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Conserved domains on  [gi|1018194321|gb|AMY27305|]
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elongation factor tu, partial (chloroplast) [Predaea sp. LAF7027]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tufA super family cl31776
elongation factor Tu
 1-237 7.45e-177

elongation factor Tu


The actual alignment was detected with superfamily member CHL00071:

Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 491.78  E-value: 7.45e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:CHL00071  101 GAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 KITEESNIQKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:CHL00071  181 ALTENPKIKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRE 260

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:CHL00071  261 TKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGY 337
 
Name Accession Description Interval E-value
tufA CHL00071
elongation factor Tu
 1-237 7.45e-177

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 491.78  E-value: 7.45e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:CHL00071  101 GAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 KITEESNIQKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:CHL00071  181 ALTENPKIKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRE 260

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:CHL00071  261 TKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGY 337
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-237 7.69e-165

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: 460.77  E-value: 7.69e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:COG0050   101 GAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 KiteesniqKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:COG0050   181 G--------DPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRD 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:COG0050   253 TQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGY 329
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-237 7.04e-142

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: 402.62  E-value: 7.04e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:TIGR00485 101 GAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 kiteesniqkGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:TIGR00485 181 ----------GDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKD 250

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:TIGR00485 251 TRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGY 327
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-113 3.18e-63

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: 195.49  E-value: 3.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:cd01884    91 GAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALE 170

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1018194321  81 KITEesniqkgsDVWVDKIHKLMDAIDDYIPTP 113
Cdd:cd01884   171 GDDP--------NKWVDKILELLDALDSYIPTP 195
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-112 2.97e-31

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: 113.39  E-value: 2.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPkIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKAle 80
Cdd:pfam00009  95 GAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKG-- 171

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1018194321  81 kiteesniqkgsdvwvDKIHKLMDAIDDYIPT 112
Cdd:pfam00009 172 ----------------EGVQTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
tufA CHL00071
elongation factor Tu
 1-237 7.45e-177

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 491.78  E-value: 7.45e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:CHL00071  101 GAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 KITEESNIQKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:CHL00071  181 ALTENPKIKRGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRE 260

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:CHL00071  261 TKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGY 337
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-237 5.14e-167

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 466.20  E-value: 5.14e-167
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:PRK00049  101 GAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 kiteesniQKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:PRK00049  181 --------GDDDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRD 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:PRK00049  253 TQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGY 329
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-237 7.69e-165

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: 460.77  E-value: 7.69e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:COG0050   101 GAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 KiteesniqKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:COG0050   181 G--------DPDPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRD 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:COG0050   253 TQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGY 329
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-237 5.95e-160

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 448.52  E-value: 5.95e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:PRK12735  101 GAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 KiteesniqKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:PRK12735  181 G--------DDDEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKE 252

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:PRK12735  253 TQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGY 329
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-237 8.09e-151

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 425.13  E-value: 8.09e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:PRK12736  101 GAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 kiteesniqkGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:PRK12736  181 ----------GDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKE 250

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:PRK12736  251 TQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNY 327
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-237 1.76e-142

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 407.08  E-value: 1.76e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:PLN03126  170 GAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALE 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 KITEESNIQKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:PLN03126  250 ALMENPNIKRGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRE 329

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:PLN03126  330 TRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGY 406
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-237 7.04e-142

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: 402.62  E-value: 7.04e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:TIGR00485 101 GAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALE 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 kiteesniqkGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:TIGR00485 181 ----------GDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKD 250

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 161 TATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:TIGR00485 251 TRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGY 327
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-237 1.67e-127

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 368.00  E-value: 1.67e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:PLN03127  150 GGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQ 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 KITEEsniqkgsdVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:PLN03127  230 GTNDE--------IGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRP 301

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1018194321 161 TAT--TTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:PLN03127  302 GGPlkTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNY 380
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-113 3.18e-63

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: 195.49  E-value: 3.18e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALE 80
Cdd:cd01884    91 GAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALE 170

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1018194321  81 KITEesniqkgsDVWVDKIHKLMDAIDDYIPTP 113
Cdd:cd01884   171 GDDP--------NKWVDKILELLDALDSYIPTP 195
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 121-207 1.22e-53

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: 167.31  E-value: 1.22e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 121 FLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKETATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERG 200
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80


                  ....*..
gi 1018194321 201 MVLAQPG 207
Cdd:cd03697    81 MVLAKPG 87
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-222 1.51e-45

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: 156.63  E-value: 1.51e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVD-DKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKAle 80
Cdd:COG5256   112 AILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWKG-- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 kiteeSNIQKGSD--VWVdKIHKLMDAIDDyIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTieIVGL 158
Cdd:COG5256   190 -----DNVVKKSDnmPWY-NGPTLLEALDN-LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDK--VVFM 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1018194321 159 KETATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGT-ITPHTQFEAEVYIL 222
Cdd:COG5256   261 PAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPDNpPTVAEEFTAQIVVL 325
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-222 1.09e-42

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 149.31  E-value: 1.09e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAAD--GPMPQTREHILLAKQVGVPKIVVFLNKEDQVD-DKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKA 78
Cdd:PRK12317  111 AVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAFEG 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  79 lekiteeSNIQKGSD--VWVDKiHKLMDAIDDyIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTieIV 156
Cdd:PRK12317  191 -------DNVVKKSEnmPWYNG-PTLLEALDN-LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDK--VV 259

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321 157 GLKETATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTI-TPHTQFEAEVYIL 222
Cdd:PRK12317  260 FMPAGVVGEVKSIEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHPDNPpTVAEEFTAQIVVL 326
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 2-222 6.88e-40

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: 144.67  E-value: 6.88e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDkELLELVQLEVTEVLDQYDFPGSeiPFISGSAlkalek 81
Cdd:COG3276    78 VLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADLVDE-EWLELVEEEIRELLAGTFLEDA--PIVPVSA------ 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  82 ITEESniqkgsdvwvdkIHKLMDAIDDYI-PTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKE 160
Cdd:COG3276   149 VTGEG------------IDELRAALDALAaAVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPSGK 216

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1018194321 161 TAttTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQPGTITPHTQFEAEVYIL 222
Cdd:COG3276   217 PV--RVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLL 276
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-112 2.97e-31

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: 113.39  E-value: 2.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPkIVVFLNKEDQVDDKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKAle 80
Cdd:pfam00009  95 GAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKG-- 171

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1018194321  81 kiteesniqkgsdvwvDKIHKLMDAIDDYIPT 112
Cdd:pfam00009 172 ----------------EGVQTLLDALDEYLPS 187
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-202 3.77e-27

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 107.91  E-value: 3.77e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMP-------QTREHILLAKQVGVPKIVVFLNKED--QVD-DKELLELVQLEVTEVLDQYDFPGSEIPFI 71
Cdd:PTZ00141  112 AILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDdkTVNySQERYDEIKKEVSAYLKKVGYNPEKVPFI 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  72 SGSALKALEKITEESNIQkgsdvWVdKIHKLMDAIDDYIPtPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGD 151
Cdd:PTZ00141  192 PISGWQGDNMIEKSDNMP-----WY-KGPTLLEALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGM 264

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1018194321 152 TIEIVglKETATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMV 202
Cdd:PTZ00141  265 VVTFA--PSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYV 313
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 1-206 1.06e-26

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: 107.65  E-value: 1.06e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDkELLELVQLEVTEVLDQYDF-PGSEIPFISGSALKAL 79
Cdd:TIGR00475  76 AALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKADRVNE-EEIKRTEMFMKQILNSYIFlKNAKIFKTSAKTGQGI 154

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  80 EKITEEsniqkgsdvwvdkIHKLMDAIDdyiptpVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLK 159
Cdd:TIGR00475 155 GELKKE-------------LKNLLESLD------IKRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPIN 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1018194321 160 EtaTTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLAQP 206
Cdd:TIGR00475 216 H--EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP 260
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-226 6.91e-24

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 98.39  E-value: 6.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADG-PMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLELVQlEVTEVLDQYDFPGSEIPFISgsalkAL 79
Cdd:PRK04000  111 GAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDLVSKERALENYE-QIKEFVKGTVAENAPIIPVS-----AL 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  80 EKIteesNIqkgsDVwvdkihkLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGT--------VATGRIERGVIKVGD 151
Cdd:PRK04000  185 HKV----NI----DA-------LIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGD 249

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 152 TIEIV-GLK---------ETATTTITGLEMFQKTLDEGMAGDNIGI---LLRGVQKKDIERGMVLAQPGTITP-HTQFEA 217
Cdd:PRK04000  250 EIEIRpGIKveeggktkwEPITTKIVSLRAGGEKVEEARPGGLVGVgtkLDPSLTKADALAGSVAGKPGTLPPvWESLTI 329

                         250
                  ....*....|....
gi 1018194321 218 EVYIL-----TKEE 226
Cdd:PRK04000  330 EVHLLervvgTKEE 343
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 121-205 7.25e-22

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: 85.66  E-value: 7.25e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 121 FLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKEtaTTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERG 200
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGK--EVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78


                  ....*
gi 1018194321 201 MVLAQ 205
Cdd:cd03696    79 FVLSE 83
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 2-206 2.11e-20

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 89.34  E-value: 2.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLElVQLEVTEVLDQYDFPGSEIpFISGSalkalek 81
Cdd:PRK10512   78 ALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKADRVDEARIAE-VRRQVKAVLREYGFAEAKL-FVTAA------- 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  82 iTEESNIqkgsdvwvdkihklmDAIDDYI---PTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGL 158
Cdd:PRK10512  149 -TEGRGI---------------DALREHLlqlPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGV 212

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1018194321 159 KEtaTTTITGLEMFQKTLDEGMAGDNIGILLRG-VQKKDIERG-MVLAQP 206
Cdd:PRK10512  213 NK--PMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRGdWLLADA 260
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 15-202 5.07e-20

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 87.84  E-value: 5.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  15 QTREHILLAKQVGVPKIVVFLNKEDQVD---DKELLELVQLEVTEVLDQYDFPGSEIPFISGSALKALEKITEESNIQkg 91
Cdd:PLN00043  132 QTREHALLAFTLGVKQMICCCNKMDATTpkySKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLD-- 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  92 sdvWVdKIHKLMDAIDDyIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGdtiEIVGLKETA-TTTITGLE 170
Cdd:PLN00043  210 ---WY-KGPTLLEALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGlTTEVKSVE 281

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1018194321 171 MFQKTLDEGMAGDNIGILLRGVQKKDIERGMV 202
Cdd:PLN00043  282 MHHESLQEALPGDNVGFNVKNVAVKDLKRGYV 313
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 135-204 1.37e-19

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: 79.62  E-value: 1.37e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1018194321 135 GTVATGRIERGVIKVGDTIEIVG---LKETATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVLA 204
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 1-187 7.82e-19

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 84.69  E-value: 7.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTRehILLAK--QVGVPKIVVfLNKED-------QVDDkELLEL-VQLEVTEvlDQYDFpgseiPF 70
Cdd:COG1217    95 GVLLLVDAFEGPMPQTR--FVLKKalELGLKPIVV-INKIDrpdarpdEVVD-EVFDLfIELGATD--EQLDF-----PV 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  71 ISGSAL--KALEKITEESniqkgsdvwvDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIK 148
Cdd:COG1217   164 VYASARngWASLDLDDPG----------EDLTPLFDTILEHVPAPEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIK 233

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1018194321 149 VGDTIEIVGLK-ETATTTITGLEMFQ----KTLDEGMAGDNIGI 187
Cdd:COG1217   234 KGQQVALIKRDgKVEKGKITKLFGFEglerVEVEEAEAGDIVAI 277
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 117-202 2.55e-18

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: 76.84  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 117 VEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIvgLKETATTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKD 196
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTF--APAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVKD 78


                  ....*.
gi 1018194321 197 IERGMV 202
Cdd:cd03693    79 IKRGDV 84
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
 1-187 3.64e-18

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: 82.73  E-value: 3.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVfLNKEDQVDDK------ELLEL-VQLEVTEvlDQYDFPgseIPFISG 73
Cdd:TIGR01394  90 GVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARpdevvdEVFDLfAELGADD--EQLDFP---IVYASG 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  74 SALKALEKITEESniqkgsdvwvDKIHKLMDAIDDYIPTPVRDVEKTFLMAVE--DVFSITGRgtVATGRIERGVIKVGD 151
Cdd:TIGR01394 164 RAGWASLDLDDPS----------DNMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRVHRGTVKKGQ 231

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1018194321 152 TIEIVGLKETATTT-ITGLEMFQ----KTLDEGMAGDNIGI 187
Cdd:TIGR01394 232 QVALMKRDGTIENGrISKLLGFEglerVEIDEAGAGDIVAV 272
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 2-219 5.97e-18

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: 81.67  E-value: 5.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVD-DKELLELVQLEVTEVLDQYDFPgsEIPFISGSALKAle 80
Cdd:COG2895   122 AILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDySEEVFEEIVADYRAFAAKLGLE--DITFIPISALKG-- 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 kiteeSNIQKGSDV--WvdkiHK---LMDAIDDyIPTPVRDVEKTFLMAVEDV--FSITGRGtVAtGRIERGVIKVGDti 153
Cdd:COG2895   198 -----DNVVERSENmpW----YDgptLLEHLET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGD-- 263

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1018194321 154 EIVGLKETATTTITGLEMFQKTLDEGMAGDNIGILL-RGVqkkDIERGMVLAQPG-TITPHTQFEAEV 219
Cdd:COG2895   264 EVVVLPSGKTSTVKSIVTFDGDLEEAFAGQSVTLTLeDEI---DISRGDVIVAADaPPEVADQFEATL 328
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-113 4.07e-16

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: 73.48  E-value: 4.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQvGVPKIVVFLNKEDQVDDkELLELVQLEVTEVLDQYDF---PGSEIPFISGSALK 77
Cdd:cd00881    88 GALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRVGE-EDFDEVLREIKELLKLIGFtflKGKDVPIIPISALT 165

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1018194321  78 AlekiteesniqkgsdvwvDKIHKLMDAIDDYIPTP 113
Cdd:cd00881   166 G------------------EGIEELLDAIVEHLPPP 183
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 121-204 4.98e-16

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: 70.37  E-value: 4.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 121 FLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGlkETATTTITGLEMFQKTLDEGMAGDNIGILLRGVqkKDIERG 200
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP--KGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILTG 76


                  ....
gi 1018194321 201 MVLA 204
Cdd:cd01342    77 DTLT 80
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 210-237 2.13e-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: 69.08  E-value: 2.13e-15
                          10        20
                  ....*....|....*....|....*...
gi 1018194321 210 TPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGY 28
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-79 1.08e-12

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: 63.78  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVDDkELLELVQLEVTEVLDQYDFPGSEIPFIS---GSALKA 78
Cdd:cd04171    77 VLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADLVDE-DRLELVEEEILELLAGTFLADAPIFPVSsvtGEGIEE 155


                  .
gi 1018194321  79 L 79
Cdd:cd04171   156 L 156
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 208-237 5.60e-12

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: 60.36  E-value: 5.60e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1018194321 208 TITPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGY 30
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 2-114 8.36e-12

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: 62.51  E-value: 8.36e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADG-------PMPQTREHILLAKQVGVPKIVVFLNKEDQVD---DKELLELVQLEVTEVLDQYDFPGSEIPFI 71
Cdd:cd01883   104 AVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMDDVTvnwSQERYDEIKKKVSPFLKKVGYNPKDVPFI 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1018194321  72 SGSALKALekiteesNIQKGSDV--WVDKIHkLMDAIDDyIPTPV 114
Cdd:cd01883   184 PISGFTGD-------NLIEKSENmpWYKGPT-LLEALDS-LEPPE 219
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 2-77 2.59e-11

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: 60.18  E-value: 2.59e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPkIVVFLNKEDQVDDK-ELLELVQLEVTEVLDQYDFPGSEIPFISGSALK 77
Cdd:cd01887    76 AILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKIDKPYGTeADPERVKNELSELGLVGEEWGGDVSIVPISAKT 151
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 121-204 3.53e-11

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: 57.61  E-value: 3.53e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 121 FLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKETA--TTTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIE 198
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                  ....*.
gi 1018194321 199 RGMVLA 204
Cdd:cd03694    81 KGMVLV 86
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
 2-219 6.21e-10

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 58.79  E-value: 6.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVD-DKELLELVQLEVTEVLDQYDFpgSEIPFISGSALKAle 80
Cdd:PRK05506  131 AIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDyDQEVFDEIVADYRAFAAKLGL--HDVTFIPISALKG-- 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  81 kiteeSNIQKGSDV--WVDKIHkLMDAIDDYIPTPVRDvEKTFLMAVEDV---------FSitgrGTVATgrierGVIKV 149
Cdd:PRK05506  207 -----DNVVTRSARmpWYEGPS-LLEHLETVEIASDRN-LKDFRFPVQYVnrpnldfrgFA----GTVAS-----GVVRP 270

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1018194321 150 GDtiEIVGLKETATTTITGLEMFQKTLDEGMAGDNIGILLRgvQKKDIERGMVLAQPGTITPHT-QFEAEV 219
Cdd:PRK05506  271 GD--EVVVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTLA--DEIDISRGDMLARADNRPEVAdQFDATV 337
PRK10218 PRK10218
translational GTPase TypA;
3-187 1.74e-09

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 57.41  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   3 ILVVSAADGPMPQTREHILLAKQVGVPKIVVfLNKEDQ-------VDDKELLELVQLEVTEvlDQYDFPgseipFISGSA 75
Cdd:PRK10218   96 LLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRpgarpdwVVDQVFDLFVNLDATD--EQLDFP-----IVYASA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  76 LKALEKITEESniqkgsdvWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEI 155
Cdd:PRK10218  168 LNGIAGLDHED--------MAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTI 239

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1018194321 156 VGL-------KETATTTITGLEMFQKTLDEgmAGDNIGI 187
Cdd:PRK10218  240 IDSegktrnaKVGKVLGHLGLERIETDLAE--AGDIVAI 276
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 2-153 4.28e-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: 55.79  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPkIVVFLNKEDQVD---DKELLELVQLEVteVLDQYdfpGSEIPFISGSALKA 78
Cdd:COG0532    78 VILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKIDKPGanpDRVKQELAEHGL--VPEEW---GGDTIFVPVSAKTG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  79 LekiteesNIQkgsdvwvdkihKLMDAI------DDYIPTPVRDVEKTFLMAVEDVfsitGRGTVATGRIERGVIKVGDT 152
Cdd:COG0532   152 E-------GID-----------ELLEMIllqaevLELKANPDRPARGTVIEAKLDK----GRGPVATVLVQNGTLKVGDI 209


                  .
gi 1018194321 153 I 153
Cdd:COG0532   210 V 210
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 210-237 5.91e-09

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: 51.85  E-value: 5.91e-09
                          10        20
                  ....*....|....*....|....*...
gi 1018194321 210 TPHTQFEAEVYILTKEEGGRHTPFFSGY 237
Cdd:cd03706     1 KMHNHFEAQVYLLSKEEGGRHKPFTSGF 28
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-155 6.93e-09

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 55.40  E-value: 6.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADG-PMPQTREHILLAKQVGVPKIVVFLNKEDQVDDkellelvqlevTEVLDQYDfpgsEI-PFISGSalka 78
Cdd:PTZ00327  143 AALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKE-----------AQAQDQYE----EIrNFVKGT---- 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  79 lekITEESNIQKGSDVWVDKIHKLMDAIDDYIPTPVRDVEKTFLMAV----------EDVFSItgRGTVATGRIERGVIK 148
Cdd:PTZ00327  204 ---IADNAPIIPISAQLKYNIDVVLEYICTQIPIPKRDLTSPPRMIVirsfdvnkpgEDIENL--KGGVAGGSILQGVLK 278


                  ....*..
gi 1018194321 149 VGDTIEI 155
Cdd:PTZ00327  279 VGDEIEI 285
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 121-203 1.05e-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: 50.97  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 121 FLMAVEDVFSITGRGTVATGRIERGVIKVGDTIEIVGLKETAttTITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERG 200
Cdd:cd16267     2 FRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNETA--TVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRVG 79


                  ...
gi 1018194321 201 MVL 203
Cdd:cd16267    80 SIL 82
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 124-204 1.90e-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: 49.99  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 124 AVEDVFSITGRgTVATGRIERGVIKVGDtiEIVGLKETATttITGLEMFQKTLDEGMAGDNIGILLRGVQKkdIERGMVL 203
Cdd:cd16265     4 RVEKVFKILGR-QVLTGEVESGVIYVGY--KVKGDKGVAL--IRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVL 76


                  .
gi 1018194321 204 A 204
Cdd:cd16265    77 E 77
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 1-113 3.69e-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: 51.83  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADGPMPQTREHILLAKQVGVPKIVVfLNKEDQVDD--KELLELVQ---LEVTEVLDQYDFPgseIPFISGSA 75
Cdd:cd01891    91 GVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKIDRPDArpEEVVDEVFdlfLELNATDEQLDFP---IVYASAKN 166

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1018194321  76 LKALEKITEESniqkgsdvwvDKIHKLMDAIDDYIPTP 113
Cdd:cd01891   167 GWASLNLDDPS----------EDLDPLFETIIEHVPAP 194
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 134-203 8.46e-08

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: 48.25  E-value: 8.46e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 134 RGTVATGRIERGVIKVGDTIEIVGLKETATttITGLEMFQKTLDEGMAGDNIGILLRGVQKKDIERGMVL 203
Cdd:cd04089    13 MGTVVMGKVESGTIRKGQKLVLMPNKTKVE--VTGIYIDEEEVDSAKPGENVKLKLKGVEEEDISPGFVL 80
infB CHL00189
translation initiation factor 2; Provisional
 2-155 1.93e-07

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 51.37  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPkIVVFLNKEDQVDDKelLELVQLEvtevLDQYDFP----GSEIPFISGSALK 77
Cdd:CHL00189  322 AILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKIDKANAN--TERIKQQ----LAKYNLIpekwGGDTPMIPISASQ 394

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1018194321  78 alekiteESNIQKgsdvWVDKIhKLMDAIDDYIPTPVRDVEKTFLMAVEDVFsitgRGTVATGRIERGVIKVGDTIEI 155
Cdd:CHL00189  395 -------GTNIDK----LLETI-LLLAEIEDLKADPTQLAQGIILEAHLDKT----KGPVATILVQNGTLHIGDIIVI 456
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 2-77 4.39e-07

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: 48.72  E-value: 4.39e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVD-DKELLELVQLEVTEVLDQYDFPgsEIPFISGSALK 77
Cdd:cd04166   105 AILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDyDEEVFEEIKADYLAFAASLGIE--DITFIPISALE 179
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 2-219 5.71e-07

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 49.53  E-value: 5.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVFLNKEDQVD-DKELLELVQLEVTEVLDQydFPGS-EIPFISGSALKAl 79
Cdd:PRK05124  134 AILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDLVDySEEVFERIREDYLTFAEQ--LPGNlDIRFVPLSALEG- 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321  80 ekiteeSNIQKGSDV--WVDKIhKLMDAIDDYipTPVRDVEKT-FLMAVEDV---------FSitgrGTVATgrierGVI 147
Cdd:PRK05124  211 ------DNVVSQSESmpWYSGP-TLLEVLETV--DIQRVVDAQpFRFPVQYVnrpnldfrgYA----GTLAS-----GVV 272

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1018194321 148 KVGDtiEIVGLKETATTTITGLEMFQKTLDEGMAGDNIGILLRgvQKKDIERGMVLAQPG-TITPHTQFEAEV 219
Cdd:PRK05124  273 KVGD--RVKVLPSGKESNVARIVTFDGDLEEAFAGEAITLVLE--DEIDISRGDLLVAADeALQAVQHASADV 341
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 1-115 8.40e-07

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: 48.03  E-value: 8.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   1 GAILVVSAADG-PMPQTREHILLAKQVGVPKIVVFLNKEDQVDDKELLElvqlevtevldQYDFPGSeipFISGS-ALKA 78
Cdd:cd01888   103 GALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALE-----------NYEQIKE---FVKGTiAENA 168

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1018194321  79 leKITEESNIQKGSdvwvdkIHKLMDAIDDYIPTPVR 115
Cdd:cd01888   169 --PIIPISAQLKYN------IDVLCEYIVKKIPTPPR 197
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 121-204 2.07e-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: 41.72  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321 121 FLMAVEDVFSiTGRGTVATGRIERGVIKVGDTIEIVGLKETATTTITGLEMFQKTlDEGMAGDNIGILLRGVQKKDIERG 200
Cdd:cd03698     2 FRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEET-DWAIAGDTVTLRLRGIEVEDIQPG 79


                  ....
gi 1018194321 201 MVLA 204
Cdd:cd03698    80 DILS 83
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 140-204 8.77e-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: 39.86  E-value: 8.77e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1018194321 140 GRIERGVIKVGDTIEIvgLKETATTTITGLEMFQKTLDEGMAGDNIGILL-RGVqkkDIERGMVLA 204
Cdd:cd03695    20 GTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTLeDEI---DVSRGDLIV 80
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 2-45 2.75e-04

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: 40.43  E-value: 2.75e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1018194321   2 AILVVSAADGPMPQTREHILLAKQVGVPKIVVfLNKEDQVDDKE 45
Cdd:cd01889    95 MLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKIDLIPEEE 137
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 135-187 6.63e-04

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: 37.94  E-value: 6.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1018194321 135 GTVATGRIERGVIKVGDTIEIVGLKETATT-TITGLEMFQKT----LDEGMAGDNIGI 187
Cdd:cd03691    15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKgRVTKLFGFEGLerveVEEAEAGDIVAI 72
Era cd04163
E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is ...
 3-82 2.39e-03

E. coli Ras-like protein (Era) is a multifunctional GTPase; Era (E. coli Ras-like protein) is a multifunctional GTPase found in all bacteria except some eubacteria. It binds to the 16S ribosomal RNA (rRNA) of the 30S subunit and appears to play a role in the assembly of the 30S subunit, possibly by chaperoning the 16S rRNA. It also contacts several assembly elements of the 30S subunit. Era couples cell growth with cytokinesis and plays a role in cell division and energy metabolism. Homologs have also been found in eukaryotes. Era contains two domains: the N-terminal GTPase domain and a C-terminal domain KH domain that is critical for RNA binding. Both domains are important for Era function. Era is functionally able to compensate for deletion of RbfA, a cold-shock adaptation protein that is required for efficient processing of the 16S rRNA.


Pssm-ID: 206726 [Multi-domain]  Cd Length: 168  Bit Score: 37.44  E-value: 2.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1018194321   3 ILVVSAADGPMPQTREHILLAKQVGVPKIVVfLNKEDQVDDKE-LLELVQlevtEVLDQYDFpgSEIPFIS---GSALKA 78
Cdd:cd04163    87 LFVVDASEWIGEGDEFILELLKKSKTPVILV-LNKIDLVKDKEdLLPLLE----KLKELHPF--AEIFPISalkGENVDE 159


                  ....
gi 1018194321  79 LEKI 82
Cdd:cd04163   160 LLEY 163
era PRK00089
GTPase Era; Reviewed
 3-77 4.46e-03

GTPase Era; Reviewed


Pssm-ID: 234624 [Multi-domain]  Cd Length: 292  Bit Score: 37.33  E-value: 4.46e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1018194321   3 ILVVSAADGPMPQTREHILLAKQVGVPKIVVfLNKEDQVDDKE-LLELVQlevtEVLDQYDFpgSEIPFIsgSALK 77
Cdd:PRK00089   89 LFVVDADEKIGPGDEFILEKLKKVKTPVILV-LNKIDLVKDKEeLLPLLE----ELSELMDF--AEIVPI--SALK 155
Era COG1159
GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];
3-77 4.58e-03

GTPase Era, involved in 16S rRNA processing [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440773 [Multi-domain]  Cd Length: 290  Bit Score: 37.28  E-value: 4.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1018194321   3 ILVVSAADGPMPQTREHILLAKQVGVPKIVVfLNKEDQVDDKELLELVQlevtEVLDQYDFpgSEIPFIsgSALK 77
Cdd:COG1159    87 LFVVDATEKIGEGDEFILELLKKLKTPVILV-INKIDLVKKEELLPLLA----EYSELLDF--AEIVPI--SALK 152
eIF2_gamma_II cd03688
Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily ...
 134-187 6.30e-03

Domain II of the gamma subunit of eukaryotic translation initiation factor 2; This subfamily represents domain II of the gamma subunit of eukaryotic translation initiation factor 2 (eIF2-gamma) found in eukaryota and archaea. eIF2 is a G protein that delivers the methionyl initiator tRNA to the small ribosomal subunit and releases it upon GTP hydrolysis after the recognition of the initiation codon. eIF2 is composed of three subunits, alpha, beta and gamma. Subunit gamma shows strongest conservation, and it confers both tRNA binding and GTP/GDP binding.


Pssm-ID: 293889 [Multi-domain]  Cd Length: 113  Bit Score: 35.62  E-value: 6.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1018194321 134 RGTVATGRIERGVIKVGDTIEIV-GLKETA---------TTTITGLEMFQKTLDEGMAGDNIGI 187
Cdd:cd03688    27 KGGVIGGSLIQGVLKVGDEIEIRpGIVVKKggkttcrpiFTKIVSLFAEGNDLEEAVPGGLIGV 90
 
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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