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Conserved domains on  [gi|371560719|gb|AEX37139|]
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elongation factor Tu, partial [Sphingomonas sp. 562]

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 4.21e-170

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 473.91  E-value: 4.21e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:PRK00049 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:PRK00049 180 EGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719 161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:PRK00049 260 GVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-234 4.21e-170

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 473.91  E-value: 4.21e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:PRK00049 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:PRK00049 180 EGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719 161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:PRK00049 260 GVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-234 2.19e-163

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: 456.92  E-value: 2.19e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:COG0050  100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:COG0050  180 EGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719 161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:COG0050  260 GVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-234 1.18e-135

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: 386.44  E-value: 1.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719    1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:TIGR00485 100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKAL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   81 DGVNpeIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:TIGR00485 180 EGDA--EWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVT 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719  161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:TIGR00485 258 GVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQF 331
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 114-200 9.36e-55

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: 170.01  E-value: 9.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 114 FLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERG 193
Cdd:cd03697    1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80


                 ....*..
gi 371560719 194 QVLCKPG 200
Cdd:cd03697   81 MVLAKPG 87
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-104 9.84e-24

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: 93.74  E-value: 9.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719    1 DGAILVVSAADGPMPQTREHILLARQVGVPaLVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAt 80
Cdd:pfam00009  94 DGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKG- 171

                          90       100
                  ....*....|....*....|....
gi 371560719   81 DGVNPeigeqrilaLMETVDSYIP 104
Cdd:pfam00009 172 EGVQT---------LLDALDEYLP 186
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-234 4.21e-170

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 473.91  E-value: 4.21e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:PRK00049 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:PRK00049 180 EGDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRDTQKTTVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719 161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:PRK00049 260 GVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-234 4.41e-165

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 461.23  E-value: 4.41e-165
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:PRK12735 100 DGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:PRK12735 180 EGDDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKETQKTTVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719 161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:PRK12735 260 GVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-234 2.19e-163

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: 456.92  E-value: 2.19e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:COG0050  100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:COG0050  180 EGDPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRDTQKTVVT 259

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719 161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:COG0050  260 GVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQF 333
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-234 2.17e-155

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 436.68  E-value: 2.17e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:PRK12736 100 DGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEigEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:PRK12736 180 EGDPKW--EDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKETQKTVVT 257

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719 161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:PRK12736 258 GVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYRPQF 331
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-234 5.16e-139

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 397.27  E-value: 5.16e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:PLN03127 149 DGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSAL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPV--QKTT 158
Cdd:PLN03127 229 QGTNDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPGgpLKTT 308

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 371560719 159 CTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:PLN03127 309 VTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQF 384
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-234 1.18e-135

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: 386.44  E-value: 1.18e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719    1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:TIGR00485 100 DGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKAL 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   81 DGVNpeIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCT 160
Cdd:TIGR00485 180 EGDA--EWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKDTRKTTVT 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 371560719  161 GVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:TIGR00485 258 GVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQF 331
tufA CHL00071
elongation factor Tu
 1-234 2.16e-133

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 381.23  E-value: 2.16e-133
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:CHL00071 100 DGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLAL 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGV--NPEI--GEQ----RILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIR 152
Cdd:CHL00071 180 EALteNPKIkrGENkwvdKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLR 259

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 153 PVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRP 232
Cdd:CHL00071 260 ETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGYRP 339


                 ..
gi 371560719 233 QF 234
Cdd:CHL00071 340 QF 341
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-234 1.60e-112

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 330.81  E-value: 1.60e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:PLN03126 169 DGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLAL 248

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGV--NPEI--GEQ----RILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIR 152
Cdd:PLN03126 249 EALmeNPNIkrGDNkwvdKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLR 328

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 153 PVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYILTKEEGGRHTPFFTNYRP 232
Cdd:PLN03126 329 ETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRP 408


                 ..
gi 371560719 233 QF 234
Cdd:PLN03126 409 QF 410
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 114-200 9.36e-55

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: 170.01  E-value: 9.36e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 114 FLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRPVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERG 193
Cdd:cd03697    1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80


                 ....*..
gi 371560719 194 QVLCKPG 200
Cdd:cd03697   81 MVLAKPG 87
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-106 7.63e-48

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: 156.20  E-value: 7.63e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAT 80
Cdd:cd01884   90 DGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKAL 169

                         90       100
                 ....*....|....*....|....*.
gi 371560719  81 DGVNPEIGEQRILALMETVDSYIPQP 106
Cdd:cd01884  170 EGDDPNKWVDKILELLDALDSYIPTP 195
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-215 2.65e-38

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: 137.37  E-value: 2.65e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVD-DEELLELVEMEVRELLSSYQFPGDDIPITKGSakaA 79
Cdd:COG5256  110 DAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVS---A 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  80 TDGVN-----PEIGEQRILALMETVDSyIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVgirPV 154
Cdd:COG5256  187 WKGDNvvkksDNMPWYNGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFM---PA 262

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371560719 155 QKTT-CTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGS-ITPHTKFVAEAYIL 215
Cdd:COG5256  263 GVVGeVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNpPTVAEEFTAQIVVL 325
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-199 5.70e-36

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 131.20  E-value: 5.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAAD--GPMPQTREHILLARQVGVPALVVFMNKVDLVD-DEELLELVEMEVRELLSSYQFPGDDIPITKGSAk 77
Cdd:PRK12317 109 DAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSA- 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  78 aaTDGVN-----PEIGEQRILALMETVDSyIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEivgIR 152
Cdd:PRK12317 188 --FEGDNvvkksENMPWYNGPTLLEALDN-LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVV---FM 261

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 371560719 153 PVQKT-TCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKP 199
Cdd:PRK12317 262 PAGVVgEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHP 309
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-215 3.77e-28

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: 111.54  E-value: 3.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKvDLVDDEELLELVEMEVRELLSSYQFPgdDIPITKGSakaAT 80
Cdd:COG3276   76 DLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTK-ADLVDEEWLELVEEEIRELLAGTFLE--DAPIVPVS---AV 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNpeIGE--QRILALMETVdsyipqPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRpvQKTT 158
Cdd:COG3276  150 TGEG--IDElrAALDALAAAV------PARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSG--KPVR 219

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 371560719 159 CTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKPGSITPHTKFVAEAYIL 215
Cdd:COG3276  220 VRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLL 276
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-199 8.33e-24

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: 99.18  E-value: 8.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719    1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKvDLVDDEELLELVEMEVRELLSSYQFpGDDIPITKGSAKAAT 80
Cdd:TIGR00475  75 DAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITK-ADRVNEEEIKRTEMFMKQILNSYIF-LKNAKIFKTSAKTGQ 152

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   81 DgvnpeIGEQR--ILALMETVDSYIPQPerpvdlPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRpvQKTT 158
Cdd:TIGR00475 153 G-----IGELKkeLKNLLESLDIKRIQK------PLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPIN--HEVR 219

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 371560719  159 CTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLCKP 199
Cdd:TIGR00475 220 VKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP 260
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 1-195 8.99e-24

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 98.28  E-value: 8.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMP-------QTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVREL---LSSYQFPGDDIP 70
Cdd:PTZ00141 110 DVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVsayLKKVGYNPEKVP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  71 ITKGSAKAATDGV--NPEIGEQRILALMETVDSYIPqPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGeevEI 148
Cdd:PTZ00141 190 FIPISGWQGDNMIekSDNMPWYKGPTLLEALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPG---MV 265

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 371560719 149 VGIRPVQKTT-CTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQV 195
Cdd:PTZ00141 266 VTFAPSGVTTeVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-104 9.84e-24

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: 93.74  E-value: 9.84e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719    1 DGAILVVSAADGPMPQTREHILLARQVGVPaLVVFMNKVDLVDDEELLELVEMEVRELLSSYQFPGDDIPITKGSAKAAt 80
Cdd:pfam00009  94 DGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKG- 171

                          90       100
                  ....*....|....*....|....
gi 371560719   81 DGVNPeigeqrilaLMETVDSYIP 104
Cdd:pfam00009 172 EGVQT---------LLDALDEYLP 186
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 110-200 7.79e-21

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


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 83.39  E-value: 7.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 110 VDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVgirPVQKTT-CTGVEMFRKLLDQGQAGDNVGVLLRGTKRE 188
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA---PAGVTGeVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77

                         90
                 ....*....|..
gi 371560719 189 DVERGQVLCKPG 200
Cdd:cd03693   78 DIKRGDVAGDSK 89
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 114-198 1.41e-18

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: 77.18  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 114 FLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRpvQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERG 193
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG--KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78


                 ....*
gi 371560719 194 QVLCK 198
Cdd:cd03696   79 FVLSE 83
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 128-197 2.11e-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: 76.54  E-value: 2.11e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371560719  128 GTVVTGRVEKGIIKVGEEVEIVGIRPVQK---TTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQVLC 197
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKkivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 203-234 9.83e-18

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: 75.24  E-value: 9.83e-18
                         10        20        30
                 ....*....|....*....|....*....|..
gi 371560719 203 TPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:cd03707    1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQF 32
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-195 7.99e-17

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 78.59  E-value: 7.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMP-------QTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVREL---LSSYQFPGDDIP 70
Cdd:PLN00043 110 DCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVssyLKKVGYNPDKIP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  71 ITKGSAKAATDGV--NPEIGEQRILALMETVDSyIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGeevEI 148
Cdd:PLN00043 190 FVPISGFEGDNMIerSTNLDWYKGPTLLEALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MV 265

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 371560719 149 VGIRPVQKTT-CTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVERGQV 195
Cdd:PLN00043 266 VTFGPTGLTTeVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYV 313
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-193 8.97e-17

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 78.55  E-value: 8.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVrELLSSYQFPGDDIPITkgsakAAT 80
Cdd:PRK10512  76 DHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAEVRRQVK-AVLREYGFAEAKLFVT-----AAT 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  81 DGVNPEIGEQRILALmetvdsyiPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGI-RPVQkttC 159
Cdd:PRK10512 150 EGRGIDALREHLLQL--------PEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVnKPMR---V 218

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 371560719 160 TGVEMFRKLLDQGQAGDNVGVLLRG-TKREDVERG 193
Cdd:PRK10512 219 RGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 201-234 1.20e-14

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: 67.29  E-value: 1.20e-14
                          10        20        30
                  ....*....|....*....|....*....|....
gi 371560719  201 SITPHTKFVAEAYILTKEEGGRHTPFFTNYRPQF 234
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQF 34
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 114-197 1.61e-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: 1.61e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 114 FLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIrpVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKreDVERG 193
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK--GITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76


                 ....
gi 371560719 194 QVLC 197
Cdd:cd01342   77 DTLT 80
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-219 2.50e-14

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 71.04  E-value: 2.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADG-PMPQTREHILLARQVGVPALVVFMNKvdlvddeelleLVEMEVRELLSSYQ----FP----GDDIPI 71
Cdd:PRK04000 110 DGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNK-----------IDLVSKERALENYEqikeFVkgtvAENAPI 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  72 TKGSAKaatDGVNpeigeqrILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGT--------VVTGRVEKGIIKVG 143
Cdd:PRK04000 179 IPVSAL---HKVN-------IDALIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVG 248

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 144 EEVEIVGIRPVQK----------TTCTGVEMFRKLLDQGQAGDNVGVllrGTK------REDVERGQVLCKPGSITP-HT 206
Cdd:PRK04000 249 DEIEIRPGIKVEEggktkwepitTKIVSLRAGGEKVEEARPGGLVGV---GTKldpsltKADALAGSVAGKPGTLPPvWE 325

                        250
                 ....*....|....*...
gi 371560719 207 KFVAEAYIL-----TKEE 219
Cdd:PRK04000 326 SLTIEVHLLervvgTKEE 343
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 1-201 1.22e-12

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: 66.26  E-value: 1.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKvdlvddeel-lelvemevRELLSSYQFPGDD-IPItkgsakA 78
Cdd:COG2895  120 DLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKmdlvdyseevfeeivadyRAFAAKLGLEDITfIPI------S 193

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  79 ATDGVN-------------PeigeqrilALMETVDSyIPQPERPVDLPFLMPVEDV--FSISGRGtvVTGRVEKGIIKVG 143
Cdd:COG2895  194 ALKGDNvversenmpwydgP--------TLLEHLET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVG 262

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371560719 144 EEVEIV--GirpvQKTTCTGVEMFRKLLDQGQAGDNVGVLLrgtKRE-DVERGQVLCKPGS 201
Cdd:COG2895  263 DEVVVLpsG----KTSTVKSIVTFDGDLEEAFAGQSVTLTL---EDEiDISRGDVIVAADA 316
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
 1-199 8.01e-11

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: 61.16  E-value: 8.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719    1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVfMNKVDLVDDEELLELVEMEvrELLSSYQFPGD--DIPITKGSAKA 78
Cdd:TIGR01394  89 DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARPDEVVDEVF--DLFAELGADDEqlDFPIVYASGRA 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   79 ATDGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGI-RPVQKT 157
Cdd:TIGR01394 166 GWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIGRVHRGTVKKGQQVALMKRdGTIENG 245

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 371560719  158 TCTGVEMFRKL----LDQGQAGDNVGVllrgTKREDVERGQVLCKP 199
Cdd:TIGR01394 246 RISKLLGFEGLerveIDEAGAGDIVAV----AGLEDINIGETIADP 287
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 1-204 1.92e-10

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 60.03  E-value: 1.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTRehILL--ARQVGVPALVVfMNKvdlvddeellelvemEVR-------------ELL-----S 60
Cdd:COG1217   94 DGVLLLVDAFEGPMPQTR--FVLkkALELGLKPIVV-INK---------------IDRpdarpdevvdevfDLFielgaT 155

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  61 SYQFpgdDIPITKGSAKAATDGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGII 140
Cdd:COG1217  156 DEQL---DFPVVYASARNGWASLDLDDPGEDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTI 232

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 371560719 141 KVGEEVEIVGIR-PVQKTTCTGVEMFRKL----LDQGQAGDNVGVllrgTKREDVERGQVLCKPGSITP 204
Cdd:COG1217  233 KKGQQVALIKRDgKVEKGKITKLFGFEGLerveVEEAEAGDIVAI----AGIEDINIGDTICDPENPEA 297
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 113-197 5.92e-10

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: 54.06  E-value: 5.92e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 113 PFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIVGIRpvQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDVER 192
Cdd:cd16267    1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSN--ETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78


                 ....*
gi 371560719 193 GQVLC 197
Cdd:cd16267   79 GSILC 83
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-38 6.87e-10

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: 56.53  E-value: 6.87e-10
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQvGVPALVVFMNK 38
Cdd:cd00881   87 DGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNK 123
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 113-197 8.57e-10

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: 53.64  E-value: 8.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 113 PFLMPVEDVFSisGRGTVVTGRVEKGIIKVGE---------EVEIVGIrpvqktTCTGVEMfrkllDQGQAGDNVGVLLR 183
Cdd:cd04089    1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGI------YIDEEEV-----DSAKPGENVKLKLK 67

                         90
                 ....*....|....
gi 371560719 184 GTKREDVERGQVLC 197
Cdd:cd04089   68 GVEEEDISPGFVLC 81
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 114-196 1.87e-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: 52.99  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 114 FLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIvGIRPVQK---TTCTGVEMFRKLLDQGQAGDNVGVLLRGTKREDV 190
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLL-GPDADGKfrpVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79


                 ....*.
gi 371560719 191 ERGQVL 196
Cdd:cd03694   80 RKGMVL 85
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 1-38 2.24e-08

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: 52.88  E-value: 2.24e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 371560719   1 DGAILVVSAADG-------PMPQTREHILLARQVGVPALVVFMNK 38
Cdd:cd01883  102 DVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNK 146
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 118-196 3.74e-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: 49.22  E-value: 3.74e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 371560719 118 VEDVFSISGRgTVVTGRVEKGIIKVGEEVeivgIRPVQKTTCTGVEMFRKLLDQGQAGDNVGVLLRGtkREDVERGQVL 196
Cdd:cd16265    5 VEKVFKILGR-QVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVL 76
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 1-38 4.72e-08

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: 50.93  E-value: 4.72e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPaLVVFMNK 38
Cdd:cd01887   74 DIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINK 110
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 113-197 6.02e-08

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: 48.65  E-value: 6.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 113 PFLMPVEDVFSiSGRGTVVTGRVEKGIIKVGEEVEIVGIrpvqKTTCTGVEMFRKL---LDQGQAGDNVGVLLRGTKRED 189
Cdd:cd03698    1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPS----QQDAEVKNIIRNSdeeTDWAIAGDTVTLRLRGIEVED 75


                 ....*...
gi 371560719 190 VERGQVLC 197
Cdd:cd03698   76 IQPGDILS 83
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 203-233 1.73e-07

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: 47.61  E-value: 1.73e-07
                         10        20        30
                 ....*....|....*....|....*....|.
gi 371560719 203 TPHTKFVAEAYILTKEEGGRHTPFFTNYRPQ 233
Cdd:cd03706    1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQ 31
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-38 2.20e-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 bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 46.44  E-value: 2.20e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNK 38
Cdd:cd04171   75 DAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTK 112
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 1-38 3.74e-06

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: 46.93  E-value: 3.74e-06
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPaLVVFMNK 38
Cdd:COG0532   76 DIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINK 112
PRK10218 PRK10218
translational GTPase TypA;
1-149 5.87e-06

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 46.63  E-value: 5.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVfMNKVDLVDDEELLELVEMEvrELLSSYQFPGD--DIPITKGSAKA 78
Cdd:PRK10218  93 DSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDFPIVYASALN 169

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 371560719  79 ATDGVNPEIGEQRILALMETVDSYIPQPERPVDLPFLMPVEDVFSISGRGTVVTGRVEKGIIKVGEEVEIV 149
Cdd:PRK10218 170 GIAGLDHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-204 1.04e-05

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 45.77  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADG-PMPQTREHILLARQVGVPALVVFMNKVDLVDDEELLELVEMEVRELLSSYqfpGDDIPITKGSAKAa 79
Cdd:PTZ00327 142 DAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTI---ADNAPIIPISAQL- 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  80 tdGVNpeigeqrILALMETVDSYIPQPERPVDLPFLM----------PVEDVFSIsgRGTVVTGRVEKGIIKVGEEVEiv 149
Cdd:PTZ00327 218 --KYN-------IDVVLEYICTQIPIPKRDLTSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIE-- 284

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371560719 150 gIRP-----VQKTTCTGVEMFRKLLDQgQAGDNV-------GVLLRGTK------REDVERGQVLCKPGSITP 204
Cdd:PTZ00327 285 -IRPgiiskDSGGEFTCRPIRTRIVSL-FAENNElqyavpgGLIGVGTTidptltRADRLVGQVLGYPGKLPE 355
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 1-106 1.50e-05

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: 44.12  E-value: 1.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVfMNKVDLVDDEELLELVEMEvrELLSSYQFPGD--DIPITKGSAKA 78
Cdd:cd01891   90 DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPDARPEEVVDEVF--DLFLELNATDEqlDFPIVYASAKN 166

                         90       100
                 ....*....|....*....|....*...
gi 371560719  79 ATDGVNPEIGEQRILALMETVDSYIPQP 106
Cdd:cd01891  167 GWASLNLDDPSEDLDPLFETIIEHVPAP 194
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 114-196 1.94e-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: 41.78  E-value: 1.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 114 FLMPVEDV--FSISGRGtvVTGRVEKGIIKVGEEVEIVgirPVQKTTC-TGVEMFRKLLDQGQAGDNVGVLLrgtKRE-D 189
Cdd:cd03695    1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTVL---PSGKTSRvKSIVTFDGELDSAGAGEAVTLTL---EDEiD 72


                 ....*..
gi 371560719 190 VERGQVL 196
Cdd:cd03695   73 VSRGDLI 79
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 1-38 5.65e-04

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: 39.91  E-value: 5.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTRehIL--LARQVGVPAlVVFMNK 38
Cdd:cd04168   89 DGAILVISAVEGVQAQTR--ILfrLLRKLNIPT-IIFVNK 125
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 1-201 2.13e-03

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 38.74  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNKvdlvddEELLELVEMEVRELLSSY-----QFPGDD----IPI 71
Cdd:PRK05124 132 DLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNK------MDLVDYSEEVFERIREDYltfaeQLPGNLdirfVPL 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719  72 TkgsakaATDGVNPEIGEQR--------ILALMETVDSyipqpERPVD-LPFLMPVEDVF--SISGRGtvVTGRVEKGII 140
Cdd:PRK05124 206 S------ALEGDNVVSQSESmpwysgptLLEVLETVDI-----QRVVDaQPFRFPVQYVNrpNLDFRG--YAGTLASGVV 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 371560719 141 KVGEEVEIVgirPVQKT-TCTGVEMFRKLLDQGQAGDNVGVLLrgtKRE-DVERGQVLCKPGS 201
Cdd:PRK05124 273 KVGDRVKVL---PSGKEsNVARIVTFDGDLEEAFAGEAITLVL---EDEiDISRGDLLVAADE 329
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 1-38 4.35e-03

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: 37.16  E-value: 4.35e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 371560719   1 DGAILVVSAADGPMPQTREHILLARQVGVPALVVFMNK 38
Cdd:cd04166  103 DLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNK 140
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 128-204 6.28e-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: 34.86  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 371560719 128 GTVVTGRVEKGIIKVGEEVEIVGIRPVQKT-TCTGVEMFRKL----LDQGQAGDNVGVllrgTKREDVERGQVLCKPGSI 202
Cdd:cd03691   15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKgRVTKLFGFEGLerveVEEAEAGDIVAI----AGLEDITIGDTICDPEVP 90


                 ..
gi 371560719 203 TP 204
Cdd:cd03691   91 EP 92
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 1-38 9.20e-03

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 36.76  E-value: 9.20e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 371560719   1 DGAILVVSAADGPMPQTrEHILlaRQvgvpAL------VVFMNK 38
Cdd:PRK07560 112 DGAIVVVDAVEGVMPQT-ETVL--RQ----ALrervkpVLFINK 148
 
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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