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Conserved domains on  [gi|1686100126|gb|QDC27034|]
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translation elongation factor Tu, partial [Streptococcus pseudoporcinus]

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
 1-257 2.82e-177

elongation factor Tu; Reviewed


The actual alignment was detected with superfamily member PRK00049:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 493.17  E-value: 2.82e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEG--DSAHEDIIMELMKTVDEYIPEP 78
Cdd:PRK00049  126 VGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTP 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  79 ERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGV 158
Cdd:PRK00049  206 ERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIR-DTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGI 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 159 QRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVE 238
Cdd:PRK00049  285 KREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVE 364

                         250
                  ....*....|....*....
gi 1686100126 239 LIHPIAVEQGTTFSIREGG 257
Cdd:PRK00049  365 LIAPIAMEEGLRFAIREGG 383
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-257 2.82e-177

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 493.17  E-value: 2.82e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEG--DSAHEDIIMELMKTVDEYIPEP 78
Cdd:PRK00049  126 VGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTP 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  79 ERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGV 158
Cdd:PRK00049  206 ERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIR-DTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGI 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 159 QRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVE 238
Cdd:PRK00049  285 KREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVE 364

                         250
                  ....*....|....*....
gi 1686100126 239 LIHPIAVEQGTTFSIREGG 257
Cdd:PRK00049  365 LIAPIAMEEGLRFAIREGG 383
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-257 3.43e-175

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: 487.74  E-value: 3.43e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEGDSAHEDI--IMELMKTVDEYIPEP 78
Cdd:COG0050   126 VGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDPDPEWEkkILELMDAVDSYIPEP 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  79 ERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGV 158
Cdd:COG0050   206 ERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIR-DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGI 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 159 QRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVE 238
Cdd:COG0050   285 KREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVE 364

                         250
                  ....*....|....*....
gi 1686100126 239 LIHPIAVEQGTTFSIREGG 257
Cdd:COG0050   365 LITPIAMEEGLRFAIREGG 383
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-257 2.30e-150

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: 424.96  E-value: 2.30e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEGDSAHEDIIMELMKTVDEYIPEPER 80
Cdd:TIGR00485 126 VGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPER 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  81 DTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGVQR 160
Cdd:TIGR00485 206 EIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLK-DTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKR 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 161 DEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVELI 240
Cdd:TIGR00485 285 EEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELI 364

                         250
                  ....*....|....*..
gi 1686100126 241 HPIAVEQGTTFSIREGG 257
Cdd:TIGR00485 365 SPIALEQGMRFAIREGG 381
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 176-257 2.62e-56

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: 175.01  E-value: 2.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 176 NPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVELIHPIAVEQGTTFSIRE 255
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80


                  ..
gi 1686100126 256 GG 257
Cdd:cd03707    81 GG 82
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 174-257 9.20e-40

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: 133.16  E-value: 9.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 174 SINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIE------LPAGT----EMVMPGDNVTIDVELIHPI 243
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80

                          90
                  ....*....|....
gi 1686100126 244 AVEQGTTFSIREGG 257
Cdd:pfam03143  81 ALEKGQRFAIREGG 94
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
 1-257 2.82e-177

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 493.17  E-value: 2.82e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEG--DSAHEDIIMELMKTVDEYIPEP 78
Cdd:PRK00049  126 VGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTP 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  79 ERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGV 158
Cdd:PRK00049  206 ERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIR-DTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGI 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 159 QRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVE 238
Cdd:PRK00049  285 KREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVE 364

                         250
                  ....*....|....*....
gi 1686100126 239 LIHPIAVEQGTTFSIREGG 257
Cdd:PRK00049  365 LIAPIAMEEGLRFAIREGG 383
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
 1-257 3.43e-175

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: 487.74  E-value: 3.43e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEGDSAHEDI--IMELMKTVDEYIPEP 78
Cdd:COG0050   126 VGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYGFPGDDTPIIRGSALKALEGDPDPEWEkkILELMDAVDSYIPEP 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  79 ERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGV 158
Cdd:COG0050   206 ERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIKVGDEVEIVGIR-DTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGI 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 159 QRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVE 238
Cdd:COG0050   285 KREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVE 364

                         250
                  ....*....|....*....
gi 1686100126 239 LIHPIAVEQGTTFSIREGG 257
Cdd:COG0050   365 LITPIAMEEGLRFAIREGG 383
PRK12736 PRK12736
elongation factor Tu; Reviewed
 1-257 3.80e-172

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 480.21  E-value: 3.80e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEGDSAHEDIIMELMKTVDEYIPEPER 80
Cdd:PRK12736  126 VGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSEYDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPER 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  81 DTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGVQR 160
Cdd:PRK12736  206 DTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVGDEVEIVGIK-ETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDR 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 161 DEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVELI 240
Cdd:PRK12736  285 DEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELI 364

                         250
                  ....*....|....*..
gi 1686100126 241 HPIAVEQGTTFSIREGG 257
Cdd:PRK12736  365 HPIAMEQGLKFAIREGG 381
PRK12735 PRK12735
elongation factor Tu; Reviewed
 1-257 1.89e-170

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 475.87  E-value: 1.89e-170
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEGDSAH--EDIIMELMKTVDEYIPEP 78
Cdd:PRK12735  126 VGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSKYDFPGDDTPIIRGSALKALEGDDDEewEAKILELMDAVDSYIPEP 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  79 ERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGV 158
Cdd:PRK12735  206 ERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVKVGDEVEIVGIK-ETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGT 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 159 QRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVE 238
Cdd:PRK12735  285 KREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVE 364

                         250
                  ....*....|....*....
gi 1686100126 239 LIHPIAVEQGTTFSIREGG 257
Cdd:PRK12735  365 LIAPIAMEEGLRFAIREGG 383
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
 1-257 2.30e-150

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: 424.96  E-value: 2.30e-150
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEGDSAHEDIIMELMKTVDEYIPEPER 80
Cdd:TIGR00485 126 VGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPER 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  81 DTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGVQR 160
Cdd:TIGR00485 206 EIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVGEEVEIVGLK-DTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKR 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 161 DEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVELI 240
Cdd:TIGR00485 285 EEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELI 364

                         250
                  ....*....|....*..
gi 1686100126 241 HPIAVEQGTTFSIREGG 257
Cdd:TIGR00485 365 SPIALEQGMRFAIREGG 381
tufA CHL00071
elongation factor Tu
 1-257 1.71e-140

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 400.49  E-value: 1.71e-140
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALE----------GDSAHEDIIMELMKT 70
Cdd:CHL00071  126 VGVPNIVVFLNKEDQVDDEELLELVELEVRELLSKYDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDA 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  71 VDEYIPEPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKeDTKKAVVTGVEMFRKQLDEGLAGDN 150
Cdd:CHL00071  206 VDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATGRIERGTVKVGDTVEIVGLR-ETKTTTVTGLEMFQKTLDEGLAGDN 284

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 151 VGILLRGVQRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIEL-----PAGTE 225
Cdd:CHL00071  285 VGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVYILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTE 364

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1686100126 226 MVMPGDNVTIDVELIHPIAVEQGTTFSIREGG 257
Cdd:CHL00071  365 MVMPGDRIKMTVELIYPIAIEKGMRFAIREGG 396
PLN03127 PLN03127
Elongation factor Tu; Provisional
 1-257 1.36e-135

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 389.57  E-value: 1.36e-135
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEG--DSAHEDIIMELMKTVDEYIPEP 78
Cdd:PLN03127  175 VGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFYKFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEP 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  79 ERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKED-TKKAVVTGVEMFRKQLDEGLAGDNVGILLRG 157
Cdd:PLN03127  255 VRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKVGEEVEIVGLRPGgPLKTTVTGVEMFKKILDQGQAGDNVGLLLRG 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 158 VQRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDV 237
Cdd:PLN03127  335 LKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEGGRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVF 414

                         250       260
                  ....*....|....*....|
gi 1686100126 238 ELIHPIAVEQGTTFSIREGG 257
Cdd:PLN03127  415 ELISPVPLEPGQRFALREGG 434
PLN03126 PLN03126
Elongation factor Tu; Provisional
 1-257 3.78e-116

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 341.21  E-value: 3.78e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALE----------GDSAHEDIIMELMKT 70
Cdd:PLN03126  195 VGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSYEFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDA 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  71 VDEYIPEPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKEdTKKAVVTGVEMFRKQLDEGLAGDN 150
Cdd:PLN03126  275 VDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGRVERGTVKVGETVDIVGLRE-TRSTTVTGVEMFQKILDEALAGDN 353

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 151 VGILLRGVQRDEIERGQVIAKPGSINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSI-----ELPAGTE 225
Cdd:PLN03126  354 VGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYVLKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESK 433

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1686100126 226 MVMPGDNVTIDVELIHPIAVEQGTTFSIREGG 257
Cdd:PLN03126  434 MVMPGDRVKMVVELIVPVACEQGMRFAIREGG 465
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
 176-257 2.62e-56

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: 175.01  E-value: 2.62e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 176 NPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVELIHPIAVEQGTTFSIRE 255
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80


                  ..
gi 1686100126 256 GG 257
Cdd:cd03707    81 GG 82
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
 87-173 2.18e-47

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: 152.29  E-value: 2.18e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  87 LLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKEdTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGVQRDEIERG 166
Cdd:cd03697     2 LMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKE-TLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80


                  ....*..
gi 1686100126 167 QVIAKPG 173
Cdd:cd03697    81 MVLAKPG 87
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
 174-257 9.20e-40

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: 133.16  E-value: 9.20e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 174 SINPHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIE------LPAGT----EMVMPGDNVTIDVELIHPI 243
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80

                          90
                  ....*....|....
gi 1686100126 244 AVEQGTTFSIREGG 257
Cdd:pfam03143  81 ALEKGQRFAIREGG 94
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
 177-257 1.25e-29

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: 106.93  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 177 PHTKFKGEVYILSKEEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEMVMPGDNVTIDVELIHPIAVEQGTTFSIREG 256
Cdd:cd03706     2 MHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLREG 81


                  .
gi 1686100126 257 G 257
Cdd:cd03706    82 G 82
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
 1-78 7.75e-26

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: 99.97  E-value: 7.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKALEGDSAHEDI--IMELMKTVDEYIPEP 78
Cdd:cd01884   116 VGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPIVRGSALKALEGDDPNKWVdkILELLDALDSYIPTP 195
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
 2-188 2.08e-23

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: 97.70  E-value: 2.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   2 GVKHLIVFMNKVDLVD-DEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKaleGDSahediIME------------LM 68
Cdd:COG5256   137 GINQLIVAVNKMDAVNySEKRYEEVKEEVSKLLKMVGYKVDKIPFIPVSAWK---GDN-----VVKksdnmpwyngptLL 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  69 KTVDEyIPEPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVgikEDTKKAVVTGVEMFRKQLDEGLAG 148
Cdd:COG5256   209 EALDN-LKEPEKPVDKPLRIPIQDVYSISGIGTVPVGRVETGVLKVGDKVVFM---PAGVVGEVKSIEMHHEELEQAEPG 284

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1686100126 149 DNVGILLRGVQRDEIERGQVIAKPGsiNPHT---KFKGEVYIL 188
Cdd:COG5256   285 DNIGFNVRGVEKNDIKRGDVAGHPD--NPPTvaeEFTAQIVVL 325
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
 2-188 2.17e-22

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 94.99  E-value: 2.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   2 GVKHLIVFMNKVDLVD-DEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALkalEGDSAHE----------DIIMELMKT 70
Cdd:PRK12317  138 GINQLIVAINKMDAVNyDEKRYEEVKEEVSKLLKMVGYKPDDIPFIPVSAF---EGDNVVKksenmpwyngPTLLEALDN 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  71 vdeyIPEPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEieiVGIKEDTKKAVVTGVEMFRKQLDEGLAGDN 150
Cdd:PRK12317  215 ----LKPPEKPTDKPLRIPIQDVYSISGVGTVPVGRVETGVLKVGDK---VVFMPAGVVGEVKSIEMHHEELPQAEPGDN 287

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1686100126 151 VGILLRGVQRDEIERGQVIAKPGsiNPHT---KFKGEVYIL 188
Cdd:PRK12317  288 IGFNVRGVGKKDIKRGDVCGHPD--NPPTvaeEFTAQIVVL 326
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
 27-257 1.38e-20

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: 90.36  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  27 MEIRDLLSEYDFPgdDLPVIQGSALkalEGDSahediIMELMKTVDEYIPE-PERDTDKPLLLPVEDVFSITGRGTVASG 105
Cdd:COG3276   127 EEIRELLAGTFLE--DAPIVPVSAV---TGEG-----IDELRAALDALAAAvPARDADGPFRLPIDRVFSIKGFGTVVTG 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 106 RIDRGTVRVNDEIEIVGIKedtKKAVVTGVEMFRKQLDEGLAGDNVGILLRGVQRDEIERGQVIAKPGSINPHTKFKGEV 185
Cdd:COG3276   197 TLLSGTVRVGDELELLPSG---KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRL 273

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1686100126 186 YILSKEeggrHTPFFNNYRPQFYFRTTDVTGSIeLPAGTEMVMPGDNVTIDVELIHPIAVEQGTTFSIREGG 257
Cdd:COG3276   274 RLLPSA----PRPLKHWQRVHLHHGTAEVLARV-VLLDREELAPGEEALAQLRLEEPLVAARGDRFILRDYS 340
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
 86-171 4.00e-19

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: 79.11  E-value: 4.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  86 LLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKEDTKkavVTGVEMFRKQLDEGLAGDNVGILLRGVQRDEIER 165
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVR---VRSIQVHDKPVEEAKAGDRVALNLTGVDAKELER 77


                  ....*.
gi 1686100126 166 GQVIAK 171
Cdd:cd03696    78 GFVLSE 83
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
 82-173 5.18e-19

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: 79.15  E-value: 5.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  82 TDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEI--VGIKEDTKKavvtgVEMFRKQLDEGLAGDNVGILLRGVQ 159
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTFapAGVTGEVKS-----VEMHHEPLEEAIPGDNVGFNVKGVS 75

                          90
                  ....*....|....
gi 1686100126 160 RDEIERGQVIAKPG 173
Cdd:cd03693    76 VKDIKRGDVAGDSK 89
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
 100-170 9.95e-17

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: 72.68  E-value: 9.95e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1686100126 100 GTVASGRIDRGTVRVNDEIEIVGIKEDTKKAV--VTGVEMFRKQLDEGLAGDNVGILLRGVQRDEIERGQVIA 170
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPNGTGKKKIVtrVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
 2-168 6.81e-16

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 76.32  E-value: 6.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   2 GVKHLIVFMNKVDLVDDEELLE---LVEMEIRDLLSEYDFPGDDLPVIqgsALKALEGDSAHEDII-ME------LMKTV 71
Cdd:PTZ00141  144 GVKQMIVCINKMDDKTVNYSQErydEIKKEVSAYLKKVGYNPEKVPFI---PISGWQGDNMIEKSDnMPwykgptLLEAL 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  72 DEYIPePERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEI--VGIKEDTKKavvtgVEMFRKQLDEGLAGD 149
Cdd:PTZ00141  221 DTLEP-PKRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFapSGVTTEVKS-----VEMHHEQLAEAVPGD 294

                         170
                  ....*....|....*....
gi 1686100126 150 NVGILLRGVQRDEIERGQV 168
Cdd:PTZ00141  295 NVGFNVKNVSVKDIKRGYV 313
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
 86-170 2.49e-15

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: 68.83  E-value: 2.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  86 LLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGikeDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGVqrDEIER 165
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILP---KGITGRVTSIERFHEEVDEAKAGDIVGIGILGV--KDILT 75


                  ....*
gi 1686100126 166 GQVIA 170
Cdd:cd01342    76 GDTLT 80
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
 1-226 8.62e-13

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 67.42  E-value: 8.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVD---DEELLELVEMEIRDLLSEYDFPGDDLPVIqgsALKALEGDSAHEDIIM-------ELMKT 70
Cdd:PLN00043  143 LGVKQMICCCNKMDATTpkySKARYDEIVKEVSSYLKKVGYNPDKIPFV---PISGFEGDNMIERSTNldwykgpTLLEA 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  71 VDEyIPEPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKEDTKkavVTGVEMFRKQLDEGLAGDN 150
Cdd:PLN00043  220 LDQ-INEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFGPTGLTTE---VKSVEMHHESLQEALPGDN 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 151 VGILLRGVQRDEIERGQVI--AKPGSINPHTKFKGEVYILSK--EEGGRHTPFFNNYRPQFYFRTTDVTGSIELPAGTEM 226
Cdd:PLN00043  296 VGFNVKNVAVKDLKRGYVAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKEL 375
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
 85-169 3.60e-09

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: 52.52  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  85 PLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEIEIVGIKEDtkkAVVTGVEMFRKQLDEGLAGDNVGILLRGVQRDEIE 164
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET---ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLR 77


                  ....*
gi 1686100126 165 RGQVI 169
Cdd:cd16267    78 VGSIL 82
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
 90-170 1.13e-08

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: 51.07  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  90 VEDVFSITGRGTVASGRIDRGTVRVNDEIEIvGIKEDTK--KAVVTGVEMFRKQLDEGLAGDNVGILLRGVQRDEIERGQ 167
Cdd:cd03694     5 IDDIYSVPGVGTVVSGTVSKGVIREGDTLLL-GPDADGKfrPVTVKSIHRNRQPVDRARAGQSASFALKKIKRESLRKGM 83


                  ...
gi 1686100126 168 VIA 170
Cdd:cd03694    84 VLV 86
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
 177-257 2.58e-08

Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) EF-Tu participates in the elongation phase during protein biosynthesis on the ribosome. Its 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. Experimental findings indicate an essential contribution of domain III to activation of GTP hydrolysis. This domain III, which is distinct from the domain III in EFG and related elongation factors, is found in several eukaryotic translation factors, like peptide chain release factors RF3, elongation factor 1, selenocysteine (Sec)-specific elongation factor, and in GT-1 family of GTPase (GTPBP1).


Pssm-ID: 275447 [Multi-domain]  Cd Length: 102  Bit Score: 50.47  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126 177 PHTKFKGEVYILSKEEggrhtPFFNNYRPQFYFRTTDVTGSIELPAGTE-----------MVMPGDNVTIDVELIHPIAV 245
Cdd:cd01513     2 AVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVVL 76

                          90
                  ....*....|....*...
gi 1686100126 246 EQGTT------FSIREGG 257
Cdd:cd01513    77 ERGKEfptlgrFALRDGG 94
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
 1-190 3.04e-08

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 53.70  E-value: 3.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   1 VGVKHLIVFMNKVDLVdDEELLELVEMEIRDLLSEYDFpgDDLPVIQGSALkalegdsaHEDIIMELMKTVDEYIPEPER 80
Cdd:PRK04000  137 IGIKNIVIVQNKIDLV-SKERALENYEQIKEFVKGTVA--ENAPIIPVSAL--------HKVNIDALIEAIEEEIPTPER 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  81 DTDKPLLLPVEDVFSITGRGT--------VASGRIDRGTVRVNDEIEIV-GIKEDTKKAV--------VTGVEMFRKQLD 143
Cdd:PRK04000  206 DLDKPPRMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGGKTkwepittkIVSLRAGGEKVE 285

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1686100126 144 EGLAGDNVGI-------LLRGvqrDEIeRGQVIAKPGSINP-HTKFKGEVYILSK 190
Cdd:PRK04000  286 EARPGGLVGVgtkldpsLTKA---DAL-AGSVAGKPGTLPPvWESLTIEVHLLER 336
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
 90-170 1.25e-07

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: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  90 VEDVFSITGRgTVASGRIDRGTVRVNDEIeivgiKEDTKKAVVTGVEMFRKQLDEGLAGDNVGILLRGVQRdeIERGQVI 169
Cdd:cd16265     5 VEKVFKILGR-QVLTGEVESGVIYVGYKV-----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEGKIK--VKEGDVL 76


                  .
gi 1686100126 170 A 170
Cdd:cd16265    77 E 77
PRK10218 PRK10218
translational GTPase TypA;
42-153 2.64e-07

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 51.25  E-value: 2.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  42 DLPVIQGSALKALEGDSaHEDI---IMELMKTVDEYIPEPERDTDKPLLLPVEDVFSITGRGTVASGRIDRGTVRVNDEI 118
Cdd:PRK10218  159 DFPIVYASALNGIAGLD-HEDMaedMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQV 237

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1686100126 119 EIVGIKEDTKKA----VVTGVEMFRKQLDEGLAGDNVGI 153
Cdd:PRK10218  238 TIIDSEGKTRNAkvgkVLGHLGLERIETDLAEAGDIVAI 276
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
 85-169 4.51e-07

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: 46.32  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  85 PLLLPVEDVFSitGRGTVASGRIDRGTVRVNDEIEIVGIKedtKKAVVTGVEMFRKQLDEGLAGDNVGILLRGVQRDEIE 164
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQKLVLMPNK---TKVEVTGIYIDEEEVDSAKPGENVKLKLKGVEEEDIS 75


                  ....*
gi 1686100126 165 RGQVI 169
Cdd:cd04089    76 PGFVL 80
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
 85-170 4.85e-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: 43.64  E-value: 4.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  85 PLLLPVEDVFSiTGRGTVASGRIDRGTVRVNDEIEIVGIKEDtkkAVVTGVEM-FRKQLDEGLAGDNVGILLRGVQRDEI 163
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQD---AEVKNIIRnSDEETDWAIAGDTVTLRLRGIEVEDI 76


                  ....*..
gi 1686100126 164 ERGQVIA 170
Cdd:cd03698    77 QPGDILS 83
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
 1-76 8.61e-06

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: 45.21  E-value: 8.61e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1686100126   1 VGVKhLIVFMNKVDLVDDEELLELVEMEIRDLLSEYDFPGDDLPVIQGSALKAlEGdsahediIMELMKTVDEYIP 76
Cdd:pfam00009 120 LGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGEFVPVVPGSALKG-EG-------VQTLLDALDEYLP 186
BipA_TypA_II cd03691
Domain II of BipA; BipA (also called TypA) is a highly conserved protein with global ...
 100-153 5.50e-04

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


Pssm-ID: 293892 [Multi-domain]  Cd Length: 94  Bit Score: 38.32  E-value: 5.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1686100126 100 GTVASGRIDRGTVRVNDEIEIVGIKEDTKKAVVTGVEMFRK----QLDEGLAGDNVGI 153
Cdd:cd03691    15 GRIAIGRIFSGTVKVGQQVTVVDEDGKIEKGRVTKLFGFEGlervEVEEAEAGDIVAI 72
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
 88-171 9.04e-04

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: 37.16  E-value: 9.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  88 LPVEDV--FSITGRGTvaSGRIDRGTVRVNDEIEIVgikEDTKKAVVTGVEMFRKQLDEGLAGDNVGILLrgvqRDEIE- 164
Cdd:cd03695     3 FPVQYVnrPNLDFRGY--AGTIASGSIRVGDEVTVL---PSGKTSRVKSIVTFDGELDSAGAGEAVTLTL----EDEIDv 73


                  ....*...
gi 1686100126 165 -RGQVIAK 171
Cdd:cd03695    74 sRGDLIVR 81
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
 2-120 2.35e-03

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 38.83  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   2 GVKHLIVFMNKVDLVDDEELLELVEmEIRDLLSEYDfpGDDLPVIQGSA-LKAlegdsaHEDIIMELMKTvdeYIPEPER 80
Cdd:PTZ00327  170 KLKHIIILQNKIDLVKEAQAQDQYE-EIRNFVKGTI--ADNAPIIPISAqLKY------NIDVVLEYICT---QIPIPKR 237

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1686100126  81 D-TDKPLL---------LPVEDVFSItgRGTVASGRIDRGTVRVNDEIEI 120
Cdd:PTZ00327  238 DlTSPPRMivirsfdvnKPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
 28-166 2.41e-03

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 38.88  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  28 EIRDLLSEYDFPGDDLPVIqgsalkalegdSAHEDIIMELMKTVDEYIPEPERDTDKPLLLPVEDVFSITGRGTVASGRI 107
Cdd:PRK10512  128 QVKAVLREYGFAEAKLFVT-----------AATEGRGIDALREHLLQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTA 196

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1686100126 108 DRGTVRVNDEIEIVGIkedtKKAV-VTGVEMFRKQLDEGLAGDNVGILLRG-VQRDEIERG 166
Cdd:PRK10512  197 LSGEVKVGDTLWLTGV----NKPMrVRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
 2-174 3.22e-03

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 38.36  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126   2 GVKHLIVFMNKvdlvddeellelveM-----------EIRDllsEY-----DFPGDdlPVIQGSALKALEGD-----SAH 60
Cdd:PRK05124  159 GIKHLVVAVNK--------------MdlvdyseevfeRIRE---DYltfaeQLPGN--LDIRFVPLSALEGDnvvsqSES 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1686100126  61 ED-----IIMELMKTVDeyipePERDTD-KPLLLPVEDV---------FSitgrGTVASgridrGTVRVNDEIEIV--Gi 123
Cdd:PRK05124  220 MPwysgpTLLEVLETVD-----IQRVVDaQPFRFPVQYVnrpnldfrgYA----GTLAS-----GVVKVGDRVKVLpsG- 284

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1686100126 124 KEDTKKAVVTgvemFRKQLDEGLAGDNVGILLrgvqRDEIE--RGQVIAKPGS 174
Cdd:PRK05124  285 KESNVARIVT----FDGDLEEAFAGEAITLVL----EDEIDisRGDLLVAADE 329
 
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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