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Conserved domains on  [gi|1124150260|gb|APQ43231|]
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elongation factor Tu, partial [Bacillus subtilis subsp. subtilis]

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
 1-204 6.08e-143

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 403.80  E-value: 6.08e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEG--DAEWEAKIFELMDAVDEYI 78
Cdd:PRK00049  123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYI 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  79 PTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLqEENKKTTVTGVEMFRKLLDYAEAGDNIGALL 158
Cdd:PRK00049  203 PTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI-RDTQKTTVTGVEMFRKLLDEGQAGDNVGALL 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1124150260 159 RGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:PRK00049  282 RGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFN 327
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-204 6.08e-143

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 403.80  E-value: 6.08e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEG--DAEWEAKIFELMDAVDEYI 78
Cdd:PRK00049  123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYI 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  79 PTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLqEENKKTTVTGVEMFRKLLDYAEAGDNIGALL 158
Cdd:PRK00049  203 PTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI-RDTQKTTVTGVEMFRKLLDEGQAGDNVGALL 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1124150260 159 RGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:PRK00049  282 RGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFN 327
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-204 2.95e-140

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: 396.83  E-value: 2.95e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEGD--AEWEAKIFELMDAVDEYI 78
Cdd:COG0050   123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYI 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  79 PTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLQEeNKKTTVTGVEMFRKLLDYAEAGDNIGALL 158
Cdd:COG0050   203 PEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRD-TQKTVVTGVEMFRKLLDEGEAGDNVGLLL 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1124150260 159 RGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:COG0050   282 RGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFN 327
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-204 7.98e-127

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: 362.94  E-value: 7.98e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEGDAEWEAKIFELMDAVDEYIPT 80
Cdd:TIGR00485 123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPT 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  81 PERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLQeENKKTTVTGVEMFRKLLDYAEAGDNIGALLRG 160
Cdd:TIGR00485 203 PEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLK-DTRKTTVTGVEMFRKELDEGRAGDNVGLLLRG 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1124150260 161 VSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:TIGR00485 282 IKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFS 325
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 89-176 3.91e-51

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: 159.61  E-value: 3.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  89 FMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLqEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQR 168
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGF-KETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79


                  ....*...
gi 1124150260 169 GQVLAKPG 176
Cdd:cd03697    80 GMVLAKPG 87
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 103-173 1.10e-19

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 78.85  E-value: 1.10e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124150260 103 GTVATGRVERGQVKVGDEVEIIGLQEENKK--TTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQRGQVLA 173
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKKivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-204 6.08e-143

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 403.80  E-value: 6.08e-143
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEG--DAEWEAKIFELMDAVDEYI 78
Cdd:PRK00049  123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYI 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  79 PTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLqEENKKTTVTGVEMFRKLLDYAEAGDNIGALL 158
Cdd:PRK00049  203 PTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGI-RDTQKTTVTGVEMFRKLLDEGQAGDNVGALL 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1124150260 159 RGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:PRK00049  282 RGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFN 327
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-204 2.95e-140

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: 396.83  E-value: 2.95e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEGD--AEWEAKIFELMDAVDEYI 78
Cdd:COG0050   123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYI 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  79 PTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLQEeNKKTTVTGVEMFRKLLDYAEAGDNIGALL 158
Cdd:COG0050   203 PEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIRD-TQKTVVTGVEMFRKLLDEGEAGDNVGLLL 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1124150260 159 RGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:COG0050   282 RGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFN 327
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-204 7.94e-137

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 388.43  E-value: 7.94e-137
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEGD--AEWEAKIFELMDAVDEYI 78
Cdd:PRK12735  123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGDddEEWEAKILELMDAVDSYI 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  79 PTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLQEeNKKTTVTGVEMFRKLLDYAEAGDNIGALL 158
Cdd:PRK12735  203 PEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIKE-TQKTTVTGVEMFRKLLDEGQAGDNVGVLL 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1124150260 159 RGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:PRK12735  282 RGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFN 327
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-204 5.31e-134

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 381.21  E-value: 5.31e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEGDAEWEAKIFELMDAVDEYIPT 80
Cdd:PRK12736  123 ARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPT 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  81 PERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLQEEnKKTTVTGVEMFRKLLDYAEAGDNIGALLRG 160
Cdd:PRK12736  203 PERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIKET-QKTVVTGVEMFRKLLDEGQAGDNVGVLLRG 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1124150260 161 VSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:PRK12736  282 VDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFN 325
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-204 7.98e-127

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: 362.94  E-value: 7.98e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEGDAEWEAKIFELMDAVDEYIPT 80
Cdd:TIGR00485 123 ARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPT 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  81 PERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLQeENKKTTVTGVEMFRKLLDYAEAGDNIGALLRG 160
Cdd:TIGR00485 203 PEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLK-DTRKTTVTGVEMFRKELDEGRAGDNVGLLLRG 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1124150260 161 VSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:TIGR00485 282 IKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFS 325
tufA CHL00071
elongation factor Tu
 1-203 8.86e-118

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 340.40  E-value: 8.86e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALE----------GDAEWEAKIFEL 70
Cdd:CHL00071  123 AKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  71 MDAVDEYIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLQEeNKKTTVTGVEMFRKLLDYAEA 150
Cdd:CHL00071  203 MDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLRE-TKTTTVTGLEMFQKTLDEGLA 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1124150260 151 GDNIGALLRGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFF 203
Cdd:CHL00071  282 GDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFF 334
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-204 1.91e-107

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 315.61  E-value: 1.91e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEG--DAEWEAKIFELMDAVDEYI 78
Cdd:PLN03127  172 ARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYI 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  79 PTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGL-QEENKKTTVTGVEMFRKLLDYAEAGDNIGAL 157
Cdd:PLN03127  252 PEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLrPGGPLKTTVTGVEMFKKILDQGQAGDNVGLL 331

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1124150260 158 LRGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:PLN03127  332 LRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFS 378
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-204 1.90e-98

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 293.45  E-value: 1.90e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALE----------GDAEWEAKIFEL 70
Cdd:PLN03126  192 AKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYEL 271

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  71 MDAVDEYIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLQEeNKKTTVTGVEMFRKLLDYAEA 150
Cdd:PLN03126  272 MDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRE-TRSTTVTGVEMFQKILDEALA 350

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1124150260 151 GDNIGALLRGVSREEIQRGQVLAKPGTITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:PLN03126  351 GDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFA 404
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 89-176 3.91e-51

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: 159.61  E-value: 3.91e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  89 FMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLqEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQR 168
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGF-KETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVER 79


                  ....*...
gi 1124150260 169 GQVLAKPG 176
Cdd:cd03697    80 GMVLAKPG 87
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-81 1.55e-34

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: 121.15  E-value: 1.55e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALEGD--AEWEAKIFELMDAVDEYI 78
Cdd:cd01884   113 ARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALEGDdpNKWVDKILELLDALDSYI 192


                  ...
gi 1124150260  79 PTP 81
Cdd:cd01884   193 PTP 195
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 1-191 5.01e-28

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: 108.87  E-value: 5.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVD-DEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKaleGD--------AEW--EAKIFE 69
Cdd:COG5256   133 ARTLGINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GDnvvkksdnMPWynGPTLLE 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  70 LMDAVDEyiptPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIiglQEENKKTTVTGVEMFRKLLDYAE 149
Cdd:COG5256   210 ALDNLKE----PEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVF---MPAGVVGEVKSIEMHHEELEQAE 282

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1124150260 150 AGDNIGALLRGVSREEIQRGQVLAKPGT-ITPHSKFKAEVYVL 191
Cdd:COG5256   283 PGDNIGFNVRGVEKNDIKRGDVAGHPDNpPTVAEEFTAQIVVL 325
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 1-191 6.93e-26

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 103.08  E-value: 6.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   1 SKNVGVPYIVVFLNKCDMVD-DEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALkalEGDaeweaKIFE---------- 69
Cdd:PRK12317  134 ARTLGINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAF---EGD-----NVVKksenmpwyng 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  70 --LMDAVDEyIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIiglQEENKKTTVTGVEMFRKLLDY 147
Cdd:PRK12317  206 ptLLEALDN-LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDKVVF---MPAGVVGEVKSIEMHHEELPQ 281

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1124150260 148 AEAGDNIGALLRGVSREEIQRGQV---LAKPGTITphSKFKAEVYVL 191
Cdd:PRK12317  282 AEPGDNIGFNVRGVGKKDIKRGDVcghPDNPPTVA--EEFTAQIVVL 326
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 5-192 9.22e-26

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: 103.84  E-value: 9.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   5 GVPYIVVFLNKCDMVDDEELLELVEMEvRDLLSEYDFPgdDVPVVKGSAlKALEGDAEWEAKIFELMDAVdeyiptPERD 84
Cdd:COG3276   103 GIKRGIVVLTKADLVDEEWLELVEEEI-RELLAGTFLE--DAPIVPVSA-VTGEGIDELRAALDALAAAV------PARD 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  85 TEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLqeeNKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSRE 164
Cdd:COG3276   173 ADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGDELELLPS---GKPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKE 249

                         170       180
                  ....*....|....*....|....*...
gi 1124150260 165 EIQRGQVLAKPGTITPHSKFKAEVYVLS 192
Cdd:COG3276   250 EIERGDVLAAPGALRPTDRIDVRLRLLP 277
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 85-171 3.51e-21

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


Pssm-ID: 293894 [Multi-domain]  Cd Length: 91  Bit Score: 83.39  E-value: 3.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  85 TEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIiglQEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSRE 164
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTF---APAGVTGEVKSVEMHHEPLEEAIPGDNVGFNVKGVSVK 77


                  ....*..
gi 1124150260 165 EIQRGQV 171
Cdd:cd03693    78 DIKRGDV 84
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 89-174 4.93e-20

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: 80.26  E-value: 4.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  89 FMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIiglQEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQR 168
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEI---PPLGKEVRVRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77


                  ....*.
gi 1124150260 169 GQVLAK 174
Cdd:cd03696    78 GFVLSE 83
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 103-173 1.10e-19

Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this is the second domain. This domain adopts a beta barrel structure. This the second domain is involved in binding to charged tRNA. This domain is also found in other proteins such as elongation factor G and translation initiation factor IF-2. This domain is structurally related to pfam03143, and in fact has weak sequence matches to this domain.


Pssm-ID: 427163 [Multi-domain]  Cd Length: 73  Bit Score: 78.85  E-value: 1.10e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124150260 103 GTVATGRVERGQVKVGDEVEIIGLQEENKK--TTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQRGQVLA 173
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKKivTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 70-191 2.59e-18

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 82.10  E-value: 2.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  70 LMDAVDEYIPtPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDeveIIGLQEENKKTTVTGVEMFRKLLDYAE 149
Cdd:PTZ00141  216 LLEALDTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGM---VVTFAPSGVTTEVKSVEMHHEQLAEAV 291

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1124150260 150 AGDNIGALLRGVSREEIQRGQVL--AKPGTITPHSKFKAEVYVL 191
Cdd:PTZ00141  292 PGDNVGFNVKNVSVKDIKRGYVAsdSKNDPAKECADFTAQVIVL 335
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 89-173 6.40e-18

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: 74.61  E-value: 6.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  89 FMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGlqeENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSreEIQR 168
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP---KGITGRVTSIERFHEEVDEAKAGDIVGIGILGVK--DILT 75


                  ....*
gi 1124150260 169 GQVLA 173
Cdd:cd01342    76 GDTLT 80
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
 2-175 2.87e-14

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: 70.67  E-value: 2.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   2 KNVGVPYIVVFLNKCDmVDDEELLELVEMEVRDLLSEYDFpGDDVPVVKGSAlKALEGDAEWEAKIFELMDAVDEyiptp 81
Cdd:TIGR00475  99 DLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIF-LKNAKIFKTSA-KTGQGIGELKKELKNLLESLDI----- 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  82 eRDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLqeeNKKTTVTGVEMFRKLLDYAEAGDNIGALLRGV 161
Cdd:TIGR00475 171 -KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI---NHEVRVKAIQAQNQDVEIAYAGQRIALNLMDV 246

                         170
                  ....*....|....
gi 1124150260 162 SREEIQRGQVLAKP 175
Cdd:TIGR00475 247 EPESLKRGLLILTP 260
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 4-80 1.24e-13

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: 66.01  E-value: 1.24e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1124150260   4 VGVPyIVVFLNKCDMVDDEELLELVEMEVRDLLSEYDFPGDDVPVVKGSALKALegdaeweaKIFELMDAVDEYIPT 80
Cdd:pfam00009 120 LGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKGE--------GVQTLLDALDEYLPS 187
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 179-204 1.88e-13

Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, designated I, II, and III. Domain III adopts a beta barrel structure. Domain III is involved in binding to both charged tRNA and to elongation factor Ts (EF-Ts). EF-Ts is the guanine-nucleotide-exchange factor for EF-Tu. EF-Tu and EF-G participate in the elongation phase during protein biosynthesis on the ribosome. Their functional cycles depend on GTP binding and its hydrolysis. The EF-Tu complexed with GTP and aminoacyl-tRNA delivers tRNA to the ribosome, whereas EF-G stimulates translocation, a process in which tRNA and mRNA movements occur in the ribosome. Crystallographic studies revealed structural similarities ("molecular mimicry") between tertiary structures of EF-G and the EF-Tu-aminoacyl-tRNA ternary complex. Domains III, IV, and V of EF-G mimic the tRNA structure in the EF-Tu ternary complex; domains III, IV and V can be related to the acceptor stem, anticodon helix and T stem of tRNA respectively.


Pssm-ID: 294006 [Multi-domain]  Cd Length: 90  Bit Score: 63.30  E-value: 1.88e-13
                          10        20
                  ....*....|....*....|....*.
gi 1124150260 179 TPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFS 26
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 70-192 1.63e-12

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 65.11  E-value: 1.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  70 LMDAVDEyIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGdevEIIGLQEENKKTTVTGVEMFRKLLDYAE 149
Cdd:PLN00043  216 LLEALDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPG---MVVTFGPTGLTTEVKSVEMHHESLQEAL 291

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1124150260 150 AGDNIGALLRGVSREEIQRGQVL--AKPGTITPHSKFKAEVYVLS 192
Cdd:PLN00043  292 PGDNVGFNVKNVAVKDLKRGYVAsnSKDDPAKEAANFTSQVIIMN 336
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 44-193 3.57e-12

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 64.10  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  44 DDVPVVKGSALKALEGDAeweakifeLMDAVDEYIPTPERDTEKPFMMPVEDVFSITGRGT--------VATGRVERGQV 115
Cdd:PRK04000  174 ENAPIIPVSALHKVNIDA--------LIEAIEEEIPTPERDLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVL 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260 116 KVGDEVEI---IGLQEENKK------TTVTGVEMFRKLLDYAEAGDNIG-------ALLRGVSreeiQRGQVLAKPGTIT 179
Cdd:PRK04000  246 KVGDEIEIrpgIKVEEGGKTkwepitTKIVSLRAGGEKVEEARPGGLVGvgtkldpSLTKADA----LAGSVAGKPGTLP 321

                         170
                  ....*....|....*
gi 1124150260 180 P-HSKFKAEVYVLSK 193
Cdd:PRK04000  322 PvWESLTIEVHLLER 336
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 89-173 1.45e-11

Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to GTPBP1 and GTPBP2. GTPBP1 is structurally related to elongation factor 1 alpha, a key component of the protein biosynthesis machinery. Immunohistochemical analyses on mouse tissues revealed that GTPBP1 is expressed in some neurons and smooth muscle cells of various organs as well as macrophages. Immunofluorescence analyses revealed that GTPBP1 is localized exclusively in cytoplasm and shows a diffuse granular network forming a gradient from the nucleus to the periphery of the cells in smooth muscle cell lines and macrophages. No significant difference was observed in the immune response to protein antigen between mutant mice and wild-type mice, suggesting normal function of antigen-presenting cells of the mutant mice. The absence of an eminent phenotype in GTPBP1-deficient mice may be due to functional compensation by GTPBP2, which is similar to GTPBP1 in structure and tissue distribution.


Pssm-ID: 293895 [Multi-domain]  Cd Length: 87  Bit Score: 58.00  E-value: 1.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  89 FMMPVEDVFSITGRGTVATGRVERGQVKVGDEVeIIGLQEENK--KTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEI 166
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTL-LLGPDADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESL 79


                  ....*..
gi 1124150260 167 QRGQVLA 173
Cdd:cd03694    80 RKGMVLV 86
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
 70-194 1.55e-11

Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and metabolism]; Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family is part of the Pathway/BioSystem: Cysteine biosynthesis


Pssm-ID: 442140 [Multi-domain]  Cd Length: 430  Bit Score: 62.41  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  70 LMDAVDEyIPTPERDTEKPFMMPVEDV--FSITGRGtVAtGRVERGQVKVGDEVEIiglQEENKKTTVTGVEMFRKLLDY 147
Cdd:COG2895   215 LLEHLET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG-YA-GTIASGTVRVGDEVVV---LPSGKTSTVKSIVTFDGDLEE 288

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1124150260 148 AEAGDNIGALLrgvSRE-EIQRGQVLAKPG-TITPHSKFKAEVYVLSKE 194
Cdd:COG2895   289 AFAGQSVTLTL---EDEiDISRGDVIVAADaPPEVADQFEATLVWMDEE 334
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 88-172 1.22e-10

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


Pssm-ID: 293906 [Multi-domain]  Cd Length: 82  Bit Score: 55.57  E-value: 1.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  88 PFMMPVEDVFSitGRGTVATGRVERGQVKVGD---------EVEIIGLQEENkkttvtgVEMfrkllDYAEAGDNIGALL 158
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGIYIDE-------EEV-----DSAKPGENVKLKL 66

                          90
                  ....*....|....
gi 1124150260 159 RGVSREEIQRGQVL 172
Cdd:cd04089    67 KGVEEEDISPGFVL 80
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 88-172 2.34e-10

Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class II release factor (eRF3). Hbs1, together with Dom34 (pelota), plays an important role in termination and recycling, but in contrast to eRF3/eRF1, Hbs1, together with Dom34 (pelota), functions on mRNA-bound ribosomes in a codon-independent manner and promotes subunit splitting on completely empty ribosomes.


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 54.83  E-value: 2.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  88 PFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIiglQEENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEIQ 167
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLV---MPSNETATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77


                  ....*
gi 1124150260 168 RGQVL 172
Cdd:cd16267    78 VGSIL 82
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 177-204 3.41e-10

Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural domains, this is the third domain. This domain adopts a beta barrel structure. This the third domain is involved in binding to both charged tRNA and binding to EF-Ts pfam00889.


Pssm-ID: 397314 [Multi-domain]  Cd Length: 105  Bit Score: 54.96  E-value: 3.41e-10
                          10        20
                  ....*....|....*....|....*...
gi 1124150260 177 TITPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFN 28
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 179-204 2.07e-08

Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% identical to bacterial EF-TU. The overall structure is similar to that observed in the Escherichia coli and Thermus aquaticus EF-TU. However, compared with that observed in prokaryotic EF-TU, the nucleotide-binding domain (domain I) of mtEF-TU is in a different orientation relative to the rest of the structure. Furthermore, domain III is followed by a short 11-amino acid extension that forms one helical turn. This extension seems to be specific to the mitochondrial factors and has not been observed in any of the prokaryotic factors.


Pssm-ID: 294005 [Multi-domain]  Cd Length: 93  Bit Score: 49.92  E-value: 2.07e-08
                          10        20
                  ....*....|....*....|....*.
gi 1124150260 179 TPHSKFKAEVYVLSKEEGGRHTPFFS 204
Cdd:cd03706     1 KMHNHFEAQVYLLSKEEGGRHKPFTS 26
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 93-173 7.59e-08

Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu consists of three structural domains; this family represents single domain proteins that are related to the second domain of EF-Tu. Domain II of EF-Tu adopts a beta barrel structure and is involved in binding to charged tRNA. Domain II is also found in other proteins such as elongation factor G and translation initiation factor IF-2.


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 48.06  E-value: 7.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  93 VEDVFSITGRgTVATGRVERGQVKVGDEVEIiglqeENKKTTVTGVEMFRKLLDYAEAGDNIGALLRGVSREEiqRGQVL 172
Cdd:cd16265     5 VEKVFKILGR-QVLTGEVESGVIYVGYKVKG-----DKGVALIRAIEREHRKVDFAVAGDEVALILEGKIKVK--EGDVL 76


                  .
gi 1124150260 173 A 173
Cdd:cd16265    77 E 77
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 89-174 1.07e-07

Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the large subunit of ATP sulfurylase (ATPS): CysN or the N-terminal portion of NodQ, found mainly in proteobacteria and homologous to the domain II of EF-Tu. Escherichia coli ATPS consists of CysN and a smaller subunit CysD. ATPS produces adenosine-5'-phosphosulfate (APS) from ATP and sulfate, coupled with GTP hydrolysis. In the subsequent reaction, APS is phosphorylated by an APS kinase (CysC), to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS) for use in amino acid (aa) biosynthesis. The Rhizobiaceae group (alpha-proteobacteria) appears to carry out the same chemistry for the sulfation of a nodulation factor. In Rhizobium meliloti, the heterodimeric complex comprised of NodP and NodQ appears to possess both ATPS and APS kinase activities. The N and C termini of NodQ correspond to CysN and CysC, respectively. Other eubacteria, archaea, and eukaryotes use a different ATP sulfurylase, which shows no amino acid sequence similarity to CysN or NodQ. CysN and the N-terminal portion of NodQ show similarity to GTPases involved in translation, in particular, EF-Tu and EF-1alpha.


Pssm-ID: 293896 [Multi-domain]  Cd Length: 81  Bit Score: 47.56  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  89 FMMPVEDV--FSITGRGTVatGRVERGQVKVGDEVEIiglQEENKKTTVTGVEMFRKLLDYAEAGDNIGALLrgvSRE-E 165
Cdd:cd03695     1 FRFPVQYVnrPNLDFRGYA--GTIASGSIRVGDEVTV---LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiD 72


                  ....*....
gi 1124150260 166 IQRGQVLAK 174
Cdd:cd03695    73 VSRGDLIVR 81
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 71-180 1.61e-07

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 50.77  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  71 MDAVDEY----IPTPERD-TEKPFMM---------PVEDVFSItgRGTVATGRVERGQVKVGDEVEII-GLQEENKKTTV 135
Cdd:PTZ00327  221 IDVVLEYictqIPIPKRDlTSPPRMIvirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEIRpGIISKDSGGEF 298

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1124150260 136 TGVEMFRKL---------LDYAEAGDNIGA---LLRGVSREEIQRGQVLAKPGTITP 180
Cdd:PTZ00327  299 TCRPIRTRIvslfaenneLQYAVPGGLIGVgttIDPTLTRADRLVGQVLGYPGKLPE 355
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 5-169 1.66e-07

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 50.82  E-value: 1.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   5 GVPYIVVFLNKCDMVDDEELLELVEMEVrDLLSEYDFPgdDVPVVKGSALKAlEGDAEWEAKIFELmdavdeyiPTPERD 84
Cdd:PRK10512  103 GNPMLTVALTKADRVDEARIAEVRRQVK-AVLREYGFA--EAKLFVTAATEG-RGIDALREHLLQL--------PEREHA 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  85 TEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVEIIGLqeeNKKTTVTGVEMFRKLLDYAEAGDNIGALLRG-VSR 163
Cdd:PRK10512  171 AQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGV---NKPMRVRGLHAQNQPTEQAQAGQRIALNIAGdAEK 247


                  ....*.
gi 1124150260 164 EEIQRG 169
Cdd:PRK10512  248 EQINRG 253
PRK10218 PRK10218
translational GTPase TypA;
45-155 6.80e-07

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 48.94  E-value: 6.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  45 DVPVVKGSALKALEG-DAEWEAK-IFELMDAVDEYIPTPERDTEKPFMMPVEDVFSITGRGTVATGRVERGQVKVGDEVE 122
Cdd:PRK10218  159 DFPIVYASALNGIAGlDHEDMAEdMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVT 238

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1124150260 123 IIGLQEENKKTTV----TGVEMFRKLLDYAEAGDNIG 155
Cdd:PRK10218  239 IIDSEGKTRNAKVgkvlGHLGLERIETDLAEAGDIVA 275
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 103-180 7.99e-07

Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global regulatory properties in Escherichia coli. BipA is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways. BipA functions as a translation factor that is required specifically for the expression of the transcriptional modulator Fis. BipA binds to ribosomes at a site that coincides with that of EF-G and has a GTPase activity that is sensitive to high GDP:GTP ratios and is stimulated by 70S ribosomes programmed with mRNA and aminoacylated tRNAs. The growth rate-dependent induction of BipA allows the efficient expression of Fis, thereby modulating a range of downstream processes, including DNA metabolism and type III secretion. The domain II of BipA shows similarity to the domain II of the elongation factors (EFs) EF-G and EF-Tu.


Pssm-ID: 293892 [Multi-domain]  Cd Length: 94  Bit Score: 45.64  E-value: 7.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260 103 GTVATGRVERGQVKVGDEVEIIGLQEENKKTTVTGVEMFRKL----LDYAEAGDNIGalLRGVsrEEIQRGQVLAKPGTI 178
Cdd:cd03691    15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGLerveVEEAEAGDIVA--IAGL--EDITIGDTICDPEVP 90


                  ..
gi 1124150260 179 TP 180
Cdd:cd03691    91 EP 92
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 88-173 1.95e-06

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: 44.41  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  88 PFMMPVEDVFSiTGRGTVATGRVERGQVKVGDEVEIIGLQE--ENKKTTVTGVEMfrklLDYAEAGDNIGALLRGVSREE 165
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQdaEVKNIIRNSDEE----TDWAIAGDTVTLRLRGIEVED 75


                  ....*...
gi 1124150260 166 IQRGQVLA 173
Cdd:cd03698    76 IQPGDILS 83
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
 5-81 7.74e-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: 41.51  E-value: 7.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260   5 GVPYIVVFLNKCDMvDDEELLELVEMEVRDLLSEYDF---PGDDVPVVKGSALKALegdaeweaKIFELMDAVDEYIPTP 81
Cdd:cd00881   113 GGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPIIPISALTGE--------GIEELLDAIVEHLPPP 183
EF2_II cd16268
Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 ...
 88-179 2.74e-04

Domain II of Elongation Factor 2; This subfamily represents domain II of elongation factor 2 (EF-2) found in eukaryotes and archaea. During the process of peptide synthesis and tRNA site changes, the ribosome is moved along the mRNA a distance equal to one codon with the addition of each amino acid. This translocation step is catalyzed by EF-2_GTP, which is hydrolyzed to provide the required energy. Thus, this action releases the uncharged tRNA from the P site and transfers the newly formed peptidyl-tRNA from the A site to the P site.


Pssm-ID: 293913 [Multi-domain]  Cd Length: 96  Bit Score: 38.74  E-value: 2.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  88 PFMMPVEDVFSI-TGRGTVATGRVERGQVKVGDEVEIIG------LQEENKKTTVTGVEMF----RKLLDYAEAGdNIGA 156
Cdd:cd16268     1 PLVMYVSKMVPTdKGAGFVAFGRVFSGTVRRGQEVYILGpkyvpgKKDDLKKKRIQQTYLMmgreREPVDEVPAG-NIVG 79

                          90       100
                  ....*....|....*....|...
gi 1124150260 157 LLrGVsreeiqrGQVLAKPGTIT 179
Cdd:cd16268    80 LV-GL-------DDFLAKSGTTT 94
PRK07560 PRK07560
elongation factor EF-2; Reviewed
 103-180 1.18e-03

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 39.08  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260 103 GTVATGRVERGQVKVGDEVEIIGLQEENKKTTVtGVEM--FRKLLDYAEAGdNIGALLrGVsrEEIQRGQVLAKPGTITP 180
Cdd:PRK07560  305 GEVATGRVFSGTLRKGQEVYLVGAKKKNRVQQV-GIYMgpEREEVEEIPAG-NIAAVT-GL--KDARAGETVVSVEDMTP 379
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 54-188 1.81e-03

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 38.36  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1124150260  54 LKALEGD--AEWEAKI--FE---LMDaVDEYIPTPERDTEKPFMMPVEDV---------FSitgrGTVATGrvergQVKV 117
Cdd:PRK05124  205 LSALEGDnvVSQSESMpwYSgptLLE-VLETVDIQRVVDAQPFRFPVQYVnrpnldfrgYA----GTLASG-----VVKV 274

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1124150260 118 GDEVEIIglqEENKKTTVTGVEMFRKLLDYAEAGDNIGALLrgvSRE-EIQRGQVLAKPG-TITPHSKFKAEV 188
Cdd:PRK05124  275 GDRVKVL---PSGKESNVARIVTFDGDLEEAFAGEAITLVL---EDEiDISRGDLLVAADeALQAVQHASADV 341
 
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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