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Conserved domains on  [gi|371560695|gb|AEX37127|]
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elongation factor Tu, partial [Sphingomonas sp. 260]

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
 1-234 1.06e-180

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 500.87  E-value: 1.06e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:PRK00049 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:PRK00049 180 EGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695 161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:PRK00049 260 GVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-234 1.06e-180

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 500.87  E-value: 1.06e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:PRK00049 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:PRK00049 180 EGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695 161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:PRK00049 260 GVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-234 1.20e-174

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: 485.42  E-value: 1.20e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:COG0050  100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:COG0050  180 EGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695 161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:COG0050  260 GVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-234 4.84e-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: 415.33  E-value: 4.84e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695    1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:TIGR00485 100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKAL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   81 EGrdDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:TIGR00485 180 EG--DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVT 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695  161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:TIGR00485 258 GVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQF 331
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-106 3.23e-67

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: 205.51  E-value: 3.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:cd01884   90 DGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKAL 169

                         90       100
                 ....*....|....*....|....*.
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQP 106
Cdd:cd01884  170 EGDDPNKWVDKILELLDALDSYIPTP 195
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-104 4.37e-32

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 115.31  E-value: 4.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695    1 DGAILVVYAADGPMPQTREHILFARQVGVPaLVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAl 80
Cdd:pfam00009  94 DGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKG- 171

                          90       100
                  ....*....|....*....|....
gi 371560695   81 egrddnigkESVLALMADVDAYIP 104
Cdd:pfam00009 172 ---------EGVQTLLDALDEYLP 186
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-234 1.06e-180

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 500.87  E-value: 1.06e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:PRK00049 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:PRK00049 180 EGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695 161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:PRK00049 260 GVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-234 7.29e-175

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 485.88  E-value: 7.29e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:PRK12735 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:PRK12735 180 EGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKETQKTTVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695 161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:PRK12735 260 GVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-234 1.20e-174

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: 485.42  E-value: 1.20e-174
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:COG0050  100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:COG0050  180 EGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695 161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:COG0050  260 GVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-234 2.76e-163

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 456.71  E-value: 2.76e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:PRK12736 100 DGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIgkESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:PRK12736 180 EGDPKWE--DAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQKTVVT 257

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695 161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:PRK12736 258 GVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYRPQF 331
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-234 5.98e-148

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 419.61  E-value: 5.98e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:PLN03127 149 DGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSAL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKD--TKKTT 158
Cdd:PLN03127 229 QGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPggPLKTT 308

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 371560695 159 VTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:PLN03127 309 VTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQF 384
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-234 4.84e-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: 415.33  E-value: 4.84e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695    1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:TIGR00485 100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKAL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   81 EGrdDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVT 160
Cdd:TIGR00485 180 EG--DAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVT 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695  161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:TIGR00485 258 GVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQF 331
tufA CHL00071
elongation factor Tu
 1-234 2.33e-143

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 406.65  E-value: 2.33e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:CHL00071 100 DGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 E--------GRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFK 152
Cdd:CHL00071 180 EaltenpkiKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 153 DTKKTTVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRP 232
Cdd:CHL00071 260 ETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGYRP 339


                 ..
gi 371560695 233 QF 234
Cdd:CHL00071 340 QF 341
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-234 1.37e-119

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 348.91  E-value: 1.37e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:PLN03126 169 DGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLAL 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EG--------RDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFK 152
Cdd:PLN03126 249 EAlmenpnikRGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLR 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 153 DTKKTTVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYVPSKDEGGRHTPFFANYRP 232
Cdd:PLN03126 329 ETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRP 408


                 ..
gi 371560695 233 QF 234
Cdd:PLN03126 409 QF 410
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-106 3.23e-67

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: 205.51  E-value: 3.23e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAL 80
Cdd:cd01884   90 DGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKAL 169

                         90       100
                 ....*....|....*....|....*.
gi 371560695  81 EGRDDNIGKESVLALMADVDAYIPQP 106
Cdd:cd01884  170 EGDDPNKWVDKILELLDALDSYIPTP 195
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 114-200 4.04e-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: 158.45  E-value: 4.04e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 114 FLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERG 193
Cdd:cd03697    1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80


                 ....*..
gi 371560695 194 QVLCKPG 200
Cdd:cd03697   81 MVLAKPG 87
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-214 1.02e-49

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: 167.80  E-value: 1.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVD-DEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAA 79
Cdd:COG5256  110 DAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKG 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  80 legrdDNIGKESV-------LALMADVDAyIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKfeIVGFK 152
Cdd:COG5256  190 -----DNVVKKSDnmpwyngPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDK--VVFMP 261

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371560695 153 DTKKTTVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSV-TPHTEFSAEIYV 214
Cdd:COG5256  262 AGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNPpTVAEEFTAQIVV 324
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-214 1.11e-49

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 167.41  E-value: 1.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAAD--GPMPQTREHILFARQVGVPALVVYMNKVDQVD-DEEILELVEMEIRELLSKYDFPGDDIPVVRGSAL 77
Cdd:PRK12317 109 DAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAF 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  78 aalEGrdDNIGKESV-------LALMADVDAyIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKfeiVG 150
Cdd:PRK12317 189 ---EG--DNVVKKSEnmpwyngPTLLEALDN-LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDK---VV 259

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371560695 151 FKDTKKT-TVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLC---KPGSVTphTEFSAEIYV 214
Cdd:PRK12317 260 FMPAGVVgEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGhpdNPPTVA--EEFTAQIVV 325
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-214 1.33e-39

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: 143.90  E-value: 1.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEiLELVEMEIRELLSKYDFPgdDIPVVRGSA---- 76
Cdd:COG3276   76 DLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDEEW-LELVEEEIRELLAGTFLE--DAPIVPVSAvtge 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  77 -LAALegrddnigKESVLALMADVdayipqPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKdtK 155
Cdd:COG3276  153 gIDEL--------RAALDALAAAV------PARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG--K 216

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 371560695 156 KTTVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKPGSVTPHTEFSAEIYV 214
Cdd:COG3276  217 PVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRL 275
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-104 4.37e-32

Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in several other families such as pfam00071, pfam00025 and pfam00063. Elongation factor Tu consists of three structural domains, this plus two C-terminal beta barrel domains.


Pssm-ID: 425418 [Multi-domain]  Cd Length: 187  Bit Score: 115.31  E-value: 4.37e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695    1 DGAILVVYAADGPMPQTREHILFARQVGVPaLVVYMNKVDQVDDEEILELVEMEIRELLSKYDFPGDDIPVVRGSALAAl 80
Cdd:pfam00009  94 DGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKG- 171

                          90       100
                  ....*....|....*....|....
gi 371560695   81 egrddnigkESVLALMADVDAYIP 104
Cdd:pfam00009 172 ---------EGVQTLLDALDEYLP 186
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-199 1.82e-31

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: 120.75  E-value: 1.82e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695    1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILElVEMEIRELLSKYDFPGDDIPVVrgsaLAAL 80
Cdd:TIGR00475  75 DAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNEEEIKR-TEMFMKQILNSYIFLKNAKIFK----TSAK 149

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   81 EGRDDNIGKESVLALMADVDAyipqpeRPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFkdTKKTTVT 160
Cdd:TIGR00475 150 TGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI--NHEVRVK 221

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 371560695  161 AVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLCKP 199
Cdd:TIGR00475 222 AIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP 260
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-195 2.57e-30

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 116.39  E-value: 2.57e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMP-------QTREHILFARQVGVPALVVYMNKVD--QVD-DEEILELVEMEIRELLSKYDFPGDDIP 70
Cdd:PTZ00141 110 DVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDdkTVNySQERYDEIKKEVSAYLKKVGYNPEKVP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  71 VVrgsALAALEG-----RDDNIGKESVLALMADVDAYIPqPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGek 145
Cdd:PTZ00141 190 FI---PISGWQGdnmieKSDNMPWYKGPTLLEALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPG-- 263

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 371560695 146 fEIVGFKDTKKTT-VTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQV 195
Cdd:PTZ00141 264 -MVVTFAPSGVTTeVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-193 5.33e-23

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 96.66  E-value: 5.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILElVEMEIRELLSKYDFPGDDIPVVrgsalAAL 80
Cdd:PRK10512  76 DHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFAEAKLFVT-----AAT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  81 EGRDDNIGKESVLALmadvdayiPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKdtKKTTVT 160
Cdd:PRK10512 150 EGRGIDALREHLLQL--------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN--KPMRVR 219

                        170       180       190
                 ....*....|....*....|....*....|....
gi 371560695 161 AVKMFRKLLDEGRAGDNIGALVRG-VGREEVERG 193
Cdd:PRK10512 220 GLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 110-200 1.72e-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: 84.93  E-value: 1.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 110 IDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKfeiVGFKDTKKTT-VTAVKMFRKLLDEGRAGDNIGALVRGVGRE 188
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMV---VTFAPAGVTGeVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77

                         90
                 ....*....|..
gi 371560695 189 EVERGQVLCKPG 200
Cdd:cd03693   78 DIKRGDVAGDSK 89
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-195 2.25e-21

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 91.69  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMP-------QTREHILFARQVGVPALVVYMNKVDQVD---DEEILELVEMEIRELLSKYDFPGDDIP 70
Cdd:PLN00043 110 DCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTpkySKARYDEIVKEVSSYLKKVGYNPDKIP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  71 VVrgsALAALEGrDDNIGKESVL------ALMADVDAyIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGe 144
Cdd:PLN00043 190 FV---PISGFEG-DNMIERSTNLdwykgpTLLEALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG- 263

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 371560695 145 kfEIVGFKDTKKTT-VTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQV 195
Cdd:PLN00043 264 --MVVTFGPTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYV 313
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-211 1.64e-19

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 86.06  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADG-PMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEmEIRELLSKYDFpgDDIPVVRGSALAA 79
Cdd:PRK04000 110 DGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYE-QIKEFVKGTVA--ENAPIIPVSALHK 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  80 LegrddNIGkesvlALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGT--------VVTGRVETGILKVGEKFEIV-G 150
Cdd:PRK04000 187 V-----NID-----ALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpG 256

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 371560695 151 FKDTKK---------TTVTAVKMFRKLLDEGRAgdniGALVrGVG--------REEVERGQVLCKPGSVTP-HTEFSAE 211
Cdd:PRK04000 257 IKVEEGgktkwepitTKIVSLRAGGEKVEEARP----GGLV-GVGtkldpsltKADALAGSVAGKPGTLPPvWESLTIE 330
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 128-197 2.96e-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: 76.15  E-value: 2.96e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371560695  128 GTVVTGRVETGILKVGEKFEIVGFKDTKK---TTVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERGQVLC 197
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-77 8.94e-18

GTP translation factor family primarily contains translation initiation, elongation and release factors; The GTP translation factor family consists primarily of translation initiation, elongation, and release factors, which play specific roles in protein translation. In addition, the family includes Snu114p, a component of the U5 small nuclear riboprotein particle which is a component of the spliceosome and is involved in excision of introns, TetM, a tetracycline resistance gene that protects the ribosome from tetracycline binding, and the unusual subfamily CysN/ATPS, which has an unrelated function (ATP sulfurylase) acquired through lateral transfer of the EF1-alpha gene and development of a new function.


Pssm-ID: 206647 [Multi-domain]  Cd Length: 183  Bit Score: 77.72  E-value: 8.94e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQvGVPALVVYMNKVDQVdDEEILELVEMEIRELLSKYDF---PGDDIPVVRGSAL 77
Cdd:cd00881   87 DGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRV-GEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISAL 164
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 114-198 1.35e-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: 74.49  E-value: 1.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 114 FLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKttVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVERG 193
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR--VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78


                 ....*
gi 371560695 194 QVLCK 198
Cdd:cd03696   79 FVLSE 83
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 1-204 1.60e-17

Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction mechanisms];


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 80.83  E-value: 1.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTRehilF----ARQVGVPALVVyMNKVDQvDDEEILELVEmEIRELLSKYDFPGD--DIPVVRG 74
Cdd:COG1217   94 DGVLLLVDAFEGPMPQTR----FvlkkALELGLKPIVV-INKIDR-PDARPDEVVD-EVFDLFIELGATDEqlDFPVVYA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  75 SALAALEGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDT 154
Cdd:COG1217  167 SARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGK 246

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 371560695 155 KKTT-VTAVKMFRKL----LDEGRAGDnIGALvrgVGREEVERGQVLCKPGSVTP 204
Cdd:COG1217  247 VEKGkITKLFGFEGLerveVEEAEAGD-IVAI---AGIEDINIGDTICDPENPEA 297
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
 1-204 5.12e-16

GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]


Pssm-ID: 273597 [Multi-domain]  Cd Length: 594  Bit Score: 76.57  E-value: 5.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695    1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVyMNKVDQvDDEEILELVEmEIRELLSKYDFPGD--DIPVVRGSALA 78
Cdd:TIGR01394  89 DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDR-PSARPDEVVD-EVFDLFAELGADDEqlDFPIVYASGRA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   79 ALEGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGfKDTKKTT 158
Cdd:TIGR01394 166 GWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMK-RDGTIEN 244

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 371560695  159 VTAVKMF------RKLLDEGRAGDnIGALvrgVGREEVERGQVLCKPGSVTP 204
Cdd:TIGR01394 245 GRISKLLgfegleRVEIDEAGAGD-IVAV---AGLEDINIGETIADPEVPEA 292
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 203-234 2.44e-15

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: 68.69  E-value: 2.44e-15
                         10        20        30
                 ....*....|....*....|....*....|..
gi 371560695 203 TPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:cd03707    1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQF 32
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 114-197 1.36e-14

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: 66.52  E-value: 1.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 114 FLMPVEDVFSISGRGTVVTGRVETGILKVGekFEIVGFKDTKKTTVTAVKMFRKLLDEGRAGDNIGALVRGVgrEEVERG 193
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVG--DEIRILPKGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTG 76


                 ....
gi 371560695 194 QVLC 197
Cdd:cd01342   77 DTLT 80
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-85 2.45e-14

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 68.40  E-value: 2.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVDDEEiLELVEMEIRELLSKYDFPgdDIPVVRGSALAAl 80
Cdd:cd04171   75 DAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDEDR-LELVEEEILELLAGTFLA--DAPIFPVSSVTG- 150


                 ....*
gi 371560695  81 EGRDD 85
Cdd:cd04171  151 EGIEE 155
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 201-234 9.10e-13

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: 62.28  E-value: 9.10e-13
                          10        20        30
                  ....*....|....*....|....*....|....
gi 371560695  201 SVTPHTEFSAEIYVPSKDEGGRHTPFFANYRPQF 234
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQF 34
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-91 1.05e-10

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, 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: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 59.43  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADG-------PMPQTREHILFARQVGVPALVVYMNKVDQVD---DEEILELVEMEIRELLSKYDFPGDDIP 70
Cdd:cd01883  102 DVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQERYDEIKKKVSPFLKKVGYNPKDVP 181

                         90       100
                 ....*....|....*....|.
gi 371560695  71 VVRGSalaALEGrdDNIGKES 91
Cdd:cd01883  182 FIPIS---GFTG--DNLIEKS 197
PRK10218 PRK10218
translational GTPase TypA;
1-202 2.17e-10

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 60.11  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVyMNKVDQVDDEEilELVEMEIRELLSKYDFPGD--DIPVVRGSALA 78
Cdd:PRK10218  93 DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARP--DWVVDQVFDLFVNLDATDEqlDFPIVYASALN 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  79 ALEGRDDNIGKESVLALMADVDAYIPQPERPIDKPFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKT- 157
Cdd:PRK10218 170 GIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTIIDSEGKTRNa 249

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 371560695 158 ----TVTAVKMFRKLLDEGRAGDNIGalVRGVGreEVERGQVLCKPGSV 202
Cdd:PRK10218 250 kvgkVLGHLGLERIETDLAEAGDIVA--ITGLG--ELNISDTVCDTQNV 294
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 1-99 3.75e-10

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 56.71  E-value: 3.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPaLVVYMNKVDQVDDEEILelvEMEIRELLSKYDFPGDD----IPVVRGSA 76
Cdd:cd01887   74 DIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTEAD---PERVKNELSELGLVGEEwggdVSIVPISA 149

                         90       100
                 ....*....|....*....|....
gi 371560695  77 LaalegRDDNIGK-ESVLALMADV 99
Cdd:cd01887  150 K-----TGEGIDDlLEAILLLAEV 168
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 114-196 1.15e-09

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: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 114 FLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVTAVKMFRKLL--DEGRAGDNIGALVRGVGREEVE 191
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKFRPVTVKSIHRNRQpvDRARAGQSASFALKKIKRESLR 80


                 ....*
gi 371560695 192 RGQVL 196
Cdd:cd03694   81 KGMVL 85
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-91 1.54e-09

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 56.04  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVD-DEEILELVEMEIRELLSKYDFPgdDIPVVrgsALAA 79
Cdd:cd04166  103 DLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAASLGIE--DITFI---PISA 177

                         90
                 ....*....|..
gi 371560695  80 LEGrdDNIGKES 91
Cdd:cd04166  178 LEG--DNVVSRS 187
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 1-143 1.59e-09

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 57.33  E-value: 1.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPaLVVYMNKVD--QVDDEEIL-ELVEMEIrellskydFP---GDDIPVVRG 74
Cdd:COG0532   76 DIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDkpGANPDRVKqELAEHGL--------VPeewGGDTIFVPV 146

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371560695  75 SALAAlEGRDDNIgkESVLaLMADVDAYIPQPERP---------IDKpflmpvedvfsisGRGTVVTGRVETGILKVG 143
Cdd:COG0532  147 SAKTG-EGIDELL--EMIL-LQAEVLELKANPDRPargtvieakLDK-------------GRGPVATVLVQNGTLKVG 207
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 113-197 7.56e-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: 51.33  E-value: 7.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 113 PFLMPVEDVFSisGRGTVVTGRVETGILKVGEKFEIVGFKdtKKTTVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVER 192
Cdd:cd04089    1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNK--TKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISP 76


                 ....*
gi 371560695 193 GQVLC 197
Cdd:cd04089   77 GFVLC 81
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 1-106 1.49e-08

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 52.98  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVyMNKVDQvDDEEILELVEmEIRELLSKYDFPGD--DIPVVRGSALA 78
Cdd:cd01891   90 DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDR-PDARPEEVVD-EVFDLFLELNATDEqlDFPIVYASAKN 166

                         90       100
                 ....*....|....*....|....*...
gi 371560695  79 ALEGRDDNIGKESVLALMADVDAYIPQP 106
Cdd:cd01891  167 GWASLNLDDPSEDLDPLFETIIEHVPAP 194
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 113-197 1.61e-08

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: 50.20  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 113 PFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTkkTTVTAVKMFRKLLDEGRAGDNIGALVRGVGREEVER 192
Cdd:cd16267    1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78


                 ....*
gi 371560695 193 GQVLC 197
Cdd:cd16267   79 GSILC 83
infB CHL00189
translation initiation factor 2; Provisional
 1-144 3.54e-08

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 53.30  E-value: 3.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPaLVVYMNKVDQVDDEEIlelvemEIRELLSKYDFP----GDDIPVVrgsA 76
Cdd:CHL00189 320 DIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANANTE------RIKQQLAKYNLIpekwGGDTPMI---P 389

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  77 LAALEGRddNIGK--ESVLaLMADVDAYIPQPERPIDKPFLMPVEDVFsisgRGTVVTGRVETGILKVGE 144
Cdd:CHL00189 390 ISASQGT--NIDKllETIL-LLAEIEDLKADPTQLAQGIILEAHLDKT----KGPVATILVQNGTLHIGD 452
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 1-200 9.88e-08

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 51.85  E-value: 9.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVD-DEEILELVEMEIRELLSKYDFPgdDIPVVRGSALaa 79
Cdd:PRK05506 129 DLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAFAAKLGLH--DVTFIPISAL-- 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  80 legRDDNIGKESV-------LALMADVD-AYIPQPERpiDKPFLMPVEDV------FsisgRGtvVTGRVETGILKVGEk 145
Cdd:PRK05506 205 ---KGDNVVTRSArmpwyegPSLLEHLEtVEIASDRN--LKDFRFPVQYVnrpnldF----RG--FAGTVASGVVRPGD- 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371560695 146 fEIVGFKDTKKTTVTAVKMFRKLLDEGRAG--------DNIgalvrgvgreEVERGQVLCKPG 200
Cdd:PRK05506 273 -EVVVLPSGKTSRVKRIVTPDGDLDEAFAGqavtltlaDEI----------DISRGDMLARAD 324
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-212 1.10e-07

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 51.84  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPALVVYMNKVDQVD-DEEILELVEMEIRELLSKydFPGD-DIPVVrgsALA 78
Cdd:PRK05124 132 DLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTFAEQ--LPGNlDIRFV---PLS 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  79 ALEGrdDNIGKESvlALMA--------DVDAYIPQPERPIDKPFLMPVEDVF--SISGRGtvVTGRVETGILKVGEkfEI 148
Cdd:PRK05124 207 ALEG--DNVVSQS--ESMPwysgptllEVLETVDIQRVVDAQPFRFPVQYVNrpNLDFRG--YAGTLASGVVKVGD--RV 278

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 371560695 149 VGFKDTKKTTVTAVKMFRKLLDEGRAGDNIgALVrgVGRE-EVERGQVLCKPGS-VTPHTEFSAEI 212
Cdd:PRK05124 279 KVLPSGKESNVARIVTFDGDLEEAFAGEAI-TLV--LEDEiDISRGDLLVAADEaLQAVQHASADV 341
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 118-196 1.18e-07

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: 1.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 371560695 118 VEDVFSISGRgTVVTGRVETGILKVGEKFEivgfKDTKKTTVTAVKMFRKLLDEGRAGDNIGALVRGVGReeVERGQVL 196
Cdd:cd16265    5 VEKVFKILGR-QVLTGEVESGVIYVGYKVK----GDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVL 76
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-148 2.26e-07

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 50.77  E-value: 2.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVyAADG--PMPQTREHILFARQVGVPALVVYMNKVDQVDDEEILELVEmEIRELLSKYDfpGDDIPVVRGSALA 78
Cdd:PTZ00327 142 DAALLLI-AANEscPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYE-EIRNFVKGTI--ADNAPIIPISAQL 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  79 alegrddnigKESVLALMADVDAYIPQPERPIDKPFLM----------PVEDVFSIsgRGTVVTGRVETGILKVGEKFEI 148
Cdd:PTZ00327 218 ----------KYNIDVVLEYICTQIPIPKRDLTSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 203-233 1.01e-06

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: 45.68  E-value: 1.01e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 371560695 203 TPHTEFSAEIYVPSKDEGGRHTPFFANYRPQ 233
Cdd:cd03706    1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQ 31
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-92 3.96e-06

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 45.82  E-value: 3.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTREHILFARQVGVPaLVVYMNKVDQVDDEEI---LELVEMEIRELLSKYDFPgdDIPVVrgsAL 77
Cdd:cd01889   93 DLMLLVVDAKKGIQTQTAECLVIGELLCKP-LIVVLNKIDLIPEEERkrkIEKMKKRLQKTLEKTRLK--DSPII---PV 166

                         90
                 ....*....|....*
gi 371560695  78 AALEGRDDNIGKESV 92
Cdd:cd01889  167 SAKPGEGEAELGGEL 181
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-204 6.07e-06

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 46.78  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695   1 DGAILVVYAADGPMPQTrEHILfaRQvgvpAL------VVYMNKVD------QVDDEEILE-LVEM--EIRELLSKYDFP 65
Cdd:PRK07560 112 DGAIVVVDAVEGVMPQT-ETVL--RQ----ALrervkpVLFINKVDrlikelKLTPQEMQQrLLKIikDVNKLIKGMAPE 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695  66 GD---------DIPVVRGSAL----------------------AALEGRDDNIGKESVL--ALMADVDAYIPQP------ 106
Cdd:PRK07560 185 EFkekwkvdveDGTVAFGSALynwaisvpmmqktgikfkdiidYYEKGKQKELAEKAPLheVVLDMVVKHLPNPieaqky 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 107 ----------ERPIDK---------PFLMPVEDVFSISGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVTAVKM--F 165
Cdd:PRK07560 265 ripkiwkgdlNSEVGKamlncdpngPLVMMVTDIIVDPHAGEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQVGIYMgpE 344

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 371560695 166 RKLLDEGRAGdNIGALvrgVGREEVERGQVLCKPGSVTP 204
Cdd:PRK07560 345 REEVEEIPAG-NIAAV---TGLKDARAGETVVSVEDMTP 379
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 113-197 1.04e-05

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: 42.49  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560695 113 PFLMPVEDVFSiSGRGTVVTGRVETGILKVGEKFEIVGFKDTKKTTVTAVKMFRKlLDEGRAGDNIGALVRGVGREEVER 192
Cdd:cd03698    1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78


                 ....*
gi 371560695 193 GQVLC 197
Cdd:cd03698   79 GDILS 83
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 1-60 1.04e-05

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 44.92  E-value: 1.04e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560695   1 DGAILVVYAADGPMPQTRehILFA--RQVGVPAlVVYMNKVDQ--VDDEEILelveMEIRELLS 60
Cdd:cd04168   89 DGAILVISAVEGVQAQTR--ILFRllRKLNIPT-IIFVNKIDRagADLEKVY----QEIKEKLS 145
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 1-49 2.35e-05

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 43.80  E-value: 2.35e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 371560695   1 DGAILVVYAADG-PMPQTREHiLFARQV-GVPALVVYMNKVDQVDDEEILE 49
Cdd:cd01888  102 DGALLLIAANEPcPQPQTSEH-LAALEImGLKHIIILQNKIDLVKEEQALE 151
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
 1-77 4.98e-04

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 39.54  E-value: 4.98e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 371560695   1 DGAILVVyaaDGPMPQTRE--HILFARQVGVPALVVYmNKVDQVDDEEILELVEMEIRELLSkydfpgdDIPVVRGSAL 77
Cdd:cd00880   78 DLVLLVV---DSDLTPVEEeaKLGLLRERGKPVLLVL-NKIDLVPESEEEELLRERKLELLP-------DLPVIAVSAL 145
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 114-179 1.34e-03

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: 36.77  E-value: 1.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 371560695 114 FLMPVEDV--FSISGRGtvVTGRVETGILKVGEkfEIVGFKDTKKTTVTAVKMFRKLLDEGRAGDNIG 179
Cdd:cd03695    1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGD--EVTVLPSGKTSRVKSIVTFDGELDSAGAGEAVT 64
 
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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