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Conserved domains on  [gi|2173160141|ref|WP_233445172|]
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GTP-binding protein, partial [Klebsiella variicola]

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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
PRK00049 super family cl35051
elongation factor Tu; Reviewed
 1-112 6.39e-68

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 208.89  E-value: 6.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEG--DAEWEAKIIELAGHLDT 78
Cdd:PRK00049  121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDS 200

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2173160141  79 YIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PRK00049  201 YIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRV 234
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-112 6.39e-68

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 208.89  E-value: 6.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEG--DAEWEAKIIELAGHLDT 78
Cdd:PRK00049  121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDS 200

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2173160141  79 YIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PRK00049  201 YIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRV 234
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-112 1.09e-65

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: 203.07  E-value: 1.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGHLDT 78
Cdd:COG0050   121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDS 200

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2173160141  79 YIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:COG0050   201 YIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRV 234
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-112 4.31e-63

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: 196.54  E-value: 4.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKIIELAGHLDTYI 80
Cdd:TIGR00485 121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYI 200

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2173160141  81 PEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:TIGR00485 201 PTPEREIDKPFLLPIEDVFSITGRGTVVTGRV 232
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-83 9.52e-36

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: 120.38  E-value: 9.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGHLDT 78
Cdd:cd01884   111 LLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALEGDdpNKWVDKILELLDALDS 190


                  ....*
gi 2173160141  79 YIPEP 83
Cdd:cd01884   191 YIPTP 195
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-81 1.23e-10

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: 55.22  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALegdaeweaKIIELAGHLDTYI 80
Cdd:pfam00009 115 RLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKGE--------GVQTLLDALDEYL 185


                  .
gi 2173160141  81 P 81
Cdd:pfam00009 186 P 186
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-112 6.39e-68

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 208.89  E-value: 6.39e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEG--DAEWEAKIIELAGHLDT 78
Cdd:PRK00049  121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDS 200

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2173160141  79 YIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PRK00049  201 YIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRV 234
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-112 2.92e-66

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 204.69  E-value: 2.92e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGHLDT 78
Cdd:PRK12735  121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGDddEEWEAKILELMDAVDS 200

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2173160141  79 YIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PRK12735  201 YIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRV 234
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-112 1.09e-65

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: 203.07  E-value: 1.09e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGHLDT 78
Cdd:COG0050   121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDS 200

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2173160141  79 YIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:COG0050   201 YIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRV 234
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-112 4.87e-64

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 198.63  E-value: 4.87e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKIIELAGHLDTYI 80
Cdd:PRK12736  121 LLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYI 200

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2173160141  81 PEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PRK12736  201 PTPERDTDKPFLMPVEDVFTITGRGTVVTGRV 232
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-112 4.31e-63

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: 196.54  E-value: 4.31e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEAKIIELAGHLDTYI 80
Cdd:TIGR00485 121 LLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYI 200

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2173160141  81 PEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:TIGR00485 201 PTPEREIDKPFLLPIEDVFSITGRGTVVTGRV 232
tufA CHL00071
elongation factor Tu
 1-112 2.79e-49

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 160.89  E-value: 2.79e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE----------GDAEWEAKII 70
Cdd:CHL00071  121 LLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIY 200

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2173160141  71 ELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:CHL00071  201 NLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRI 242
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-112 8.41e-48

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 158.06  E-value: 8.41e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEG--DAEWEAKIIELAGHLDT 78
Cdd:PLN03127  170 LLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDE 249

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2173160141  79 YIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PLN03127  250 YIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRV 283
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-112 5.25e-40

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 138.21  E-value: 5.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALE----------GDAEWEAKII 70
Cdd:PLN03126  190 LLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIY 269

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2173160141  71 ELAGHLDTYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PLN03126  270 ELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRV 311
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-83 9.52e-36

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: 120.38  E-value: 9.52e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGHLDT 78
Cdd:cd01884   111 LLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALEGDdpNKWVDKILELLDALDS 190


                  ....*
gi 2173160141  79 YIPEP 83
Cdd:cd01884   191 YIPTP 195
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-112 2.26e-13

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 64.56  E-value: 2.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVD-DEELLELVEMEVRELLSQYDFPGDDTPIVRGSALkalEGDaeweaKIIELAGHLDTY 79
Cdd:PRK12317  132 FLARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAF---EGD-----NVVKKSENMPWY 203

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2173160141  80 -----------IPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PRK12317  204 ngptllealdnLKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRV 247
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-112 3.76e-13

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: 63.80  E-value: 3.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVD-DEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKaleGDaeweaKIIELAGHLDTY 79
Cdd:COG5256   131 FLARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GD-----NVVKKSDNMPWY 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2173160141  80 -----------IPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:COG5256   203 ngptllealdnLKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRV 246
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-81 1.23e-10

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: 55.22  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALegdaeweaKIIELAGHLDTYI 80
Cdd:pfam00009 115 RLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKGE--------GVQTLLDALDEYL 185


                  .
gi 2173160141  81 P 81
Cdd:pfam00009 186 P 186
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 91-112 5.81e-10

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: 51.37  E-value: 5.81e-10
                          10        20
                  ....*....|....*....|..
gi 2173160141  91 FLLPIEDVFSISGRGTVVTGRV 112
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRI 22
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 7-110 2.69e-08

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: 49.91  E-value: 2.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   7 GVPYIIVFLNKCDMVDDEELLELVEMEvRELLSQYDFPgdDTPIVRGSAlKALEGdaeweakIIELAGHLDTYIPE-PER 85
Cdd:COG3276   103 GIKRGIVVLTKADLVDEEWLELVEEEI-RELLAGTFLE--DAPIVPVSA-VTGEG-------IDELRAALDALAAAvPAR 171

                          90       100
                  ....*....|....*....|....*
gi 2173160141  86 AIDKPFLLPIEDVFSISGRGTVVTG 110
Cdd:COG3276   172 DADGPFRLPIDRVFSIKGFGTVVTG 196
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 72-112 3.64e-08

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 49.75  E-value: 3.64e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2173160141  72 LAGHLDTYIPePERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PTZ00141  216 LLEALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRV 255
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-112 1.27e-07

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 48.16  E-value: 1.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   1 LLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVREL---LSQYDFPGDDTPIVrgsALKALEGDaeweaKIIELAGHLD 77
Cdd:PLN00043  138 LLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVssyLKKVGYNPDKIPFV---PISGFEGD-----NMIERSTNLD 209

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2173160141  78 TY-----------IPEPERAIDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:PLN00043  210 WYkgptllealdqINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRV 255
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 87-112 1.94e-07

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: 45.26  E-value: 1.94e-07
                          10        20
                  ....*....|....*....|....*.
gi 2173160141  87 IDKPFLLPIEDVFSISGRGTVVTGRV 112
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRV 26
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 5-83 7.97e-05

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: 39.59  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2173160141   5 QVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDF---PGDDTPIVRGSALKALEGDaeweakiiELAGHLDTYIP 81
Cdd:cd00881   111 LAGGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGEGIE--------ELLDAIVEHLP 181


                  ..
gi 2173160141  82 EP 83
Cdd:cd00881   182 PP 183
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 69-110 1.80e-04

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 39.26  E-value: 1.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2173160141  69 IIELAGHLDTyIPEPERAIDKPFLLPIEDVFSISGRGTVVTG 110
Cdd:PRK10512  154 IDALREHLLQ-LPEREHAAQHRFRLAIDRAFTVKGAGLVVTG 194
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 91-112 5.06e-04

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: 35.97  E-value: 5.06e-04
                          10        20
                  ....*....|....*....|..
gi 2173160141  91 FLLPIEDVFSISGRGTVVTGRV 112
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTV 22
 
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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