGkefptlGRFALRDGGRTVGAGLI 102
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 1-83 1.07e-12

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: 60.36  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIrpTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKrd*VERGQ 80
Cdd:cd01342    2 VMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK--GITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTGD 77


                 ...
gi 655576748  81 VLA 83
Cdd:cd01342   78 TLT 80
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-183 2.12e-12

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 64.38  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDVFSISGRGTVVTGRIERGVIKVGDeveIVGIRPTTKTT-VTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PTZ00141 236 LPLQDVYKIGGIGTVPVGRVETGILKPGM---VVTFAPSGVTTeVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGY 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VL--AKPGTITPHTDFEAEVYVLSkdeggrHTPFFK-GYRPQFYFRTTDI--------------TGAVqLPEGVEMVMPG 143
Cdd:PTZ00141 313 VAsdSKNDPAKECADFTAQVIVLN------HPGQIKnGYTPVLDCHTAHIackfaeieskidrrSGKV-LEENPKAIKSG 385

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 655576748 144 DN--VKMVVSliNPVAMDE-------GlRFAIREGGRTVGAGVVAKIIK 183
Cdd:PTZ00141 386 DAaiVKMVPT--KPMCVEVfneypplG-RFAVRDMKQTVAVGVIKSVEK 431
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 2-136 3.08e-10

selenocysteine-specific elongation factor SelB; 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-prime or 5-prime non-coding elements of mRNA have been found as probable structures for directing selenocysteine incorporation. This model describes the elongation factor SelB, a close homolog rf EF-Tu. It may function by replacing EF-Tu. A C-terminal domain not found in EF-Tu is in all SelB sequences in the seed alignment except that from Methanococcus jannaschii. This model does not find an equivalent protein for eukaryotes. [Protein synthesis, Translation factors]


Pssm-ID: 129567 [Multi-domain]  Cd Length: 581  Bit Score: 57.96  E-value: 3.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748    2 MPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIrpTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQV 81
Cdd:TIGR00475 179 MAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI--NHEVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLL 256

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 655576748   82 LAKPgtitPHTDFEAEVYVLSkdeggrHTPFFKGYRPQFYFRTTDITGAVQLPEG 136
Cdd:TIGR00475 257 ILTP----EDPKLRVVVKFIA------EVPLLELQPYHIAHGMSVTTGKISLLDK 301
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 1-83 6.45e-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: 53.38  E-value: 6.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIvGIRPT---TKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VE 77
Cdd:cd03694    2 EFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLL-GPDADgkfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                 ....*.
gi 655576748  78 RGQVLA 83
Cdd:cd03694   81 KGMVLV 86
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 2-183 1.95e-09

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 55.87  E-value: 1.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDVFSISGRGTVVTGRIERGVIKVGdevEIVGIRPTTKTT-VTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:PLN00043 236 LPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGY 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  81 VL--AKPGTITPHTDFEAEVYVLSK--DEGGRHTPFFKGYRPQFYFRTTDITGAVQLPEGVEM------VMPGDN--VKM 148
Cdd:PLN00043 313 VAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLKNGDAgfVKM 392

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 655576748 149 VVS---LINPVAMDEGL-RFAIREGGRTVGAGVVAKIIK 183
Cdd:PLN00043 393 IPTkpmVVETFSEYPPLgRFAVRDMRQTVAVGVIKSVEK 431
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 2-98 3.06e-08

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 52.01  E-value: 3.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDV--FSISGRGtvVTGRIERGVIKVGDEVEIVgirPT-TKTTVTGVEMFRKLLDQGQAGDNAGLLLrgtKRD*-VE 77
Cdd:COG2895  235 FPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVVVL---PSgKTSTVKSIVTFDGDLEEAFAGQSVTLTL---EDEIdIS 306

                         90       100
                 ....*....|....*....|..
gi 655576748  78 RGQVLAKPG-TITPHTDFEAEV 98
Cdd:COG2895  307 RGDVIVAADaPPEVADQFEATL 328
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 4-83 6.39e-08

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: 48.06  E-value: 6.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   4 VEDVFSISGRgTVVTGRIERGVIKVGDEVeivgIRPTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRd*VERGQVLA 83
Cdd:cd16265    5 VEKVFKILGR-QVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVLE 77
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 2-82 9.73e-07

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: 44.81  E-value: 9.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDVFSISGRGTVVTGRIERGVIKVGDEVEIVGIRPTtkTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQV 81
Cdd:cd16267    4 LSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVGSI 81


                 .
gi 655576748  82 L 82
Cdd:cd16267   82 L 82
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 13-178 8.44e-06

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 44.84  E-value: 8.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  13 RGTVVTGRIERGVIKVGDEVEIV-GIRPTTK---------TTVTGVEMFRKLLDQGQAGdnaGLLLRGTKRD------*V 76
Cdd:PRK04000 232 KGGVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPG---GLVGVGTKLDpsltkaDA 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748  77 ERGQVLAKPGTITP-HTDFEAEVYVLSK----DEGGRHTPFFKGYRPQFYFRTTDITGAVQlpegvemVMPGDNVKmvVS 151
Cdd:PRK04000 309 LAGSVAGKPGTLPPvWESLTIEVHLLERvvgtKEELKVEPIKTGEPLMLNVGTATTVGVVT-------SARKDEAE--VK 379

                        170       180       190
                 ....*....|....*....|....*....|.
gi 655576748 152 LINPVAMDEGLRFAI--REGGR--TVGAGVV 178
Cdd:PRK04000 380 LKRPVCAEEGDRVAIsrRVGGRwrLIGYGII 410
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 2-84 2.49e-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: 41.01  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDV--FSISGRGtvVTGRIERGVIKVGDEVEIVgirPT-TKTTVTGVEMFRKLLDQGQAGDNAGLLLrgtKRD-*VE 77
Cdd:cd03695    3 FPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTVL---PSgKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDVS 74


                 ....*..
gi 655576748  78 RGQVLAK 84
Cdd:cd03695   75 RGDLIVR 81
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 2-82 9.68e-05

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: 39.39  E-value: 9.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   2 MPVEDVFSisGRGTVVTGRIERGVIKVGDEVEIVGIRptTKTTVTGVEMFRKLLDQGQAGDNAGLLLRGTKRD*VERGQV 81
Cdd:cd04089    4 MPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNK--TKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFV 79


                 .
gi 655576748  82 L 82
Cdd:cd04089   80 L 80
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 1-83 1.86e-04

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: 38.64  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   1 LMPVEDVFSiSGRGTVVTGRIERGVIKVGDEVEIVGIRPTTKTTVTGVEMFRKlLDQGQAGDNAGLLLRGTKRD*VERGQ 80
Cdd:cd03698    3 RLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQPGD 80


                 ...
gi 655576748  81 VLA 83
Cdd:cd03698   81 ILS 83
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 3-90 1.72e-03

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 38.06  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 655576748   3 PVEDVFSIsgRGTVVTGRIERGVIKVGDEVEivgIRP-----TTKTTVTGVEMFRKLLDQgQAGDNA-------GLLLRG 70
Cdd:PTZ00327 256 PGEDIENL--KGGVAGGSILQGVLKVGDEIE---IRPgiiskDSGGEFTCRPIRTRIVSL-FAENNElqyavpgGLIGVG 329

                         90       100
                 ....*....|....*....|....*.
gi 655576748  71 TK------RD*VERGQVLAKPGTITP 90
Cdd:PTZ00327 330 TTidptltRADRLVGQVLGYPGKLPE 355
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 14-62 1.97e-03

Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.


Pssm-ID: 293892 [Multi-domain]  Cd Length: 94  Bit Score: 36.01  E-value: 1.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 655576748  14 GTVVTGRIERGVIKVGDEVEIVGIRPTTKT-TVTGVEMFRKL----LDQGQAGD 62
Cdd:cd03691   15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKgRVTKLFGFEGLerveVEEAEAGD 68
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 7-79 7.12e-03

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 36.57  E-value: 7.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 655576748   7 VFSISGRGTVVTGRIERGVIKVGDEVEIVGIrpTTKTTVTGVEMFRKLLDQGQAGDNAGLLLRG-TKRD*VERG 79
Cdd:PRK10512 182 AFTVKGAGLVVTGTALSGEVKVGDTLWLTGV--NKPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
 
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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