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Conserved domains on  [gi|118480969|gb|ABK92438|]
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elongation factor Tu, partial [Mycobacteroides immunogenum]

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
 1-216 9.84e-137

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 388.39  E-value: 9.84e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:PRK00049  99 MDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LEG--DAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTT 158
Cdd:PRK00049 179 LEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRD-TQKTT 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969 159 VTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:PRK00049 258 VTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLS 315
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-216 9.84e-137

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 388.39  E-value: 9.84e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:PRK00049  99 MDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LEG--DAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTT 158
Cdd:PRK00049 179 LEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRD-TQKTT 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969 159 VTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:PRK00049 258 VTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLS 315
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-216 1.49e-134

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: 382.96  E-value: 1.49e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:COG0050   99 MDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LEGD--AEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTT 158
Cdd:COG0050  179 LEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRD-TQKTV 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969 159 VTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:COG0050  258 VTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLS 315
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-216 2.37e-112

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: 326.73  E-value: 2.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969    1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:TIGR00485  99 MDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKA 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   81 LEGDAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTTVT 160
Cdd:TIGR00485 179 LEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKD-TRKTTVT 257

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 118480969  161 GVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:TIGR00485 258 GVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLS 313
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-105 3.45e-49

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: 158.90  E-value: 3.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:cd01884   89 MDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKA 168

                         90       100
                 ....*....|....*....|....*..
gi 118480969  81 LEGD--AEWGKTVADLMDAVDESIPDP 105
Cdd:cd01884  169 LEGDdpNKWVDKILELLDALDSYIPTP 195
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-104 1.69e-27

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: 102.99  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969    1 MDGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKa 80
Cdd:pfam00009  93 ADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALK- 170

                          90       100
                  ....*....|....*....|....
gi 118480969   81 legdaewGKTVADLMDAVDESIPD 104
Cdd:pfam00009 171 -------GEGVQTLLDALDEYLPS 187
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-216 9.84e-137

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 388.39  E-value: 9.84e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:PRK00049  99 MDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LEG--DAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTT 158
Cdd:PRK00049 179 LEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIRD-TQKTT 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969 159 VTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:PRK00049 258 VTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLS 315
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-216 1.49e-134

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: 382.96  E-value: 1.49e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:COG0050   99 MDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LEGD--AEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTT 158
Cdd:COG0050  179 LEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRD-TQKTV 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969 159 VTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:COG0050  258 VTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLS 315
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-216 2.79e-128

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 366.96  E-value: 2.79e-128
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:PRK12736  99 MDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LEGDAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTTVT 160
Cdd:PRK12736 179 LEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKE-TQKTVVT 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 118480969 161 GVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:PRK12736 258 GVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILT 313
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-216 5.74e-127

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 363.77  E-value: 5.74e-127
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:PRK12735  99 MDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LEGD--AEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTT 158
Cdd:PRK12735 179 LEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKE-TQKTT 257

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969 159 VTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:PRK12735 258 VTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLS 315
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-216 2.37e-112

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: 326.73  E-value: 2.37e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969    1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:TIGR00485  99 MDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKA 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   81 LEGDAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtTTKTTVT 160
Cdd:TIGR00485 179 LEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLKD-TRKTTVT 257

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 118480969  161 GVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:TIGR00485 258 GVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLS 313
tufA CHL00071
elongation factor Tu
 1-216 5.39e-107

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 313.43  E-value: 5.39e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:CHL00071  99 MDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LE----------GDAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGI 150
Cdd:CHL00071 179 LEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGL 258

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118480969 151 KDtTTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:CHL00071 259 RE-TKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILT 323
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-216 5.77e-103

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 304.44  E-value: 5.77e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:PLN03127 148 MDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSA 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LEG-DAEWGK-TVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDTTTK-T 157
Cdd:PLN03127 228 LQGtNDEIGKnAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPGGPLkT 307

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 118480969 158 TVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:PLN03127 308 TVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLT 366
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-215 3.51e-87

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 265.33  E-value: 3.51e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:PLN03126 168 MDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLA 247

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 LE----------GDAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGI 150
Cdd:PLN03126 248 LEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGL 327

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118480969 151 KDtTTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYIL 215
Cdd:PLN03126 328 RE-TRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVL 391
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-105 3.45e-49

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: 158.90  E-value: 3.45e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKA 80
Cdd:cd01884   89 MDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKA 168

                         90       100
                 ....*....|....*....|....*..
gi 118480969  81 LEGD--AEWGKTVADLMDAVDESIPDP 105
Cdd:cd01884  169 LEGDdpNKWVDKILELLDALDSYIPTP 195
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 113-200 1.57e-44

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: 143.43  E-value: 1.57e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969 113 FLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDTTTKTTVtGVEMFRKLLDQGQAGDNVGLLVRGVKREDVER 192
Cdd:cd03697    1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVT-GIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79


                 ....*...
gi 118480969 193 GQVVVKPG 200
Cdd:cd03697   80 GMVLAKPG 87
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-215 3.15e-42

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: 147.39  E-value: 3.15e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVD-DEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKa 80
Cdd:COG5256  110 DAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK- 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 leGD--------AEW--GKTVADLMDAVDEsipdPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVgi 150
Cdd:COG5256  189 --GDnvvkksdnMPWynGPTLLEALDNLKE----PEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFM-- 260

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969 151 kDTTTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPgtTTPHT---EFEGSVYIL 215
Cdd:COG5256  261 -PAGVVGEVKSIEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHP--DNPPTvaeEFTAQIVVL 325
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-215 1.57e-38

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 137.36  E-value: 1.57e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATD--GPMPQTREHVLLARQVGVPYILVALNKSDMVD-DEELLELVEMEVRELLSSQDFDGDNAPVVRVSAL 78
Cdd:PRK12317 109 DAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAF 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  79 kalEGD--------AEW--GKTvadLMDAVDeSIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDV--- 145
Cdd:PRK12317 189 ---EGDnvvkksenMPWynGPT---LLEALD-NLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVvfm 261

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118480969 146 --EIVG-IKDtttkttvtgVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPgtTTPHT---EFEGSVYIL 215
Cdd:PRK12317 262 paGVVGeVKS---------IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGHP--DNPPTvaeEFTAQIVVL 326
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 1-216 7.60e-34

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: 127.34  E-value: 7.60e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMvDDEELLELVEMEVRELLSSQDFdgDNAPVVRVSALKa 80
Cdd:COG3276   75 IDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGTFL--EDAPIVPVSAVT- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 legdaewGKTVADLMDAVDESIPD-PVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVG------IKdt 153
Cdd:COG3276  151 -------GEGIDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPsgkpvrVR-- 221

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118480969 154 ttkttvtGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVVKPGTTTPHTEFEGSVYILS 216
Cdd:COG3276  222 -------GIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP 277
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-104 1.69e-27

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: 102.99  E-value: 1.69e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969    1 MDGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKSDMVDDEELLELVEMEVRELLSSQDFDGDNAPVVRVSALKa 80
Cdd:pfam00009  93 ADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALK- 170

                          90       100
                  ....*....|....*....|....
gi 118480969   81 legdaewGKTVADLMDAVDESIPD 104
Cdd:pfam00009 171 -------GEGVQTLLDALDEYLPS 187
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 2-203 5.70e-27

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: 5.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969    2 DGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDmVDDEELLELVEMEVRELLSSQDFDgDNAPVVRVSAlKAL 81
Cdd:TIGR00475  75 DAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIFL-KNAKIFKTSA-KTG 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   82 EGDAEWGKTVADLMDAVDESipdpvrETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIkdtttkttvtG 161
Cdd:TIGR00475 152 QGIGELKKELKNLLESLDIK------RIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI----------N 215

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 118480969  162 VEM-FRKLLDQGQ------AGDNVGLLVRGVKREDVERGQVVVKPGTTT 203
Cdd:TIGR00475 216 HEVrVKAIQAQNQdveiayAGQRIALNLMDVEPESLKRGLLILTPEDPK 264
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-196 3.71e-26

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 104.44  E-value: 3.71e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMP-------QTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVREL---LSSQDFDGDNAP 71
Cdd:PTZ00141 110 DVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCINKMDDKTVNYSQERYDEIKKEVsayLKKVGYNPEKVP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  72 VVRVSALkalEGD--------AEW--GKTVADLMDAVDEsipdPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINV 141
Cdd:PTZ00141 190 FIPISGW---QGDnmieksdnMPWykGPTLLEALDTLEP----PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKP 262

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 118480969 142 NedvEIVGIKDTTTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVV 196
Cdd:PTZ00141 263 G---MVVTFAPSGVTTEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDIKRGYVA 314
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 2-195 2.15e-18

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 82.83  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMP-------QTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVREL---LSSQDFDGDNAP 71
Cdd:PLN00043 110 DCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVssyLKKVGYNPDKIP 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  72 VVRVSALkalEGD--------AEWGKTvADLMDAVDEsIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNe 143
Cdd:PLN00043 190 FVPISGF---EGDnmierstnLDWYKG-PTLLEALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG- 263

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 118480969 144 dvEIVGIKDTTTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQV 195
Cdd:PLN00043 264 --MVVTFGPTGLTTEVKSVEMHHESLQEALPGDNVGFNVKNVAVKDLKRGYV 313
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 109-201 1.01e-17

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: 74.92  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969 109 TEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVgikDTTTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKRE 188
Cdd:cd03693    1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFA---PAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77

                         90
                 ....*....|...
gi 118480969 189 DVERGQVVVKPGT 201
Cdd:cd03693   78 DIKRGDVAGDSKN 90
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-151 1.18e-17

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 80.28  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDG-PMPQTREHVLLARQVGVPYILVALNKSDMvddeellelveMEVRELLSS----QDF-DG---DNAP 71
Cdd:PRK04000 109 MDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL-----------VSKERALENyeqiKEFvKGtvaENAP 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  72 VVRVSALKALEGDAewgktvadLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGT--------VVTGRVERGVINVNE 143
Cdd:PRK04000 178 IIPVSALHKVNIDA--------LIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGD 249


                 ....*....
gi 118480969 144 DVEIV-GIK 151
Cdd:PRK04000 250 EIEIRpGIK 258
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 113-198 5.26e-17

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


Pssm-ID: 293897 [Multi-domain]  Cd Length: 83  Bit Score: 72.56  E-value: 5.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969 113 FLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKdttTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVER 192
Cdd:cd03696    1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLG---KEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77


                 ....*.
gi 118480969 193 GQVVVK 198
Cdd:cd03696   78 GFVLSE 83
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 1-105 2.18e-14

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: 68.48  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQvGVPYILVALNKSDMVDDEELLELVEMEVREL--LSSQDFDGDNAPVVRVSAL 78
Cdd:cd00881   86 ADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDRVGEEDFDEVLREIKELLklIGFTFLKGKDVPIIPISAL 164

                         90       100
                 ....*....|....*....|....*..
gi 118480969  79 KALEGDaewgktvaDLMDAVDESIPDP 105
Cdd:cd00881  165 TGEGIE--------ELLDAIVEHLPPP 183
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 1-193 5.28e-14

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 70.08  E-value: 5.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDmVDDEELLELVEMEVRELLSSQDFDGdnAPVVRVSALKa 80
Cdd:PRK10512  75 IDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKAD-RVDEARIAEVRRQVKAVLREYGFAE--AKLFVTAATE- 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  81 legdaewGKTVADLMDAVdESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKdttTKTTVT 160
Cdd:PRK10512 151 -------GRGIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVN---KPMRVR 219

                        170       180       190
                 ....*....|....*....|....*....|....
gi 118480969 161 GVEMFRKLLDQGQAGDNVGLLVRG-VKREDVERG 193
Cdd:PRK10512 220 GLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 127-197 1.06e-13

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: 63.82  E-value: 1.06e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118480969  127 GTVVTGRVERGVINVNEDVEIVGIKDTTTKTTV--TGVEMFRKLLDQGQAGDNVGLLVRGVKREDVERGQVVV 197
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKKIVTrvTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
 1-78 8.85e-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: 61.08  E-value: 8.85e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMvDDEELLELVEMEVRELLSSQDFdgDNAPVVRVSAL 78
Cdd:cd04171   74 IDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADL-VDEDRLELVEEEILELLAGTFL--ADAPIFPVSSV 148
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
 2-176 2.37e-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: 62.32  E-value: 2.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969    2 DGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKSDMVDDEELLELVEMEvrELLSSQDFDGD--NAPVVRVSAL- 78
Cdd:TIGR01394  89 DGVLLLVDASEGPMPQTRFVLKKALELGLKPIVV-INKIDRPSARPDEVVDEVF--DLFAELGADDEqlDFPIVYASGRa 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   79 -KALEGDAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVE--DVFTITGRgtVVTGRVERGVINVNEDVEIVGIKDTTT 155
Cdd:TIGR01394 166 gWASLDLDDPSDNMAPLFDAIVRHVPAPKGDLDEPLQMLVTnlDYDEYLGR--IAIGRVHRGTVKKGQQVALMKRDGTIE 243

                         170       180
                  ....*....|....*....|....*
gi 118480969  156 KTTVTGVEMFRKL----LDQGQAGD 176
Cdd:TIGR01394 244 NGRISKLLGFEGLerveIDEAGAGD 268
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 113-197 1.48e-10

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: 55.35  E-value: 1.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969 113 FLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIkdtTTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKreDVER 192
Cdd:cd01342    1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPK---GITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75


                 ....*
gi 118480969 193 GQVVV 197
Cdd:cd01342   76 GDTLT 80
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
 2-176 1.74e-09

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 56.57  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMPQTReHVL---LARqvGVPYILVaLNKSDmvddeellelvemevR-------------ELL----- 60
Cdd:COG1217   94 DGVLLLVDAFEGPMPQTR-FVLkkaLEL--GLKPIVV-INKID---------------RpdarpdevvdevfDLFielga 154

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969  61 -SSQ-DFdgdnaPVVRVSALK---ALEGDAEwGKTVADLMDAVDESIPDPVRETEKPFLMpveDVFTI-----TGRgtVV 130
Cdd:COG1217  155 tDEQlDF-----PVVYASARNgwaSLDLDDP-GEDLTPLFDTILEHVPAPEVDPDGPLQM---LVTNLdysdyVGR--IA 223

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 118480969 131 TGRVERGVINVNEDVEIVGIKDTTTKTTVTGVEMFRKL----LDQGQAGD 176
Cdd:COG1217  224 IGRIFRGTIKKGQQVALIKRDGKVEKGKITKLFGFEGLerveVEEAEAGD 273
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
 2-100 1.80e-09

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: 54.79  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKSDmvdDEELLELVEMEVRELLSSQDFDGDN----APVVRVSA 77
Cdd:cd01887   74 DIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEwggdVSIVPISA 149

                         90       100
                 ....*....|....*....|...
gi 118480969  78 LKalegdaewGKTVADLMDAVDE 100
Cdd:cd01887  150 KT--------GEGIDDLLEAILL 164
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 1-147 3.54e-09

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 55.78  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDG-PMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLELVEMEVRELLSSQdfdGDNAPVVRVSALK 79
Cdd:PTZ00327 141 MDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKIDLVKEAQAQDQYEEIRNFVKGTI---ADNAPIIPISAQL 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969  80 ALEGDAewgktvadLMDAVDESIPDPVRETEKPFLM----------PVEDVFTItgRGTVVTGRVERGVINVNEDVEI 147
Cdd:PTZ00327 218 KYNIDV--------VLEYICTQIPIPKRDLTSPPRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 113-197 4.14e-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: 51.84  E-value: 4.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969 113 FLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDTT-TKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVE 191
Cdd:cd03694    1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLGPDADGKfRPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLR 80


                 ....*.
gi 118480969 192 RGQVVV 197
Cdd:cd03694   81 KGMVLV 86
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
 2-41 6.76e-09

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: 54.03  E-value: 6.76e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 118480969   2 DGAILVVAATDG-------PMPQTREHVLLARQVGVPYILVALNKSD 41
Cdd:cd01883  102 DVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
 2-41 8.35e-08

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: 51.55  E-value: 8.35e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMPQTREHVLLARQVGVPyILVALNKSD 41
Cdd:COG0532   76 DIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
 1-107 1.42e-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: 49.96  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDG-PMPQTREHVLLARQVGVPYILVALNKSDMVDDEELLElvemevrELLSSQDF-DG---DNAPVVRV 75
Cdd:cd01888  101 MDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEEQALE-------NYEQIKEFvKGtiaENAPIIPI 173

                         90       100       110
                 ....*....|....*....|....*....|..
gi 118480969  76 SALKALEGDAewgktvadLMDAVDESIPDPVR 107
Cdd:cd01888  174 SAQLKYNIDV--------LCEYIVKKIPTPPR 197
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 117-195 3.51e-06

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: 43.44  E-value: 3.51e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118480969 117 VEDVFTITGRgTVVTGRVERGVINVNEDVeivgiKDTTTKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKRedVERGQV 195
Cdd:cd16265    5 VEKVFKILGR-QVLTGEVESGVIYVGYKV-----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDV 75
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
 2-99 4.07e-06

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: 45.64  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMPQTREHVLLARQVGVPYILVALNKSDMVDDEELL-ELVEMEVRELLSSQDFdgdnaPVVRVSALKA 80
Cdd:cd04166  103 DLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDLVDYDEEVfEEIKADYLAFAASLGI-----EDITFIPISA 177

                         90       100
                 ....*....|....*....|....*....
gi 118480969  81 LEGD--------AEW--GKTVADLMDAVD 99
Cdd:cd04166  178 LEGDnvvsrsenMPWykGPTLLEHLETVE 206
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 112-196 6.12e-06

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: 42.89  E-value: 6.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969 112 PFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIVGIKDtttKTTVTGVEMFRKLLDQGQAGDNVGLLVRGVKREDVE 191
Cdd:cd16267    1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNE---TATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77


                 ....*
gi 118480969 192 RGQVV 196
Cdd:cd16267   78 VGSIL 82
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 112-195 2.31e-05

Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is mediated by two interacting release factors, eRF1 and eRF3, which act as class I and II factors, respectively. eRF1 functions as an omnipotent release factor, decoding all three stop codons and triggering the release of the nascent peptide catalyzed by the ribosome. eRF3 is a GTPase, which enhances termination efficiency by stimulating eRF1 activity in a GTP-dependent manner. Sequence comparison of class II release factors with elongation factors shows that eRF3 is more similar to eEF-1alpha whereas prokaryote RF3 is more similar to EF-G, implying that their precise function may differ. Only eukaryote RF3s are found in this group. Saccharomyces cerevisiae eRF3 (Sup35p) is a translation termination factor which is divided into three regions N, M and a C-terminal eEF1a-like region essential for translation termination. Sup35NM is a non-pathogenic prion-like protein with the property of aggregating into polymer-like fibrils.


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 41.32  E-value: 2.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969 112 PFLMPVEDVFTitGRGTVVTGRVERGVINVNE---------DVEIVGIkdtttktTVTGVEMfrkllDQGQAGDNVGLLV 182
Cdd:cd04089    1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGI-------YIDEEEV-----DSAKPGENVKLKL 66

                         90
                 ....*....|...
gi 118480969 183 RGVKREDVERGQV 195
Cdd:cd04089   67 KGVEEEDISPGFV 79
PRK10218 PRK10218
translational GTPase TypA;
1-148 2.59e-05

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 44.31  E-value: 2.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKSDMVDDEELLELVEMEvrELLSSQDFDGD--NAPVVRVSAL 78
Cdd:PRK10218  92 VDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDFPIVYASAL 168

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118480969  79 KALEG--DAEWGKTVADLMDAVDESIPDPVRETEKPFLMPVEDVFTITGRGTVVTGRVERGVINVNEDVEIV 148
Cdd:PRK10218 169 NGIAGldHEDMAEDMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 112-195 3.79e-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: 40.95  E-value: 3.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969 112 PFLMPVEDVFTiTGRGTVVTGRVERGVINVNEDVEIVGIKDTTTKT---TVTGVEMfrkllDQGQAGDNVGLLVRGVKRE 188
Cdd:cd03698    1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKniiRNSDEET-----DWAIAGDTVTLRLRGIEVE 74


                 ....*..
gi 118480969 189 DVERGQV 195
Cdd:cd03698   75 DIQPGDI 81
infB CHL00189
translation initiation factor 2; Provisional
 2-79 6.63e-05

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 43.28  E-value: 6.63e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118480969   2 DGAILVVAATDGPMPQTREHVLLARQVGVPYIlVALNKSDMVDDEELLELVEMEVRELLsSQDFDGDnAPVVRVSALK 79
Cdd:CHL00189 320 DIAILIIAADDGVKPQTIEAINYIQAANVPII-VAINKIDKANANTERIKQQLAKYNLI-PEKWGGD-TPMIPISASQ 394
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
 2-41 2.31e-04

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: 40.66  E-value: 2.31e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKSD 41
Cdd:cd01891   90 DGVLLLVDASEGPMPQTRFVLKKALEAGLKPIVV-INKID 128
PRK04004 PRK04004
translation initiation factor IF-2; Validated
 2-41 2.38e-03

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 38.24  E-value: 2.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMPQTREHVLLARQVGVPYIlVALNKSD 41
Cdd:PRK04004  96 DIAILVVDINEGFQPQTIEAINILKRRKTPFV-VAANKID 134
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
 1-41 8.19e-03

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: 36.06  E-value: 8.19e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 118480969   1 MDGAILVVAATDGPMPQTREHVLLARQVGVPYILVaLNKSD 41
Cdd:cd04168   88 LDGAILVISAVEGVQAQTRILFRLLRKLNIPTIIF-VNKID 127
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 2-79 9.71e-03

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 35.51  E-value: 9.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118480969   2 DGAILVVAATDGPMPQTREHVLLARQV--GVPYILVaLNKSDMVDDEELLELVEMEVRELLSsqdfdgdNAPVVRVSALK 79
Cdd:cd00882   77 DLILLVVDSTDRESEEDAKLLILRRLRkeGIPIILV-GNKIDLLEEREVEELLRLEELAKIL-------GVPVFEVSAKT 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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