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Conserved domains on  [gi|1383508603|ref|WP_108629465|]
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MULTISPECIES: elongation factor Tu, partial [Salmonella]

Protein Classification

elongation factor Tu( domain architecture ID 11477830)

elongation factor Tu promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-385 0e+00

elongation factor Tu; Reviewed


:

Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 868.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK00049    1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:PRK00049   81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEG--DAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK 238
Cdd:PRK00049  161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 239 VGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGG 318
Cdd:PRK00049  241 VGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383508603 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:PRK00049  321 RHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVG 387
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-385 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 868.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK00049    1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:PRK00049   81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEG--DAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK 238
Cdd:PRK00049  161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 239 VGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGG 318
Cdd:PRK00049  241 VGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383508603 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:PRK00049  321 RHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVG 387
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
1-385 0e+00

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: 850.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:COG0050     1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:COG0050    81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK 238
Cdd:COG0050   161 YGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 239 VGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGG 318
Cdd:COG0050   241 VGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383508603 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:COG0050   321 RHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVG 387
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
1-385 0e+00

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: 758.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:TIGR00485   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:TIGR00485  81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEGDAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 241 EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRH 320
Cdd:TIGR00485 241 EEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRH 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1383508603 321 TPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:TIGR00485 321 TPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVG 385
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
11-203 3.19e-132

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: 376.54  E-value: 3.19e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVK 90
Cdd:cd01884     1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  91 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPI 170
Cdd:cd01884    81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1383508603 171 VRGSALKALEGD--AEWEAKIIELAGFLDSYIPEP 203
Cdd:cd01884   161 VRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
10-201 4.94e-79

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: 240.89  E-value: 4.94e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  10 KPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHA 86
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGD 166
Cdd:pfam00009  81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1383508603 167 DTPIVRGSALKALegdaeweaKIIELAGFLDSYIP 201
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLP 186
 
Name Accession Description Interval E-value
PRK00049 PRK00049
elongation factor Tu; Reviewed
1-385 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 234596 [Multi-domain]  Cd Length: 396  Bit Score: 868.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK00049    1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAEAKAYDQIDKAPEEKARGITINTAHVEYETEKRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:PRK00049   81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEG--DAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK 238
Cdd:PRK00049  161 YDFPGDDTPIIRGSALKALEGddDEEWEKKILELMDAVDSYIPTPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIIK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 239 VGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGG 318
Cdd:PRK00049  241 VGEEVEIVGIRDTQKTTVTGVEMFRKLLDEGQAGDNVGALLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383508603 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:PRK00049  321 RHTPFFNGYRPQFYFRTTDVTGVIELPEGVEMVMPGDNVEMTVELIAPIAMEEGLRFAIREGGRTVG 387
TufA COG0050
Translation elongation factor EF-Tu, a GTPase [Translation, ribosomal structure and biogenesis] ...
1-385 0e+00

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: 850.98  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:COG0050     1 MAKEKFERTKPHVNIGTIGHVDHGKTTLTAAITKVLAKKGGAKAKAYDQIDKAPEEKERGITINTSHVEYETEKRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:COG0050    81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK 238
Cdd:COG0050   161 YGFPGDDTPIIRGSALKALEGDpdPEWEKKILELMDAVDSYIPEPERDTDKPFLMPVEDVFSITGRGTVVTGRVERGIIK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 239 VGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGG 318
Cdd:COG0050   241 VGDEVEIVGIRDTQKTVVTGVEMFRKLLDEGEAGDNVGLLLRGIKREDVERGQVLAKPGSITPHTKFEAEVYVLSKEEGG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383508603 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:COG0050   321 RHTPFFNGYRPQFYFRTTDVTGVITLPEGVEMVMPGDNVTMTVELITPIAMEEGLRFAIREGGRTVG 387
PRK12735 PRK12735
elongation factor Tu; Reviewed
1-385 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 183708 [Multi-domain]  Cd Length: 396  Bit Score: 845.27  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK12735    1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITKVLAKKGGGEAKAYDQIDNAPEEKARGITINTSHVEYETANRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:PRK12735   81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEGD--AEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIK 238
Cdd:PRK12735  161 YDFPGDDTPIIRGSALKALEGDddEEWEAKILELMDAVDSYIPEPERAIDKPFLMPIEDVFSISGRGTVVTGRVERGIVK 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 239 VGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGG 318
Cdd:PRK12735  241 VGDEVEIVGIKETQKTTVTGVEMFRKLLDEGQAGDNVGVLLRGTKREDVERGQVLAKPGSIKPHTKFEAEVYVLSKEEGG 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1383508603 319 RHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:PRK12735  321 RHTPFFNGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIAPIAMEEGLRFAIREGGRTVG 387
PRK12736 PRK12736
elongation factor Tu; Reviewed
1-385 0e+00

elongation factor Tu; Reviewed


Pssm-ID: 237184 [Multi-domain]  Cd Length: 394  Bit Score: 795.69  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:PRK12736    1 MAKEKFDRSKPHVNIGTIGHVDHGKTTLTAAITKVLAERGLNQAKDYDSIDAAPEEKERGITINTAHVEYETEKRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:PRK12736   81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLARQVGVPYLVVFLNKVDLVDDEELLELVEMEVRELLSE 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEGDAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG 240
Cdd:PRK12736  161 YDFPGDDIPVIRGSALKALEGDPKWEDAIMELMDAVDEYIPTPERDTDKPFLMPVEDVFTITGRGTVVTGRVERGTVKVG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 241 EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRH 320
Cdd:PRK12736  241 DEVEIVGIKETQKTVVTGVEMFRKLLDEGQAGDNVGVLLRGVDRDEVERGQVLAKPGSIKPHTKFKAEVYILTKEEGGRH 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1383508603 321 TPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:PRK12736  321 TPFFNNYRPQFYFRTTDVTGSIELPEGTEMVMPGDNVTITVELIHPIAMEQGLKFAIREGGRTVG 385
EF-Tu TIGR00485
translation elongation factor TU; This model models orthologs of translation elongation factor ...
1-385 0e+00

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: 758.93  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:TIGR00485   1 MAKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKEGGAAARAYDQIDNAPEEKARGITINTAHVEYETETRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:TIGR00485  81 DCPGHADYVKNMITGAAQMDGAILVVSATDGPMPQTREHILLARQVGVPYIVVFLNKCDMVDDEELLELVEMEVRELLSQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALEGDAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVG 240
Cdd:TIGR00485 161 YDFPGDDTPIIRGSALKALEGDAEWEAKILELMDAVDEYIPTPEREIDKPFLLPIEDVFSITGRGTVVTGRVERGIIKVG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 241 EEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEGGRH 320
Cdd:TIGR00485 241 EEVEIVGLKDTRKTTVTGVEMFRKELDEGRAGDNVGLLLRGIKREEIERGMVLAKPGSIKPHTKFEAEVYVLSKEEGGRH 320
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1383508603 321 TPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:TIGR00485 321 TPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELISPIALEQGMRFAIREGGRTVG 385
tufA CHL00071
elongation factor Tu
1-385 0e+00

elongation factor Tu


Pssm-ID: 177010 [Multi-domain]  Cd Length: 409  Bit Score: 707.88  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:CHL00071    1 MAREKFERKKPHVNIGTIGHVDHGKTTLTAAITMTLAAKGGAKAKKYDEIDSAPEEKARGITINTAHVEYETENRHYAHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQ 160
Cdd:CHL00071   81 DCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTKEHILLAKQVGVPNIVVFLNKEDQVDDEELLELVELEVRELLSK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 161 YDFPGDDTPIVRGSALKALE----------GDAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTG 230
Cdd:CHL00071  161 YDFPGDDIPIVSGSALLALEaltenpkikrGENKWVDKIYNLMDAVDSYIPTPERDTDKPFLMAIEDVFSITGRGTVATG 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 231 RVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVY 310
Cdd:CHL00071  241 RIERGTVKVGDTVEIVGLRETKTTTVTGLEMFQKTLDEGLAGDNVGILLRGIQKEDIERGMVLAKPGTITPHTKFEAQVY 320
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 311 ILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIEL-----PEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:CHL00071  321 ILTKEEGGRHTPFFPGYRPQFYVRTTDVTGKIESftaddGSKTEMVMPGDRIKMTVELIYPIAIEKGMRFAIREGGRTVG 400
PLN03127 PLN03127
Elongation factor Tu; Provisional
2-385 0e+00

Elongation factor Tu; Provisional


Pssm-ID: 178673 [Multi-domain]  Cd Length: 447  Bit Score: 667.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   2 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 81
Cdd:PLN03127   51 SMATFTRTKPHVNVGTIGHVDHGKTTLTAAITKVLAEEGKAKAVAFDEIDKAPEEKARGITIATAHVEYETAKRHYAHVD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 161
Cdd:PLN03127  131 CPGHADYVKNMITGAAQMDGGILVVSAPDGPMPQTKEHILLARQVGVPSLVVFLNKVDVVDDEELLELVEMELRELLSFY 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 162 DFPGDDTPIVRGSALKALEG--DAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKV 239
Cdd:PLN03127  211 KFPGDEIPIIRGSALSALQGtnDEIGKNAILKLMDAVDEYIPEPVRVLDKPFLMPIEDVFSIQGRGTVATGRVEQGTIKV 290
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 240 GEEVEIVGIKE--TQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSKDEG 317
Cdd:PLN03127  291 GEEVEIVGLRPggPLKTTVTGVEMFKKILDQGQAGDNVGLLLRGLKREDVQRGQVICKPGSIKTYKKFEAEIYVLTKDEG 370
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383508603 318 GRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:PLN03127  371 GRHTPFFSNYRPQFYLRTADVTGKVELPEGVKMVMPGDNVTAVFELISPVPLEPGQRFALREGGRTVG 438
PLN03126 PLN03126
Elongation factor Tu; Provisional
2-385 0e+00

Elongation factor Tu; Provisional


Pssm-ID: 215592 [Multi-domain]  Cd Length: 478  Bit Score: 592.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   2 SKEKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVD 81
Cdd:PLN03126   71 ARGKFERKKPHVNIGTIGHVDHGKTTLTAALTMALASMGGSAPKKYDEIDAAPEERARGITINTATVEYETENRHYAHVD 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQY 161
Cdd:PLN03126  151 CPGHADYVKNMITGAAQMDGAILVVSGADGPMPQTKEHILLAKQVGVPNMVVFLNKQDQVDDEELLELVELEVRELLSSY 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 162 DFPGDDTPIVRGSALKALE----------GDAEWEAKIIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGR 231
Cdd:PLN03126  231 EFPGDDIPIISGSALLALEalmenpnikrGDNKWVDKIYELMDAVDSYIPIPQRQTDLPFLLAVEDVFSITGRGTVATGR 310
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 232 VERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYI 311
Cdd:PLN03126  311 VERGTVKVGETVDIVGLRETRSTTVTGVEMFQKILDEALAGDNVGLLLRGIQKADIQRGMVLAKPGSITPHTKFEAIVYV 390
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1383508603 312 LSKDEGGRHTPFFKGYRPQFYFRTTDVTGTI-----ELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIREGGRTVG 385
Cdd:PLN03126  391 LKKEEGGRHSPFFAGYRPQFYMRTTDVTGKVtsimnDKDEESKMVMPGDRVKMVVELIVPVACEQGMRFAIREGGKTVG 469
EF_Tu cd01884
Elongation Factor Tu (EF-Tu) GTP-binding proteins; EF-Tu subfamily. This subfamily includes ...
11-203 3.19e-132

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: 376.54  E-value: 3.19e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVK 90
Cdd:cd01884     1 PHVNVGTIGHVDHGKTTLTAAITKVLAKKGGAKAKKYDEIDKAPEEKARGITINTAHVEYETANRHYAHVDCPGHADYIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  91 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPI 170
Cdd:cd01884    81 NMITGAAQMDGAILVVSATDGPMPQTREHLLLARQVGVPYIVVFLNKADMVDDEELLELVEMEVRELLSKYGFDGDDTPI 160
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1383508603 171 VRGSALKALEGD--AEWEAKIIELAGFLDSYIPEP 203
Cdd:cd01884   161 VRGSALKALEGDdpNKWVDKILELLDALDSYIPTP 195
GTP_EFTU pfam00009
Elongation factor Tu GTP binding domain; This domain contains a P-loop motif, also found in ...
10-201 4.94e-79

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: 240.89  E-value: 4.94e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  10 KPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHA 86
Cdd:pfam00009   1 KRHRNIGIIGHVDHGKTTLTDRLLYYTGAISKRGEVKGEGeagLDNLPEERERGITIKSAAVSFETKDYLINLIDTPGHV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSQYDFPGD 166
Cdd:pfam00009  81 DFVKEVIRGLAQADGAILVVDAVEGVMPQTREHLRLARQLGVP-IIVFINKMDRVDGAELEEVVEEVSRELLEKYGEDGE 159
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1383508603 167 DTPIVRGSALKALegdaeweaKIIELAGFLDSYIP 201
Cdd:pfam00009 160 FVPVVPGSALKGE--------GVQTLLDALDEYLP 186
TEF1 COG5256
Translation elongation factor EF-1alpha (GTPase) [Translation, ribosomal structure and ...
8-385 9.69e-77

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: 243.30  E-value: 9.69e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   8 RTKPHVNVGTIGHVDHGKTTL-------TAAITTVLAKTYGGAARAFDQ--------IDNAPEEKARGITINTSHVEYDT 72
Cdd:COG5256     3 SEKPHLNLVVIGHVDHGKSTLvgrllyeTGAIDEHIIEKYEEEAEKKGKesfkfawvMDRLKEERERGVTIDLAHKKFET 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  73 PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVD-DEELLELVE 151
Cdd:COG5256    83 DKYYFTIIDAPGHRDFVKNMITGASQADAAILVVSAKDGVMGQTREHAFLARTLGINQLIVAVNKMDAVNySEKRYEEVK 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 152 MEVRELLSQYDFPGDDTPIVRGSALKaleGDaeweaKIIE------------LAGFLDSyIPEPERAIDKPFLLPIEDVF 219
Cdd:COG5256   163 EEVSKLLKMVGYKVDKIPFIPVSAWK---GD-----NVVKksdnmpwyngptLLEALDN-LKEPEKPVDKPLRIPIQDVY 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 220 SISGRGTVVTGRVERGIIKVGEEVEIV--GIKETQKStctgVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPG 297
Cdd:COG5256   234 SISGIGTVPVGRVETGVLKVGDKVVFMpaGVVGEVKS----IEMHHEELEQAEPGDNIGFNVRGVEKNDIKRGDVAGHPD 309
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 298 tiKPHT---KFESEVYILskdeggRH-TPFFKGYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIKMV 360
Cdd:COG5256   310 --NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHVHTAQVACTFVelvskldprtgqvKEENPQFLKTGDAAIVK 381
                         410       420       430
                  ....*....|....*....|....*....|..
gi 1383508603 361 VTLIHPIAMDD-------GlRFAIREGGRTVG 385
Cdd:COG5256   382 IKPTKPLVIEKfkefpqlG-RFAIRDMGQTVA 412
PRK12317 PRK12317
elongation factor 1-alpha; Reviewed
8-385 1.52e-74

elongation factor 1-alpha; Reviewed


Pssm-ID: 237055 [Multi-domain]  Cd Length: 425  Bit Score: 237.52  E-value: 1.52e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   8 RTKPHVNVGTIGHVDHGKTTL-------TAAITTVL-------AKTYGGAARAFDQI-DNAPEEKARGITINTSHVEYDT 72
Cdd:PRK12317    2 KEKPHLNLAVIGHVDHGKSTLvgrllyeTGAIDEHIieelreeAKEKGKESFKFAWVmDRLKEERERGVTIDLAHKKFET 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  73 PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATD--GPMPQTREHILLGRQVGVPYIIVFLNKCDMVD-DEELLEL 149
Cdd:PRK12317   82 DKYYFTIVDCPGHRDFVKNMITGASQADAAVLVVAADDagGVMPQTREHVFLARTLGINQLIVAINKMDAVNyDEKRYEE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 150 VEMEVRELLSQYDFPGDDTPIVRGSalkALEGDaeweaKIIE------------LAGFLDSyIPEPERAIDKPFLLPIED 217
Cdd:PRK12317  162 VKEEVSKLLKMVGYKPDDIPFIPVS---AFEGD-----NVVKksenmpwyngptLLEALDN-LKPPEKPTDKPLRIPIQD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 218 VFSISGRGTVVTGRVERGIIKVGEEV--EIVGIKETQKStctgVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAK 295
Cdd:PRK12317  233 VYSISGVGTVPVGRVETGVLKVGDKVvfMPAGVVGEVKS----IEMHHEELPQAEPGDNIGFNVRGVGKKDIKRGDVCGH 308
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 296 PGtiKPHT---KFESEVYILskdeggRH-TPFFKGYRPQFYFRTTDVTGTIE-------------LPEGVEMVMPGDNIK 358
Cdd:PRK12317  309 PD--NPPTvaeEFTAQIVVL------QHpSAITVGYTPVFHAHTAQVACTFEelvkkldprtgqvAEENPQFIKTGDAAI 380
                         410       420       430
                  ....*....|....*....|....*....|....
gi 1383508603 359 MVVTLIHPIAMDD-------GlRFAIREGGRTVG 385
Cdd:PRK12317  381 VKIKPTKPLVIEKvkeipqlG-RFAIRDMGQTIA 413
SelB COG3276
Selenocysteine-specific translation elongation factor SelB [Translation, ribosomal structure ...
13-385 3.67e-62

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: 210.54  E-value: 3.67e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  13 VNVGTIGHVDHGKTTLTAAITTVLAktyggaarafdqiDNAPEEKARGITINTShveydtptrhYAH-----------VD 81
Cdd:COG3276     1 MIIGTAGHIDHGKTTLVKALTGIDT-------------DRLKEEKKRGITIDLG----------FAYlplpdgrrlgfVD 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  82 CPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQY 161
Cdd:COG3276    58 VPGHEKFIKNMLAGAGGIDLVLLVVAADEGVMPQTREHLAILDLLGIKRGIVVLTKADL-VDEEWLELVEEEIRELLAGT 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 162 DFPgdDTPIVRGSAlKALEGDAEWEAKIIELAGfldsyiPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGE 241
Cdd:COG3276   137 FLE--DAPIVPVSA-VTGEGIDELRAALDALAA------AVPARDADGPFRLPIDRVFSIKGFGTVVTGTLLSGTVRVGD 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 242 EVEIVGIKetQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPGTIKPHTKFESEVYILSkdegGRHT 321
Cdd:COG3276   208 ELELLPSG--KPVRVRGIQVHGQPVEEAYAGQRVALNLAGVEKEEIERGDVLAAPGALRPTDRIDVRLRLLP----SAPR 281
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383508603 322 PFFKGYRPQFYFRTTDVTGTIELPEGVEMVmPGDniKMVVTLI--HPIAMDDGLRFAIREGG--RTVG 385
Cdd:COG3276   282 PLKHWQRVHLHHGTAEVLARVVLLDREELA-PGE--EALAQLRleEPLVAARGDRFILRDYSprRTIG 346
EFTU_III cd03707
Domain III of Elongation Factor (EF) Tu; EF-Tu consists of three structural domains, ...
300-385 4.03e-62

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: 194.27  E-value: 4.03e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 300 KPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIRE 379
Cdd:cd03707     1 KPHTKFEAEVYVLTKEEGGRHTPFFSGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNVKMTVELIHPIALEEGLRFAIRE 80

                  ....*.
gi 1383508603 380 GGRTVG 385
Cdd:cd03707    81 GGRTVG 86
GTP_translation_factor cd00881
GTP translation factor family primarily contains translation initiation, elongation and ...
14-203 1.23e-56

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: 183.27  E-value: 1.23e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMI 93
Cdd:cd00881     1 NVGVIGHVDHGKTTLTGSLLYQTGAIDRRGTRKETFLDTLKEERERGITIKTGVVEFEWPKRRINFIDTPGHEDFSKETV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  94 TGAAQMDGAILVVAATDGPMPQTREHILLGRQvGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDF---PGDDTPI 170
Cdd:cd00881    81 RGLAQADGALLVVDANEGVEPQTREHLNIALA-GGLPIIVAVNKIDR-VGEEDFDEVLREIKELLKLIGFtflKGKDVPI 158
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1383508603 171 VRGSALKALEGDaeweakiiELAGFLDSYIPEP 203
Cdd:cd00881   159 IPISALTGEGIE--------ELLDAIVEHLPPP 183
EFTU_II cd03697
Domain II of elongation factor Tu; Elongation factors Tu (EF-Tu) are three-domain GTPases with ...
211-297 2.67e-52

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: 168.85  E-value: 2.67e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 211 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERG 290
Cdd:cd03697     1 FLMPIEDVFSIPGRGTVVTGRIERGVIKVGDEVEIVGFKETLKTTVTGIEMFRKTLDEAEAGDNVGVLLRGVKKEDVERG 80

                  ....*..
gi 1383508603 291 QVLAKPG 297
Cdd:cd03697    81 MVLAKPG 87
PTZ00141 PTZ00141
elongation factor 1- alpha; Provisional
1-312 4.22e-51

elongation factor 1- alpha; Provisional


Pssm-ID: 185474 [Multi-domain]  Cd Length: 446  Bit Score: 176.86  E-value: 4.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKfertkPHVNVGTIGHVDHGKTTLTAAIttvLAKTYGGAARAFDQ------------------IDNAPEEKARGIT 62
Cdd:PTZ00141    1 MGKEK-----THINLVVIGHVDSGKSTTTGHL---IYKCGGIDKRTIEKfekeaaemgkgsfkyawvLDKLKAERERGIT 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  63 INTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLGRQVGVPYIIVFL 135
Cdd:PTZ00141   73 IDIALWKFETPKYYFTIIDAPGHRDFIKNMITGTSQADVAILVVASTAGEFEagiskdgQTREHALLAFTLGVKQMIVCI 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 136 NKCDMVDDEELLELVEMEVRELLSQYDFPGDDTPIVRGSALKALEGDAEWEaKIIELAGF--------LDSYIPePERAI 207
Cdd:PTZ00141  153 NKMDDKTVNYSQERYDEIKKEVSAYLKKVGYNPEKVPFIPISGWQGDNMIE-KSDNMPWYkgptlleaLDTLEP-PKRPV 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 208 DKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETqkSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEI 287
Cdd:PTZ00141  231 DKPLRLPLQDVYKIGGIGTVPVGRVETGILKPGMVVTFAPSGVT--TEVKSVEMHHEQLAEAVPGDNVGFNVKNVSVKDI 308
                         330       340
                  ....*....|....*....|....*..
gi 1383508603 288 ERGQVL--AKPGTIKPHTKFESEVYIL 312
Cdd:PTZ00141  309 KRGYVAsdSKNDPAKECADFTAQVIVL 335
selB TIGR00475
selenocysteine-specific elongation factor SelB; In prokaryotes, the incorporation of ...
13-383 1.77e-49

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: 175.45  E-value: 1.77e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  13 VNVGTIGHVDHGKTTLTAAITTVLAktyggaarafdqiDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNM 92
Cdd:TIGR00475   1 MIIATAGHVDHGKTTLLKALTGIAA-------------DRLPEEKKRGMTIDLGFAYFPLPDYRLGFIDVPGHEKFISNA 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  93 ITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDmVDDEELLELVEMEVRELLSQYDFpGDDTPIVR 172
Cdd:TIGR00475  68 IAGGGGIDAALLVVDADEGVMTQTGEHLAVLDLLGIPHTIVVITKAD-RVNEEEIKRTEMFMKQILNSYIF-LKNAKIFK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 173 GSAlKALEGDAEWEAKIIELAGFLDSyipepeRAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIkeTQ 252
Cdd:TIGR00475 146 TSA-KTGQGIGELKKELKNLLESLDI------KRIQKPLRMAIDRAFKVKGAGTVVTGTAFSGEVKVGDNLRLLPI--NH 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 253 KSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLAKPgtikPHTKFESEVYILSkdeggrHTPFFKGYRPQFY 332
Cdd:TIGR00475 217 EVRVKAIQAQNQDVEIAYAGQRIALNLMDVEPESLKRGLLILTP----EDPKLRVVVKFIA------EVPLLELQPYHIA 286
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1383508603 333 FRTTDVTGTIELPEgvemvmpgDNIKMvVTLIHPIAMDDGLRFAIREGGRT 383
Cdd:TIGR00475 287 HGMSVTTGKISLLD--------KGIAL-LTLDAPLILAKGDKLVLRDSSGN 328
GTP_EFTU_D3 pfam03143
Elongation factor Tu C-terminal domain; Elongation factor Tu consists of three structural ...
298-385 2.40e-44

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: 148.95  E-value: 2.40e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 298 TIKPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIE------LPEGV----EMVMPGDNIKMVVTLIHPI 367
Cdd:pfam03143   1 PIKPHTKFEAQVYILNKEEGGRHTPFFNGYRPQFYFRTADVTGKFVellhklDPGGVsenpEFVMPGDNVIVTVELIKPI 80
                          90
                  ....*....|....*...
gi 1383508603 368 AMDDGLRFAIREGGRTVG 385
Cdd:pfam03143  81 ALEKGQRFAIREGGRTVA 98
eif2g_arch TIGR03680
translation initiation factor 2 subunit gamma; This model represents the archaeal translation ...
11-314 1.48e-41

translation initiation factor 2 subunit gamma; This model represents the archaeal translation initiation factor 2 subunit gamma and is found in all known archaea. eIF-2 functions in the early steps of protein synthesis by forming a ternary complex with GTP and initiator tRNA.


Pssm-ID: 274720 [Multi-domain]  Cd Length: 406  Bit Score: 150.59  E-value: 1.48e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  11 PHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgaarafdqidnapEEKARGITINTSHVE---YDTPT------------- 74
Cdd:TIGR03680   3 PEVNIGMVGHVDHGKTTLTKALTGVWTDTHS-------------EELKRGISIRLGYADaeiYKCPEcdgpecyttepvc 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  75 ----------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMvdd 143
Cdd:TIGR03680  70 pncgsetellRRVSFVDAPGHETLMATMLSGAALMDGALLVIAANEPcPQPQTKEHLMALEIIGIKNIVIVQNKIDL--- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 144 eellelveMEVRELLSQYD--------FPGDDTPIVRGSALKALEGDAEWEAkiielagfLDSYIPEPERAIDKPFLLPI 215
Cdd:TIGR03680 147 --------VSKEKALENYEeikefvkgTVAENAPIIPVSALHNANIDALLEA--------IEKFIPTPERDLDKPPLMYV 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 216 EDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIKETQK---------STCTGVEMFRKLLDEGRAGENVGV 277
Cdd:TIGR03680 211 ARSFDVNKPGTppeklkggVIGGSLIQGKLKVGDEIEIRpGIKVEKGgktkwepiyTEITSLRAGGYKVEEARPGGLVGV 290
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1383508603 278 ---LLRGIKREEIERGQVLAKPGTIKP-HTKFESEVYILSK 314
Cdd:TIGR03680 291 gtkLDPALTKADALAGQVVGKPGTLPPvWESLELEVHLLER 331
PLN00043 PLN00043
elongation factor 1-alpha; Provisional
1-385 2.49e-38

elongation factor 1-alpha; Provisional


Pssm-ID: 165621 [Multi-domain]  Cd Length: 447  Bit Score: 142.92  E-value: 2.49e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFertkpHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFDQ---------------IDNAPEEKARGITINT 65
Cdd:PLN00043    1 MGKEKV-----HINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKeaaemnkrsfkyawvLDKLKAERERGITIDI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  66 SHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMP-------QTREHILLGRQVGVPYIIVFLNKC 138
Cdd:PLN00043   76 ALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEagiskdgQTREHALLAFTLGVKQMICCCNKM 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 139 DMVDDEELLELVEMEVREL---LSQYDFPGDDTPIVrgsALKALEGDaeweaKIIELAGFLDSY-----------IPEPE 204
Cdd:PLN00043  156 DATTPKYSKARYDEIVKEVssyLKKVGYNPDKIPFV---PISGFEGD-----NMIERSTNLDWYkgptllealdqINEPK 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 205 RAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI--VGIKETQKStctgVEMFRKLLDEGRAGENVGVLLRGI 282
Cdd:PLN00043  228 RPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFgpTGLTTEVKS----VEMHHESLQEALPGDNVGFNVKNV 303
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 283 KREEIERGQVL--AKPGTIKPHTKFESEVYILSK--DEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEM------VM 352
Cdd:PLN00043  304 AVKDLKRGYVAsnSKDDPAKEAANFTSQVIIMNHpgQIGNGYAPVLDCHTSHIAVKFAEILTKIDRRSGKELekepkfLK 383
                         410       420       430
                  ....*....|....*....|....*....|....*....
gi 1383508603 353 PGDN--IKMVVT---LIHPIAMDDGL-RFAIREGGRTVG 385
Cdd:PLN00043  384 NGDAgfVKMIPTkpmVVETFSEYPPLgRFAVRDMRQTVA 422
EF1_alpha cd01883
Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent ...
14-139 3.53e-38

Elongation Factor 1-alpha (EF1-alpha) protein family; EF1 is responsible for the GTP-dependent binding of aminoacyl-tRNAs to the ribosomes. EF1 is composed of four subunits: the alpha chain which binds GTP and aminoacyl-tRNAs, the gamma chain that probably plays a role in anchoring the complex to other cellular components and the beta and delta (or beta') chains. This subfamily is the alpha subunit, and represents the counterpart of bacterial EF-Tu for the archaea (aEF1-alpha) and eukaryotes (eEF1-alpha). eEF1-alpha interacts with the actin of the eukaryotic cytoskeleton and may thereby play a role in cellular transformation and apoptosis. EF-Tu can have no such role in bacteria. In humans, the isoform eEF1A2 is overexpressed in 2/3 of breast cancers and has been identified as a putative oncogene. This subfamily also includes Hbs1, a G protein known to be important for efficient growth and protein synthesis under conditions of limiting translation initiation in yeast, and to associate with Dom34. It has been speculated that yeast Hbs1 and Dom34 proteins may function as part of a complex with a role in gene expression.


Pssm-ID: 206670 [Multi-domain]  Cd Length: 219  Bit Score: 136.47  E-value: 3.53e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAITTVL--------------AKTYGGAARAFDQI-DNAPEEKARGITINTSHVEYDTPTRHYA 78
Cdd:cd01883     1 NLVVIGHVDAGKSTLTGHLLYKLggvdkrtiekyekeAKEMGKESFKYAWVlDKLKEERERGVTIDVGLAKFETEKYRFT 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1383508603  79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDG-------PMPQTREHILLGRQVGVPYIIVFLNKCD 139
Cdd:cd01883    81 IIDAPGHRDFVKNMITGASQADVAVLVVSARKGefeagfeKGGQTREHALLARTLGVKQLIVAVNKMD 148
PRK04000 PRK04000
translation initiation factor IF-2 subunit gamma; Validated
7-314 9.01e-38

translation initiation factor IF-2 subunit gamma; Validated


Pssm-ID: 235194 [Multi-domain]  Cd Length: 411  Bit Score: 140.37  E-value: 9.01e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   7 ERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgaarafdqidnapEEKARGITI-------------NTSHVEYDTP 73
Cdd:PRK04000    4 EKVQPEVNIGMVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIrlgyadatirkcpDCEEPEAYTT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  74 T-------------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCD 139
Cdd:PRK04000   71 EpkcpncgsetellRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKID 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 140 MvddeellelveMEVRELLSQY----DFP----GDDTPIVRGSALKALEGDAeweakiieLAGFLDSYIPEPERAIDKPF 211
Cdd:PRK04000  151 L-----------VSKERALENYeqikEFVkgtvAENAPIIPVSALHKVNIDA--------LIEAIEEEIPTPERDLDKPP 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 212 LLPIEDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIKETQK---------STCTGVEMFRKLLDEGRAGE 273
Cdd:PRK04000  212 RMYVARSFDVNKPGTppeklkggVIGGSLIQGVLKVGDEIEIRpGIKVEEGgktkwepitTKIVSLRAGGEKVEEARPGG 291
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1383508603 274 NVGV---LLRGIKREEIERGQVLAKPGTIKP-HTKFESEVYILSK 314
Cdd:PRK04000  292 LVGVgtkLDPSLTKADALAGSVAGKPGTLPPvWESLTIEVHLLER 336
GTPBP1 COG5258
GTPase [General function prediction only];
4-385 1.40e-35

GTPase [General function prediction only];


Pssm-ID: 444076 [Multi-domain]  Cd Length: 531  Bit Score: 136.60  E-value: 1.40e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   4 EKFERTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGGAARAFdqIDNAPEEKARGITINTSH----------VEYDTP 73
Cdd:COG5258   114 EGKEKDPEHIVVGVAGHVDHGKSTLVGTLVTGKLDDGNGGTRSF--LDVQPHEVERGLSADLSYavygfdddgpVRMKNP 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  74 TRHY-------------AHVDCPGHADYVKNMITG--AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKC 138
Cdd:COG5258   192 LRKTdrarvveesdklvSFVDTVGHEPWLRTTIRGlvGQKLDYGLLVVAADDGPTHTTREHLGILLAMDLPVIVA-ITKI 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 139 DMvDDEELLELVEMEVRELLSQYdfpgDDTPIV---RGSALKALEGDAEWEAKIIE-----------LAGFLDSyIPEPE 204
Cdd:COG5258   271 DK-VDDERVEEVEREIENLLRIV----GRTPLEvesRHDVDAAIEEINGRVVPILKtsavtgegldlLDELFER-LPKRA 344
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 205 RAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI--VGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGI 282
Cdd:COG5258   345 TDEDEPFLMYIDRIYNVTGVGTVVSGTVKSGKVEAGDELLIgpTKDGSFREVEVKSIEMHYHRVDKAEAGRIVGIALKGV 424
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 283 KREEIERGQVLAKPGTI-KPHTKFESEVYILSkdeggrH-TPFFKGYRPQFYFRTTDVTGTIElPEGVEMVMPGDNIKMV 360
Cdd:COG5258   425 EEEELERGMVLLPRDADpKAVREFEAEVMVLN------HpTTIKEGYEPVVHLETISEAVRFE-PIDKGYLLPGDSGRVR 497
                         410       420
                  ....*....|....*....|....*.
gi 1383508603 361 VT-LIHPIAMDDGLRFAIREgGRTVG 385
Cdd:COG5258   498 LRfKYRPYYVEEGQRFVFRE-GRSKG 522
SelB cd04171
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
15-193 1.66e-35

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec, and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains bacterial SelBs, as well as, one from archaea.


Pssm-ID: 206734 [Multi-domain]  Cd Length: 170  Bit Score: 128.11  E-value: 1.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  15 VGTIGHVDHGKTTLTAAITTVlaktyggaarafdQIDNAPEEKARGITINTSHVEYDTPT-RHYAHVDCPGHADYVKNMI 93
Cdd:cd04171     2 IGTAGHIDHGKTTLIKALTGI-------------ETDRLPEEKKRGITIDLGFAYLDLPDgKRLGFIDVPGHEKFVKNML 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  94 TGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMvDDEELLELVEMEVRELLSQYDFPgdDTPIVRG 173
Cdd:cd04171    69 AGAGGIDAVLLVVAADEGIMPQTREHLEILELLGIKKGLVVLTKADL-VDEDRLELVEEEILELLAGTFLA--DAPIFPV 145
                         170       180
                  ....*....|....*....|
gi 1383508603 174 SALKAlEGDAEWEAKIIELA 193
Cdd:cd04171   146 SSVTG-EGIEELKNYLDELA 164
GCD11 COG5257
Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal ...
8-312 1.82e-35

Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) [Translation, ribosomal structure and biogenesis]; Translation initiation factor 2, gamma subunit (eIF-2gamma; GTPase) is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 444075 [Multi-domain]  Cd Length: 408  Bit Score: 134.19  E-value: 1.82e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   8 RTKPHVNVGTIGHVDHGKTTLTAAITTVLAKTYGgaarafdqidnapEEKARGITINTSHVE--------------YDT- 72
Cdd:COG5257     1 KKQPEVNIGVVGHVDHGKTTLVQALTGVWTDRHS-------------EELKRGITIRLGYADatfykcpnceppeaYTTe 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  73 -----------PTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDM 140
Cdd:COG5257    68 pkcpncgseteLLRRVSFVDAPGHETLMATMLSGAALMDGAILVIAANEPcPQPQTKEHLMALDIIGIKNIVIVQNKIDL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 141 vddeellelveMEVRELLSQY----DF----PGDDTPIVRGSALKALEGDAeweakiieLAGFLDSYIPEPERAIDKPFL 212
Cdd:COG5257   148 -----------VSKERALENYeqikEFvkgtVAENAPIIPVSAQHKVNIDA--------LIEAIEEEIPTPERDLSKPPR 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 213 LPIEDVFSISGRGT--------VVTGRVERGIIKVGEEVEIV-GIKETQK---------STCTGVEMFRKLLDEGRAGEN 274
Cdd:COG5257   209 MLVARSFDVNKPGTppkdlkggVIGGSLIQGVLKVGDEIEIRpGIKVEKGgktkyepitTTVVSLRAGGEEVEEAKPGGL 288
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 1383508603 275 VGV---LLRGIKREEIERGQVLAKPGTIKP-HTKFESEVYIL 312
Cdd:COG5257   289 VAVgtkLDPSLTKSDSLVGSVAGKPGTLPPvLDSLTMEVHLL 330
PRK10512 PRK10512
selenocysteinyl-tRNA-specific translation factor; Provisional
17-290 6.85e-35

selenocysteinyl-tRNA-specific translation factor; Provisional


Pssm-ID: 182508 [Multi-domain]  Cd Length: 614  Bit Score: 135.56  E-value: 6.85e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  17 TIGHVDHGKTTLTAAITTVLAktyggaarafdqiDNAPEEKARGITINTSHVEYDTPT-RHYAHVDCPGHADYVKNMITG 95
Cdd:PRK10512    5 TAGHVDHGKTTLLQAITGVNA-------------DRLPEEKKRGMTIDLGYAYWPQPDgRVLGFIDVPGHEKFLSNMLAG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  96 AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDmVDDEELLELVEMEVRELLSQYDFPgdDTPIVRGSA 175
Cdd:PRK10512   72 VGGIDHALLVVACDDGVMAQTREHLAILQLTGNPMLTVALTKAD-RVDEARIAEVRRQVKAVLREYGFA--EAKLFVTAA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 176 LKALegdaeweaKIIELAGFLdSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKst 255
Cdd:PRK10512  149 TEGR--------GIDALREHL-LQLPEREHAAQHRFRLAIDRAFTVKGAGLVVTGTALSGEVKVGDTLWLTGVNKPMR-- 217
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1383508603 256 CTGVEMFRKLLDEGRAGENVGVLLRG-IKREEIERG 290
Cdd:PRK10512  218 VRGLHAQNQPTEQAQAGQRIALNIAGdAEKEQINRG 253
mtEFTU_III cd03706
Domain III of mitochondrial EF-TU (mtEF-TU); mtEF-TU is highly conserved and is 55-60% ...
300-385 1.82e-32

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: 117.33  E-value: 1.82e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 300 KPHTKFESEVYILSKDEGGRHTPFFKGYRPQFYFRTTDVTGTIELPEGVEMVMPGDNIKMVVTLIHPIAMDDGLRFAIRE 379
Cdd:cd03706     1 KMHNHFEAQVYLLSKEEGGRHKPFTSGFQQQMFSKTWDCACRIDLPEGKEMVMPGEDTSVKLTLLKPMVLEKGQRFTLRE 80

                  ....*.
gi 1383508603 380 GGRTVG 385
Cdd:cd03706    81 GGRTIG 86
CysN COG2895
Sulfate adenylyltransferase subunit 1, EFTu-like GTPase family [Inorganic ion transport and ...
1-297 6.63e-32

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: 124.81  E-value: 6.63e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKPHVNVG-----TIGHVDHGKTTL-------TAAITT----VLAKTygGAARAFDQIDNAP------EEKA 58
Cdd:COG2895     1 MSTDIEAYLAQHENKDllrfiTCGSVDDGKSTLigrllydTKSIFEdqlaALERD--SKKRGTQEIDLALltdglqAERE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  59 RGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKC 138
Cdd:COG2895    79 QGITIDVAYRYFSTPKRKFIIADTPGHEQYTRNMVTGASTADLAILLIDARKGVLEQTRRHSYIASLLGIRHVVVAVNKM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 139 D---------------MvddeellelvemevRELLSQYDFPgDDTPIvrgsALKALEGDaeweaKIIE------------ 191
Cdd:COG2895   159 DlvdyseevfeeivadY--------------RAFAAKLGLE-DITFI----PISALKGD-----NVVErsenmpwydgpt 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 192 LAGFLDSyIPEPERAIDKPFLLPIEDV--FSISGRGtvVTGRVERGIIKVGEEVEIV--GiketQKSTCTGVEMFRKLLD 267
Cdd:COG2895   215 LLEHLET-VEVAEDRNDAPFRFPVQYVnrPNLDFRG--YAGTIASGTVRVGDEVVVLpsG----KTSTVKSIVTFDGDLE 287
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1383508603 268 EGRAGENVGVLLrgiKRE-EIERGQVLAKPG 297
Cdd:COG2895   288 EAFAGQSVTLTL---EDEiDISRGDVIVAAD 315
eIF2_gamma cd01888
Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation ...
13-205 1.82e-29

Gamma subunit of initiation factor 2 (eIF2 gamma); eIF2 is a heterotrimeric translation initiation factor that consists of alpha, beta, and gamma subunits. The GTP-bound gamma subunit also binds initiator methionyl-tRNA and delivers it to the 40S ribosomal subunit. Following hydrolysis of GTP to GDP, eIF2:GDP is released from the ribosome. The gamma subunit has no intrinsic GTPase activity, but is stimulated by the GTPase activating protein (GAP) eIF5, and GDP/GTP exchange is stimulated by the guanine nucleotide exchange factor (GEF) eIF2B. eIF2B is a heteropentamer, and the epsilon chain binds eIF2. Both eIF5 and eIF2B-epsilon are known to bind strongly to eIF2-beta, but have also been shown to bind directly to eIF2-gamma. It is possible that eIF2-beta serves simply as a high-affinity docking site for eIF5 and eIF2B-epsilon, or that eIF2-beta serves a regulatory role. eIF2-gamma is found only in eukaryotes and archaea. It is closely related to SelB, the selenocysteine-specific elongation factor from eubacteria. The translational factor components of the ternary complex, IF2 in eubacteria and eIF2 in eukaryotes are not the same protein (despite their unfortunately similar names). Both factors are GTPases; however, eubacterial IF-2 is a single polypeptide, while eIF2 is heterotrimeric. eIF2-gamma is a member of the same family as eubacterial IF2, but the two proteins are only distantly related. This family includes translation initiation, elongation, and release factors.


Pssm-ID: 206675 [Multi-domain]  Cd Length: 197  Bit Score: 112.75  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  13 VNVGTIGHVDHGKTTLTAAITTVlaktyggaarafdQIDNAPEEKARGITI-------------------NTSHVEYDTP 73
Cdd:cd01888     1 INIGTIGHVAHGKTTLVKALSGV-------------WTVRHKEELKRNITIklgyanakiykcpncgcprPYDTPECECP 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  74 T--------RHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKCDMVDDE 144
Cdd:cd01888    68 GcggetklvRHVSFVDCPGHEILMATMLSGAAVMDGALLLIAANEPcPQPQTSEHLAALEIMGLKHIIILQNKIDLVKEE 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1383508603 145 ellelvemevrELLSQYDF--------PGDDTPIVRGSALKalegdaewEAKIIELAGFLDSYIPEPER 205
Cdd:cd01888   148 -----------QALENYEQikefvkgtIAENAPIIPISAQL--------KYNIDVLCEYIVKKIPTPPR 197
SelB_euk cd01889
SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; ...
13-139 2.83e-28

SelB, the dedicated elongation factor for delivery of selenocysteinyl-tRNA to the ribosome; SelB is an elongation factor needed for the co-translational incorporation of selenocysteine. Selenocysteine is coded by a UGA stop codon in combination with a specific downstream mRNA hairpin. In bacteria, the C-terminal part of SelB recognizes this hairpin, while the N-terminal part binds GTP and tRNA in analogy with elongation factor Tu (EF-Tu). It specifically recognizes the selenocysteine charged tRNAsec, which has a UCA anticodon, in an EF-Tu like manner. This allows insertion of selenocysteine at in-frame UGA stop codons. In E. coli SelB binds GTP, selenocysteyl-tRNAsec and a stem-loop structure immediately downstream of the UGA codon (the SECIS sequence). The absence of active SelB prevents the participation of selenocysteyl-tRNAsec in translation. Archaeal and animal mechanisms of selenocysteine incorporation are more complex. Although the SECIS elements have different secondary structures and conserved elements between archaea and eukaryotes, they do share a common feature. Unlike in E. coli, these SECIS elements are located in the 3' UTRs. This group contains eukaryotic SelBs and some from archaea.


Pssm-ID: 206676 [Multi-domain]  Cd Length: 192  Bit Score: 109.38  E-value: 2.83e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  13 VNVGTIGHVDHGKTTLTAAITTVLAKTyggaarAFDQidnAPEEKARGITINT--SHVEYDTPTRHYAH----------- 79
Cdd:cd01889     1 VNVGLLGHVDSGKTSLAKALSEIASTA------AFDK---NPQSQERGITLDLgfSSFEVDKPKHLEDNenpqienyqit 71
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1383508603  80 -VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCD 139
Cdd:cd01889    72 lVDCPGHASLIRTIIGGAQIIDLMLLVVDAKKGIQTQTAECLVIGELLCKPLIVV-LNKID 131
PTZ00327 PTZ00327
eukaryotic translation initiation factor 2 gamma subunit; Provisional
13-245 5.97e-26

eukaryotic translation initiation factor 2 gamma subunit; Provisional


Pssm-ID: 240362 [Multi-domain]  Cd Length: 460  Bit Score: 108.55  E-value: 5.97e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  13 VNVGTIGHVDHGKTTLTAAITTVLAKTYggaarafdqidnaPEEKARGITIN-----------------------TSHVE 69
Cdd:PTZ00327   35 INIGTIGHVAHGKSTVVKALSGVKTVRF-------------KREKVRNITIKlgyanakiykcpkcprptcyqsyGSSKP 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  70 YDTP----------TRHYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDG-PMPQTREHILLGRQVGVPYIIVFLNKC 138
Cdd:PTZ00327  102 DNPPcpgcghkmtlKRHVSFVDCPGHDILMATMLNGAAVMDAALLLIAANEScPQPQTSEHLAAVEIMKLKHIIILQNKI 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 139 DMVDDEellelvemevrELLSQY----DF----PGDDTPIVRGSALKALEGDAeweakiieLAGFLDSYIPEPERAIDKP 210
Cdd:PTZ00327  182 DLVKEA-----------QAQDQYeeirNFvkgtIADNAPIIPISAQLKYNIDV--------VLEYICTQIPIPKRDLTSP 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1383508603 211 FLL----------PIEDVFSIsgRGTVVTGRVERGIIKVGEEVEI 245
Cdd:PTZ00327  243 PRMivirsfdvnkPGEDIENL--KGGVAGGSILQGVLKVGDEIEI 285
CysN_ATPS cd04166
CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS ...
17-140 7.88e-26

CysN, together with protein CysD, forms the ATP sulfurylase (ATPS) complex; CysN_ATPS subfamily. CysN, together with protein CysD, form the ATP sulfurylase (ATPS) complex in some bacteria and lower eukaryotes. ATPS catalyzes the production of ATP sulfurylase (APS) and pyrophosphate (PPi) from ATP and sulfate. CysD, which catalyzes ATP hydrolysis, is a member of the ATP pyrophosphatase (ATP PPase) family. CysN hydrolysis of GTP is required for CysD hydrolysis of ATP; however, CysN hydrolysis of GTP is not dependent on CysD hydrolysis of ATP. CysN is an example of lateral gene transfer followed by acquisition of new function. In many organisms, an ATPS exists which is not GTP-dependent and shares no sequence or structural similarity to CysN.


Pssm-ID: 206729 [Multi-domain]  Cd Length: 209  Bit Score: 103.42  E-value: 7.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  17 TIGHVDHGKTTL-------TAAI------TTVLAKTYGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHV 80
Cdd:cd04166     4 TCGSVDDGKSTLigrllydSKSIfedqlaALERSKSSGTQGEKLDLallVDGLQAEREQGITIDVAYRYFSTPKRKFIIA 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  81 DCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDM 140
Cdd:cd04166    84 DTPGHEQYTRNMVTGASTADLAILLVDARKGVLEQTRRHSYIASLLGIRHVVVAVNKMDL 143
TypA COG1217
Predicted membrane GTPase TypA/BipA involved in stress response [Signal transduction ...
14-301 1.77e-24

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


Pssm-ID: 440830 [Multi-domain]  Cd Length: 606  Bit Score: 105.10  E-value: 1.77e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAIttvLAKTygGAARAFDQI-----DNAPEEKARGITI---NTShVEY-DTptrhyaH---VD 81
Cdd:COG1217     8 NIAIIAHVDHGKTTLVDAL---LKQS--GTFRENQEVaervmDSNDLERERGITIlakNTA-VRYkGV------KiniVD 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  82 CPGHADY------VKNMItgaaqmDGAILVVAATDGPMPQTRehILLGR--QVGVPyIIVFLNKCDmvddeellelveme 153
Cdd:COG1217    76 TPGHADFggeverVLSMV------DGVLLLVDAFEGPMPQTR--FVLKKalELGLK-PIVVINKID-------------- 132
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 154 vR-------------ELL-------SQYDFpgddtPIVRGSalkALEGDA--EWEAK----------IIElagfldsYIP 201
Cdd:COG1217   133 -RpdarpdevvdevfDLFielgatdEQLDF-----PVVYAS---ARNGWAslDLDDPgedltplfdtILE-------HVP 196
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 202 EPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKST-CTGVEMFRKL----LDEGRAGENVG 276
Cdd:COG1217   197 APEVDPDGPLQMLVTNLDYSDYVGRIAIGRIFRGTIKKGQQVALIKRDGKVEKGkITKLFGFEGLerveVEEAEAGDIVA 276
                         330       340
                  ....*....|....*....|....*
gi 1383508603 277 VLlrGIkrEEIERGQVLAKPGTIKP 301
Cdd:COG1217   277 IA--GI--EDINIGDTICDPENPEA 297
TypA_BipA TIGR01394
GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, ...
14-296 9.09e-23

GTP-binding protein TypA/BipA; This bacterial (and Arabidopsis) protein, termed TypA or BipA, a GTP-binding protein, is phosphorylated on a tyrosine residue under some cellular conditions. Mutants show altered regulation of some pathways, but the precise function is unknown. [Regulatory functions, Other, Cellular processes, Adaptations to atypical conditions, Protein synthesis, Translation factors]


Pssm-ID: 273597 [Multi-domain]  Cd Length: 594  Bit Score: 100.07  E-value: 9.09e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAI---TTVLAKTYGGAARAFDQIDnapEEKARGITI---NTShVEYDtPTRhYAHVDCPGHAD 87
Cdd:TIGR01394   3 NIAIIAHVDHGKTTLVDALlkqSGTFRANEAVAERVMDSND---LERERGITIlakNTA-IRYN-GTK-INIVDTPGHAD 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  88 Y------VKNMItgaaqmDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEvrELL--- 158
Cdd:TIGR01394  77 FggeverVLGMV------DGVLLLVDASEGPMPQTRFVLKKALELGLK-PIVVINKIDRPSARPDEVVDEVF--DLFael 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 159 ----SQYDFpgddtPIVRGSALKALEG-DAEWEAKiiELAGFLDS---YIPEPERAIDKPFLLPIEDVFSISGRGTVVTG 230
Cdd:TIGR01394 148 gaddEQLDF-----PIVYASGRAGWASlDLDDPSD--NMAPLFDAivrHVPAPKGDLDEPLQMLVTNLDYDEYLGRIAIG 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1383508603 231 RVERGIIKVGEEVEIVGIKET-QKSTCTGVEMFRKL----LDEGRAGENVGVLlrGIkrEEIERGQVLAKP 296
Cdd:TIGR01394 221 RVHRGTVKKGQQVALMKRDGTiENGRISKLLGFEGLerveIDEAGAGDIVAVA--GL--EDINIGETIADP 287
IF2_eIF5B cd01887
Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B ...
19-193 6.90e-21

Initiation Factor 2 (IF2)/ eukaryotic Initiation Factor 5B (eIF5B) family; IF2/eIF5B contribute to ribosomal subunit joining and function as GTPases that are maximally activated by the presence of both ribosomal subunits. As seen in other GTPases, IF2/IF5B undergoes conformational changes between its GTP- and GDP-bound states. Eukaryotic IF2/eIF5Bs possess three characteristic segments, including a divergent N-terminal region followed by conserved central and C-terminal segments. This core region is conserved among all known eukaryotic and archaeal IF2/eIF5Bs and eubacterial IF2s.


Pssm-ID: 206674 [Multi-domain]  Cd Length: 169  Bit Score: 88.68  E-value: 6.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  19 GHVDHGKTTLTAAITtvlaKTyggaarafdqidNAPEEKARGIT--INTSHVEYDTPTRHYAHVDCPGHADYvKNMITGA 96
Cdd:cd01887     7 GHVDHGKTTLLDKIR----KT------------NVAAGEAGGITqhIGAYQVPIDVKIPGITFIDTPGHEAF-TNMRARG 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  97 AQM-DGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvdDEELLELVEMEVRELLSQYDFPGDD----TPIV 171
Cdd:cd01887    70 ASVtDIAILVVAADDGVMPQTIEAINHAKAANVP-IIVAINKID---KPYGTEADPERVKNELSELGLVGEEwggdVSIV 145
                         170       180
                  ....*....|....*....|..
gi 1383508603 172 RGSALKAlEGDAEWEAKIIELA 193
Cdd:cd01887   146 PISAKTG-EGIDDLLEAILLLA 166
SelB_II cd03696
Domain II of elongation factor SelB; This subfamily represents the domain of elongation factor ...
211-295 2.29e-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: 84.50  E-value: 2.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 211 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKStcTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERG 290
Cdd:cd03696     1 FRLPIDHVFSIKGAGTVVTGTVLSGKVKVGDELEIPPLGKEVRV--RSIQVHDKPVEEAKAGDRVALNLTGVDAKELERG 78

                  ....*
gi 1383508603 291 QVLAK 295
Cdd:cd03696    79 FVLSE 83
EF1_alpha_II cd03693
Domain II of elongation factor 1-alpha; This family represents domain II of elongation factor ...
207-292 2.87e-20

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: 84.55  E-value: 2.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 207 IDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIvgiketQKSTCTG----VEMFRKLLDEGRAGENVGVLLRGI 282
Cdd:cd03693     1 TDKPLRLPIQDVYKIGGIGTVPVGRVETGILKPGMVVTF------APAGVTGevksVEMHHEPLEEAIPGDNVGFNVKGV 74
                          90
                  ....*....|
gi 1383508603 283 KREEIERGQV 292
Cdd:cd03693    75 SVKDIKRGDV 84
CysN TIGR02034
sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic ...
17-296 1.29e-19

sulfate adenylyltransferase, large subunit; Metabolic assimilation of sulfur from inorganic sulfate, requires sulfate activation by coupling to a nucleoside, for the production of high-energy nucleoside phosphosulfates. This pathway appears to be similar in all prokaryotic organisms. Activation is first achieved through sulfation of sulfate with ATP by sulfate adenylyltransferase (ATP sulfurylase) to produce 5'-phosphosulfate (APS), coupled by GTP hydrolysis. Subsequently, APS is phosphorylated by an APS kinase to produce 3'-phosphoadenosine-5'-phosphosulfate (PAPS). In Escherichia coli, ATP sulfurylase is a heterodimer composed of two subunits encoded by cysD and cysN, with APS kinase encoded by cysC. These genes are located in a unidirectionally transcribed gene cluster, and have been shown to be required for the synthesis of sulfur-containing amino acids. Homologous to this E.coli activation pathway are nodPQH gene products found among members of the Rhizobiaceae family. These gene products have been shown to exhibit ATP sulfurase and APS kinase activity, yet are involved in Nod factor sulfation, and sulfation of other macromolecules. With members of the Rhizobiaceae family, nodQ often appears as a fusion of cysN (large subunit of ATP sulfurase) and cysC (APS kinase). [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 213679 [Multi-domain]  Cd Length: 406  Bit Score: 89.74  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  17 TIGHVDHGKTTLT---------------AAITTVLAK--TYGGAARAFDQIDNAPEEKARGITINTSHVEYDTPTRHYAH 79
Cdd:TIGR02034   5 TCGSVDDGKSTLIgrllhdtkqiyedqlAALERDSKKhgTQGGEIDLALLVDGLQAEREQGITIDVAYRYFSTDKRKFIV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELL-ELVEMEVRELL 158
Cdd:TIGR02034  85 ADTPGHEQYTRNMATGASTADLAVLLVDARKGVLEQTRRHSYIASLLGIRHVVLAVNKMDLVDYDEEVfENIKKDYLAFA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 159 SQYDFpGDDTPIvrgsALKALEGD--------AEWEAKIIeLAGFLDSYIPEPERAiDKPFLLPIEDVF--SISGRGtvV 228
Cdd:TIGR02034 165 EQLGF-RDVTFI----PLSALKGDnvvsrsesMPWYSGPT-LLEILETVEVERDAQ-DLPLRFPVQYVNrpNLDFRG--Y 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1383508603 229 TGRVERGIIKVGEEVEIVgiKETQKSTCTGVEMFRKLLDEGRAGENVGVLLrgiKRE-EIERGQVLAKP 296
Cdd:TIGR02034 236 AGTIASGSVHVGDEVVVL--PSGRSSRVARIVTFDGDLEQARAGQAVTLTL---DDEiDISRGDLLAAA 299
TypA_BipA cd01891
Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA ...
14-139 3.48e-19

Tyrosine phosphorylated protein A (TypA)/BipA family belongs to ribosome-binding GTPases; BipA is a protein belonging to the ribosome-binding family of GTPases and is widely distributed in bacteria and plants. BipA was originally described as a protein that is induced in Salmonella typhimurium after exposure to bactericidal/permeability-inducing protein (a cationic antimicrobial protein produced by neutrophils), and has since been identified in E. coli as well. The properties thus far described for BipA are related to its role in the process of pathogenesis by enteropathogenic E. coli. It appears to be involved in the regulation of several processes important for infection, including rearrangements of the cytoskeleton of the host, bacterial resistance to host defense peptides, flagellum-mediated cell motility, and expression of K5 capsular genes. It has been proposed that BipA may utilize a novel mechanism to regulate the expression of target genes. In addition, BipA from enteropathogenic E. coli has been shown to be phosphorylated on a tyrosine residue, while BipA from Salmonella and from E. coli K12 strains is not phosphorylated under the conditions assayed. The phosphorylation apparently modifies the rate of nucleotide hydrolysis, with the phosphorylated form showing greatly increased GTPase activity.


Pssm-ID: 206678 [Multi-domain]  Cd Length: 194  Bit Score: 84.57  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAITTvlaktYGGAARAFDQI-----DNAPEEKARGITI---NTShVEYDTPTRHYahVDCPGH 85
Cdd:cd01891     4 NIAIIAHVDHGKTTLVDALLK-----QSGTFRENEEVgervmDSNDLERERGITIlakNTA-ITYKDTKINI--IDTPGH 75
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1383508603  86 ADY------VKNMItgaaqmDGAILVVAATDGPMPQTRehILLGR--QVGVPyIIVFLNKCD 139
Cdd:cd01891    76 ADFggeverVLSMV------DGVLLLVDASEGPMPQTR--FVLKKalEAGLK-PIVVINKID 128
GTP_EFTU_D2 pfam03144
Elongation factor Tu domain 2; Elongation factor Tu consists of three structural domains, this ...
225-294 2.32e-18

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: 78.46  E-value: 2.32e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1383508603 225 GTVVTGRVERGIIKVGEEVEIVG---IKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIERGQVLA 294
Cdd:pfam03144   1 GTVATGRVESGTLKKGDKVRILPngtGKKKIVTRVTSLLMFHAPLREAVAGDNAGLILAGVGLEDIRVGDTLT 73
PRK05506 PRK05506
bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional
17-297 7.08e-18

bifunctional sulfate adenylyltransferase subunit 1/adenylylsulfate kinase protein; Provisional


Pssm-ID: 180120 [Multi-domain]  Cd Length: 632  Bit Score: 85.37  E-value: 7.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  17 TIGHVDHGKTTLT---------------AAITTVlAKTYGGAARAFD---QIDNAPEEKARGITINTSHVEYDTPTRHYA 78
Cdd:PRK05506   29 TCGSVDDGKSTLIgrllydskmifedqlAALERD-SKKVGTQGDEIDlalLVDGLAAEREQGITIDVAYRYFATPKRKFI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  79 HVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCDMVDDEELL-ELVEMEVREL 157
Cdd:PRK05506  108 VADTPGHEQYTRNMVTGASTADLAIILVDARKGVLTQTRRHSFIASLLGIRHVVLAVNKMDLVDYDQEVfDEIVADYRAF 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 158 LSQYDFPgDDTPIvrgsALKALEGDaeweaKIIE------------LAGFLDSYIPEPERAiDKPFLLPIEDV------F 219
Cdd:PRK05506  188 AAKLGLH-DVTFI----PISALKGD-----NVVTrsarmpwyegpsLLEHLETVEIASDRN-LKDFRFPVQYVnrpnldF 256
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 220 sisgRGtvVTGRVERGIIKVGEEVeiVGIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLrgikREEIE--RGQVLAKPG 297
Cdd:PRK05506  257 ----RG--FAGTVASGVVRPGDEV--VVLPSGKTSRVKRIVTPDGDLDEAFAGQAVTLTL----ADEIDisRGDMLARAD 324
EF2 cd01885
Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a ...
14-139 1.09e-17

Elongation Factor 2 (EF2) in archaea and eukarya; Translocation requires hydrolysis of a molecule of GTP and is mediated by EF-G in bacteria and by eEF2 in eukaryotes. The eukaryotic elongation factor eEF2 is a GTPase involved in the translocation of the peptidyl-tRNA from the A site to the P site on the ribosome. The 95-kDa protein is highly conserved, with 60% amino acid sequence identity between the human and yeast proteins. Two major mechanisms are known to regulate protein elongation and both involve eEF2. First, eEF2 can be modulated by reversible phosphorylation. Increased levels of phosphorylated eEF2 reduce elongation rates presumably because phosphorylated eEF2 fails to bind the ribosomes. Treatment of mammalian cells with agents that raise the cytoplasmic Ca2+ and cAMP levels reduce elongation rates by activating the kinase responsible for phosphorylating eEF2. In contrast, treatment of cells with insulin increases elongation rates by promoting eEF2 dephosphorylation. Second, the protein can be post-translationally modified by ADP-ribosylation. Various bacterial toxins perform this reaction after modification of a specific histidine residue to diphthamide, but there is evidence for endogenous ADP ribosylase activity. Similar to the bacterial toxins, it is presumed that modification by the endogenous enzyme also inhibits eEF2 activity.


Pssm-ID: 206672 [Multi-domain]  Cd Length: 218  Bit Score: 81.12  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAA-------ITTVLAktygGAARAfdqIDNAPEEKARGITINTSHV----EYDTPTRHYAH--- 79
Cdd:cd01885     2 NICIIAHVDHGKTTLSDSllasagiISEKLA----GKARY---LDTREDEQERGITIKSSAIslyfEYEEEKMDGNDyli 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1383508603  80 --VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTreHILLgRQVGVPYI--IVFLNKCD 139
Cdd:cd01885    75 nlIDSPGHVDFSSEVTAALRLTDGALVVVDAVEGVCVQT--ETVL-RQALEERVkpVLVINKID 135
PRK10218 PRK10218
translational GTPase TypA;
14-246 1.39e-17

translational GTPase TypA;


Pssm-ID: 104396 [Multi-domain]  Cd Length: 607  Bit Score: 84.38  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLtaaITTVLAKTYGGAARAFDQ---IDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVK 90
Cdd:PRK10218    7 NIAIIAHVDHGKTTL---VDKLLQQSGTFDSRAETQervMDSNDLEKERGITILAKNTAIKWNDYRINIVDTPGHADFGG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  91 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCDMVDDEELLELVEMEvrELLSQYDFPGD--DT 168
Cdd:PRK10218   84 EVERVMSMVDSVLLVVDAFDGPMPQTRFVTKKAFAYGLKPIVV-INKVDRPGARPDWVVDQVF--DLFVNLDATDEqlDF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 169 PIVRGSALKALEG-DAEWEAK-IIELAGFLDSYIPEPERAIDKPFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIV 246
Cdd:PRK10218  161 PIVYASALNGIAGlDHEDMAEdMTPLYQAIVDHVPAPDVDLDGPFQMQISQLDYNSYVGVIGIGRIKRGKVKPNQQVTII 240
TetM_like cd04168
Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline ...
14-139 1.86e-17

Tet(M)-like family includes Tet(M), Tet(O), Tet(W), and OtrA, containing tetracycline resistant proteins; Tet(M), Tet(O), Tet(W), and OtrA are tetracycline resistance genes found in Gram-positive and Gram-negative bacteria. Tetracyclines inhibit protein synthesis by preventing aminoacyl-tRNA from binding to the ribosomal acceptor site. This subfamily contains tetracycline resistance proteins that function through ribosomal protection and are typically found on mobile genetic elements, such as transposons or plasmids, and are often conjugative. Ribosomal protection proteins are homologous to the elongation factors EF-Tu and EF-G. EF-G and Tet(M) compete for binding on the ribosomes. Tet(M) has a higher affinity than EF-G, suggesting these two proteins may have overlapping binding sites and that Tet(M) must be released before EF-G can bind. Tet(M) and Tet(O) have been shown to have ribosome-dependent GTPase activity. These proteins are part of the GTP translation factor family, which includes EF-G, EF-Tu, EF2, LepA, and SelB.


Pssm-ID: 206731 [Multi-domain]  Cd Length: 237  Bit Score: 80.74  E-value: 1.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAIttvLAKTygGAARAFDQIDNAPE-------EKARGITINTSHVEYDTPTRHYAHVDCPGHA 86
Cdd:cd04168     1 NIGILAHVDAGKTTLTESL---LYTS--GAIRELGSVDKGTTrtdsmelERQRGITIFSAVASFQWEDTKVNIIDTPGHM 75
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1383508603  87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIvFLNKCD 139
Cdd:cd04168    76 DFIAEVERSLSVLDGAILVISAVEGVQAQTRILFRLLRKLNIPTII-FVNKID 127
IF-2 TIGR00487
translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) ...
9-243 2.26e-17

translation initiation factor IF-2; This model discriminates eubacterial (and mitochondrial) translation initiation factor 2 (IF-2), encoded by the infB gene in bacteria, from similar proteins in the Archaea and Eukaryotes. In the bacteria and in organelles, the initiator tRNA is charged with N-formyl-Met instead of Met. This translation factor acts in delivering the initator tRNA to the ribosome. It is one of a number of GTP-binding translation factors recognized by the pfam model GTP_EFTU. [Protein synthesis, Translation factors]


Pssm-ID: 273102 [Multi-domain]  Cd Length: 587  Bit Score: 83.66  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   9 TKPHVnVGTIGHVDHGKTTLTAAI--TTVLAKTYGGaarafdqidnapeekargIT--INTSHVEYDTpTRHYAHVDCPG 84
Cdd:TIGR00487  85 ERPPV-VTIMGHVDHGKTSLLDSIrkTKVAQGEAGG------------------ITqhIGAYHVENED-GKMITFLDTPG 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  85 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvddeeLLELVEMEVRELLSQYDFP 164
Cdd:TIGR00487 145 HEAFTSMRARGAKVTDIVVLVVAADDGVMPQTIEAISHAKAANVP-IIVAINKID------KPEANPDRVKQELSEYGLV 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 165 ----GDDTPIVRGSALKALEGDAEWEAkiIELAGFLDSYIPEPERAIDKPFLlpieDVFSISGRGTVVTGRVERGIIKVG 240
Cdd:TIGR00487 218 pedwGGDTIFVPVSALTGDGIDELLDM--ILLQSEVEELKANPNGQASGVVI----EAQLDKGRGPVATVLVQSGTLRVG 291

                  ...
gi 1383508603 241 EEV 243
Cdd:TIGR00487 292 DIV 294
FusA COG0480
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ...
1-139 1.33e-16

Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440248 [Multi-domain]  Cd Length: 693  Bit Score: 81.63  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   1 MSKEKFERTKphvNVGTIGHVDHGKTTLTAAI------TTVLAKTYGGAArafdQIDNAPEEKARGITINTS--HVEYDT 72
Cdd:COG0480     1 MAEYPLEKIR---NIGIVAHIDAGKTTLTERIlfytgaIHRIGEVHDGNT----VMDWMPEEQERGITITSAatTCEWKG 73
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1383508603  73 ptrhyaH----VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTrehILLGRQV---GVPyIIVFLNKCD 139
Cdd:COG0480    74 ------HkiniIDTPGHVDFTGEVERSLRVLDGAVVVFDAVAGVEPQT---ETVWRQAdkyGVP-RIVFVNKMD 137
EF-G_bact cd04170
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ...
14-139 2.28e-15

Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.


Pssm-ID: 206733 [Multi-domain]  Cd Length: 268  Bit Score: 75.32  E-value: 2.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAIttvLAKTygGAARAFDQIDN-------APEEKARGITINTS--HVEYDTpTRHYAhVDCPG 84
Cdd:cd04170     1 NIALVGHSGSGKTTLAEAL---LYAT--GAIDRLGRVEDgntvsdyDPEEKKRKMSIETSvaPLEWNG-HKINL-IDTPG 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1383508603  85 HADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 139
Cdd:cd04170    74 YADFVGETLSALRAVDAALIVVEAQSGVEVGTEKVWEFLDDAKLP-RIIFINKMD 127
PRK12740 PRK12740
elongation factor G-like protein EF-G2;
18-139 2.51e-15

elongation factor G-like protein EF-G2;


Pssm-ID: 237186 [Multi-domain]  Cd Length: 668  Bit Score: 77.47  E-value: 2.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  18 IGHVDHGKTTLTAAI------TTVLAKTYGGAARAfdqiDNAPEEKARGITINTS--HVEYDTpTRHYAhVDCPGHADYV 89
Cdd:PRK12740    1 VGHSGAGKTTLTEAIlfytgaIHRIGEVEDGTTTM----DFMPEERERGISITSAatTCEWKG-HKINL-IDTPGHVDFT 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1383508603  90 KNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 139
Cdd:PRK12740   75 GEVERALRVLDGAVVVVCAVGGVEPQTETVWRQAEKYGVP-RIIFVNKMD 123
PRK07560 PRK07560
elongation factor EF-2; Reviewed
14-139 2.56e-15

elongation factor EF-2; Reviewed


Pssm-ID: 236047 [Multi-domain]  Cd Length: 731  Bit Score: 77.60  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLT-----AA--ITTVLAktygGAARAFDQIDnapEEKARGITINTSHV----EYDTPTRHYAHVDC 82
Cdd:PRK07560   22 NIGIIAHIDHGKTTLSdnllaGAgmISEELA----GEQLALDFDE---EEQARGITIKAANVsmvhEYEGKEYLINLIDT 94
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1383508603  83 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTrEHILlgRQV---GV-PyiIVFLNKCD 139
Cdd:PRK07560   95 PGHVDFGGDVTRAMRAVDGAIVVVDAVEGVMPQT-ETVL--RQAlreRVkP--VLFINKVD 150
InfB COG0532
Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; ...
17-139 4.40e-15

Translation initiation factor IF-2, a GTPase [Translation, ribosomal structure and biogenesis]; Translation initiation factor IF-2, a GTPase is part of the Pathway/BioSystem: Translation factors


Pssm-ID: 440298 [Multi-domain]  Cd Length: 502  Bit Score: 76.59  E-value: 4.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  17 TI-GHVDHGKTTLTAAI--TTVLAKtyggaarafdqidnapeEkARGIT--INTSHVEydTPTRHYAHVDCPGHADYVKN 91
Cdd:COG0532     8 TVmGHVDHGKTSLLDAIrkTNVAAG-----------------E-AGGITqhIGAYQVE--TNGGKITFLDTPGHEAFTAM 67
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1383508603  92 MITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 139
Cdd:COG0532    68 RARGAQVTDIVILVVAADDGVMPQTIEAINHAKAAGVP-IIVAINKID 114
infB CHL00189
translation initiation factor 2; Provisional
15-241 8.93e-15

translation initiation factor 2; Provisional


Pssm-ID: 177089 [Multi-domain]  Cd Length: 742  Bit Score: 76.02  E-value: 8.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  15 VGTIGHVDHGKTTLTAAITtvlaKTyggaarafdqidNAPEEKARGIT--INTSHVEYD--TPTRHYAHVDCPGHADYVK 90
Cdd:CHL00189  247 VTILGHVDHGKTTLLDKIR----KT------------QIAQKEAGGITqkIGAYEVEFEykDENQKIVFLDTPGHEAFSS 310
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  91 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDmvddeeLLELVEMEVRELLSQYDFP----GD 166
Cdd:CHL00189  311 MRSRGANVTDIAILIIAADDGVKPQTIEAINYIQAANVP-IIVAINKID------KANANTERIKQQLAKYNLIpekwGG 383
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 167 DTPIVRGSALKALEGDAEWEAkIIELAGFLD-SYIPEP-------ERAIDKPfllpiedvfsisgRGTVVTGRVERGIIK 238
Cdd:CHL00189  384 DTPMIPISASQGTNIDKLLET-ILLLAEIEDlKADPTQlaqgiilEAHLDKT-------------KGPVATILVQNGTLH 449

                  ...
gi 1383508603 239 VGE 241
Cdd:CHL00189  450 IGD 452
PRK13351 PRK13351
elongation factor G-like protein;
14-139 1.04e-14

elongation factor G-like protein;


Pssm-ID: 237358 [Multi-domain]  Cd Length: 687  Bit Score: 75.76  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAITtvlakTYGGAARAFDQIDNA-------PEEKARGITINTSHVEYDTPTRHYAHVDCPGHA 86
Cdd:PRK13351   10 NIGILAHIDAGKTTLTERIL-----FYTGKIHKMGEVEDGttvtdwmPQEQERGITIESAATSCDWDNHRINLIDTPGHI 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1383508603  87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 139
Cdd:PRK13351   85 DFTGEVERSLRVLDGAVVVFDAVTGVQPQTETVWRQADRYGIP-RLIFINKMD 136
aEF-2 TIGR00490
translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a ...
3-139 3.07e-14

translation elongation factor aEF-2; This model represents archaeal elongation factor 2, a protein more similar to eukaryotic EF-2 than to bacterial EF-G, both in sequence similarity and in sharing with eukaryotes the property of having a diphthamide (modified His) residue at a conserved position. The diphthamide can be ADP-ribosylated by diphtheria toxin in the presence of NAD. [Protein synthesis, Translation factors]


Pssm-ID: 129581 [Multi-domain]  Cd Length: 720  Bit Score: 74.16  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603   3 KEKFERTKPHVNVGTIGHVDHGKTTLT---AAITTVLAKTYGGAARAFDqIDNapEEKARGITINTSHV----EYDTPTR 75
Cdd:TIGR00490  10 KELMWKPKFIRNIGIVAHIDHGKTTLSdnlLAGAGMISEELAGQQLYLD-FDE--QEQERGITINAANVsmvhEYEGNEY 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1383508603  76 HYAHVDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTrEHILlgRQVGVPYI--IVFLNKCD 139
Cdd:TIGR00490  87 LINLIDTPGHVDFGGDVTRAMRAVDGAIVVVCAVEGVMPQT-ETVL--RQALKENVkpVLFINKVD 149
Translation_Factor_II_like cd01342
Domain II of Elongation factor Tu (EF-Tu)-like proteins; Elongation factor Tu consists of ...
211-294 1.09e-13

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: 65.75  E-value: 1.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 211 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETQKstCTGVEMFRKLLDEGRAGENVGVLLRGIKreEIERG 290
Cdd:cd01342     1 LVMQVFKVFYIPGRGRVAGGRVESGTLKVGDEIRILPKGITGR--VTSIERFHEEVDEAKAGDIVGIGILGVK--DILTG 76

                  ....
gi 1383508603 291 QVLA 294
Cdd:cd01342    77 DTLT 80
PTZ00416 PTZ00416
elongation factor 2; Provisional
14-139 7.41e-13

elongation factor 2; Provisional


Pssm-ID: 240409 [Multi-domain]  Cd Length: 836  Bit Score: 70.08  E-value: 7.41e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAITT---VLAKTYGGAARAfdqIDNAPEEKARGITINTS----HVEYDTPTRHYAH------V 80
Cdd:PTZ00416   21 NMSVIAHVDHGKSTLTDSLVCkagIISSKNAGDARF---TDTRADEQERGITIKSTgislYYEHDLEDGDDKQpflinlI 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1383508603  81 DCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlgRQVGVPYI--IVFLNKCD 139
Cdd:PTZ00416   98 DSPGHVDF-SSEVTAALRVtDGALVVVDCVEGVCVQT-ETVL--RQALQERIrpVLFINKVD 155
cysN PRK05124
sulfate adenylyltransferase subunit 1; Provisional
17-298 1.16e-12

sulfate adenylyltransferase subunit 1; Provisional


Pssm-ID: 235349 [Multi-domain]  Cd Length: 474  Bit Score: 68.79  E-value: 1.16e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  17 TIGHVDHGKTTL-------TAAI----TTVLAKTYGGAARAFDQIDNA------PEEKARGITINTSHVEYDTPTRHYAH 79
Cdd:PRK05124   32 TCGSVDDGKSTLigrllhdTKQIyedqLASLHNDSKRHGTQGEKLDLAllvdglQAEREQGITIDVAYRYFSTEKRKFII 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  80 VDCPGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVFLNKCD-MVDDEELLELVEMEVRELL 158
Cdd:PRK05124  112 ADTPGHEQYTRNMATGASTCDLAILLIDARKGVLDQTRRHSFIATLLGIKHLVVAVNKMDlVDYSEEVFERIREDYLTFA 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 159 SQydFPGDdtPIVRGSALKALEGD--AEWEAKI-----IELAGFLDSyIPEPERAIDKPFLLPIEDVF--SISGRGtvVT 229
Cdd:PRK05124  192 EQ--LPGN--LDIRFVPLSALEGDnvVSQSESMpwysgPTLLEVLET-VDIQRVVDAQPFRFPVQYVNrpNLDFRG--YA 264
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1383508603 230 GRVERGIIKVGEEVEIV--GIKETQKSTCTgvemFRKLLDEGRAGENVGVLLrgiKRE-EIERGQVLAKPGT 298
Cdd:PRK05124  265 GTLASGVVKVGDRVKVLpsGKESNVARIVT----FDGDLEEAFAGEAITLVL---EDEiDISRGDLLVAADE 329
Translation_factor_III cd01513
Domain III of Elongation factor (EF) Tu (EF-TU) and related proteins; Elongation factor (EF) ...
300-385 1.18e-12

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: 63.57  E-value: 1.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 300 KPHTKFESEVYILSKDEggrhtPFFKGYRPQFYFRTTDVTGTIELPEGVE-----------MVMPGDNIKMVVTLIHPIA 368
Cdd:cd01513     1 QAVWKFDAKVIVLEHPK-----PIRPGYKPVMDVGTAHVPGRIAKLLSKEdgktkekkppdSLQPGENGTVEVELQKPVV 75
                          90       100
                  ....*....|....*....|...
gi 1383508603 369 MDDG------LRFAIREGGRTVG 385
Cdd:cd01513    76 LERGkefptlGRFALRDGGRTVG 98
EF-G cd01886
Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling ...
14-139 1.20e-10

Elongation factor G (EF-G) family involved in both the elongation and ribosome recycling phases of protein synthesis; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains both eukaryotic and bacterial members.


Pssm-ID: 206673 [Multi-domain]  Cd Length: 270  Bit Score: 61.35  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAI------TTVLAKTYGGAArafdQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHAD 87
Cdd:cd01886     1 NIGIIAHIDAGKTTTTERIlyytgrIHKIGEVHGGGA----TMDWMEQERERGITIQSAATTCFWKDHRINIIDTPGHVD 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1383508603  88 YVKNMITGAAQMDGAILVVAATDGPMPQTrehILLGRQV---GVPYIIvFLNKCD 139
Cdd:cd01886    77 FTIEVERSLRVLDGAVAVFDAVAGVQPQT---ETVWRQAdryGVPRIA-FVNKMD 127
Snu114p cd04167
Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several ...
14-139 1.98e-10

Snu114p, a spliceosome protein, is a GTPase; Snu114p subfamily. Snu114p is one of several proteins that make up the U5 small nuclear ribonucleoprotein (snRNP) particle. U5 is a component of the spliceosome, which catalyzes the splicing of pre-mRNA to remove introns. Snu114p is homologous to EF-2, but typically contains an additional N-terminal domain not found in Ef-2. This protein is part of the GTP translation factor family and the Ras superfamily, characterized by five G-box motifs.


Pssm-ID: 206730 [Multi-domain]  Cd Length: 213  Bit Score: 59.97  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLtaaITTVLAKTY--GGAARAFDQI----DNAPEEKARGITINTSHVEYDTP-TRHYAHV----DC 82
Cdd:cd04167     2 NVCIAGHLHHGKTSL---LDMLIEQTHkrTPSVKLGWKPlrytDTRKDEQERGISIKSNPISLVLEdSKGKSYLiniiDT 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1383508603  83 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCD 139
Cdd:cd04167    79 PGHVNFMDEVAAALRLCDGVVLVVDVVEGLTSVTERLIRHAIQEGLPMVLV-INKID 134
LepA cd01890
LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) ...
14-140 2.26e-10

LepA also known as Elongation Factor 4 (EF4); LepA (also known as elongation factor 4, EF4) belongs to the GTPase family and exhibits significant homology to the translation factors EF-G and EF-Tu, indicating its possible involvement in translation and association with the ribosome. LepA is ubiquitous in bacteria and eukaryota (e.g. yeast GUF1p), but is missing from archaea. This pattern of phyletic distribution suggests that LepA evolved through a duplication of the EF-G gene in bacteria, followed by early transfer into the eukaryotic lineage, most likely from the promitochondrial endosymbiont. Yeast GUF1p is not essential and mutant cells did not reveal any marked phenotype.


Pssm-ID: 206677 [Multi-domain]  Cd Length: 179  Bit Score: 59.08  E-value: 2.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAIttvLAKTYGGAARAF-DQI-DNAPEEKARGITINTSHV----EYDTPTRHYAH-VDCPGHA 86
Cdd:cd01890     2 NFSIIAHIDHGKSTLADRL---LELTGTVSEREMkEQVlDSMDLERERGITIKAQAVrlfyKAKDGEEYLLNlIDTPGHV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1383508603  87 DYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDM 140
Cdd:cd01890    79 DFSYEVSRSLAACEGALLVVDATQGVEAQTLANFYLALENNLE-IIPVINKIDL 131
GTPBP_II cd03694
Domain II of the GTPBP family of GTP binding proteins; This group includes proteins similar to ...
211-294 4.51e-10

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: 55.69  E-value: 4.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 211 FLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEI----------VGIKetqkstctGVEMFRKLLDEGRAGENVGVLLR 280
Cdd:cd03694     1 FEFQIDDIYSVPGVGTVVSGTVSKGVIREGDTLLLgpdadgkfrpVTVK--------SIHRNRQPVDRARAGQSASFALK 72
                          90
                  ....*....|....
gi 1383508603 281 GIKREEIERGQVLA 294
Cdd:cd03694    73 KIKRESLRKGMVLV 86
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
13-139 9.49e-10

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 57.00  E-value: 9.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  13 VNVGTIGHVDHGKTTLtaaiTTVLAKTYGgaarafdqidnAPEEKARGIT--INTSHVEYDTPTRHYAHVDCPGHADYVK 90
Cdd:TIGR00231   2 IKIVIVGHPNVGKSTL----LNSLLGNKG-----------SITEYYPGTTrnYVTTVIEEDGKTYKFNLLDTAGQEDYDA 66
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1383508603  91 ------NMITGAAQM-DGAILVVAATDGPMPQTREHILLgRQVGVPyIIVFLNKCD 139
Cdd:TIGR00231  67 irrlyyPQVERSLRVfDIVILVLDVEEILEKQTKEIIHH-ADSGVP-IILVGNKID 120
eRF3_II_like cd03698
Domain II of the eukaryotic class II release factor-like proteins; This model represents the ...
210-294 1.76e-09

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: 54.04  E-value: 1.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 210 PFLLPIEDVFSiSGRGTVVTGRVERGIIKVGEEVEIVGIKETQKSTCTGVEMFRKlLDEGRAGENVGVLLRGIKREEIER 289
Cdd:cd03698     1 PFRLSIDDKYK-SPRGTTVTGKLEAGSIQKNQVLYDMPSQQDAEVKNIIRNSDEE-TDWAIAGDTVTLRLRGIEVEDIQP 78

                  ....*
gi 1383508603 290 GQVLA 294
Cdd:cd03698    79 GDILS 83
eRF3_II cd04089
Domain II of the eukaryotic class II release factor; In eukaryotes, translation termination is ...
210-293 4.09e-09

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: 52.87  E-value: 4.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 210 PFLLPIEDVFSisGRGTVVTGRVERGIIKVGE---------EVEIVGIketqksTCTGVEMfrkllDEGRAGENVGVLLR 280
Cdd:cd04089     1 PLRMPILDKYK--DMGTVVMGKVESGTIRKGQklvlmpnktKVEVTGI------YIDEEEV-----DSAKPGENVKLKLK 67
                          90
                  ....*....|...
gi 1383508603 281 GIKREEIERGQVL 293
Cdd:cd04089    68 GVEEEDISPGFVL 80
RF3 cd04169
Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; ...
18-140 5.91e-09

Release Factor 3 (RF3) protein involved in the terminal step of translocation in bacteria; Peptide chain release factor 3 (RF3) is a protein involved in the termination step of translation in bacteria. Termination occurs when class I release factors (RF1 or RF2) recognize the stop codon at the A-site of the ribosome and activate the release of the nascent polypeptide. The class II release factor RF3 then initiates the release of the class I RF from the ribosome. RF3 binds to the RF/ribosome complex in the inactive (GDP-bound) state. GDP/GTP exchange occurs, followed by the release of the class I RF. Subsequent hydrolysis of GTP to GDP triggers the release of RF3 from the ribosome. RF3 also enhances the efficiency of class I RFs at less preferred stop codons and at stop codons in weak contexts.


Pssm-ID: 206732 [Multi-domain]  Cd Length: 268  Bit Score: 56.45  E-value: 5.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  18 IGHVDHGKTTLT-------AAIT---TVLAKTYGGAARAfdqiDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHAD 87
Cdd:cd04169     8 ISHPDAGKTTLTeklllfgGAIQeagAVKARKSRKHATS----DWMEIEKQRGISVTSSVMQFEYKGCVINLLDTPGHED 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1383508603  88 YVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCDM 140
Cdd:cd04169    84 FSEDTYRTLTAVDSAVMVIDAAKGVEPQTRKLFEVCRLRGIP-IITFINKLDR 135
HBS1-like_II cd16267
Domain II of Hbs1-like proteins; S. cerevisiae Hbs1 is closely related to the eukaryotic class ...
210-293 1.92e-08

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


Pssm-ID: 293912 [Multi-domain]  Cd Length: 84  Bit Score: 50.97  E-value: 1.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 210 PFLLPIEDVFSISGRGTVVTGRVERGIIKVGEEVEIVGIKETqkSTCTGVEMFRKLLDEGRAGENVGVLLRGIKREEIER 289
Cdd:cd16267     1 PFRLSVSDVFKGQGSGFTVSGRIEAGSVQVGDKVLVMPSNET--ATVKSIEIDDEPVDWAVAGDNVTLTLTGIDPNHLRV 78

                  ....
gi 1383508603 290 GQVL 293
Cdd:cd16267    79 GSIL 82
PLN00116 PLN00116
translation elongation factor EF-2 subunit; Provisional
14-125 4.95e-08

translation elongation factor EF-2 subunit; Provisional


Pssm-ID: 177730 [Multi-domain]  Cd Length: 843  Bit Score: 55.12  E-value: 4.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLT---AAITTVLAKTYGGAARAfdqIDNAPEEKARGITINTSHV----EY-DTPTRHYAH------ 79
Cdd:PLN00116   21 NMSVIAHVDHGKSTLTdslVAAAGIIAQEVAGDVRM---TDTRADEAERGITIKSTGIslyyEMtDESLKDFKGerdgne 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1383508603  80 -----VDCPGHADYvKNMITGAAQM-DGAILVVAATDGPMPQTrEHILlgRQ 125
Cdd:PLN00116   98 ylinlIDSPGHVDF-SSEVTAALRItDGALVVVDCIEGVCVQT-ETVL--RQ 145
PRK04004 PRK04004
translation initiation factor IF-2; Validated
19-139 1.38e-07

translation initiation factor IF-2; Validated


Pssm-ID: 235195 [Multi-domain]  Cd Length: 586  Bit Score: 53.26  E-value: 1.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  19 GHVDHGKTTLTAAI--TTVLAKTYGG-----AARA--FDQIdnapeEKARGITINTSHVEYDTPTRHYahVDCPGHADYV 89
Cdd:PRK04004   13 GHVDHGKTTLLDKIrgTAVAAKEAGGitqhiGATEvpIDVI-----EKIAGPLKKPLPIKLKIPGLLF--IDTPGHEAFT 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1383508603  90 KNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCD 139
Cdd:PRK04004   86 NLRKRGGALADIAILVVDINEGFQPQTIEAINILKRRKTPFVVA-ANKID 134
aIF-2 TIGR00491
translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic ...
15-139 2.76e-07

translation initiation factor aIF-2/yIF-2; This model describes archaeal and eukaryotic orthologs of bacterial IF-2. Like IF-2, it helps convey the initiator tRNA to the ribosome, although the initiator is N-formyl-Met in bacteria and Met here. This protein is not closely related to the subunits of eIF-2 of eukaryotes, which is also involved in the initiation of translation. The aIF-2 of Methanococcus jannaschii contains a large intein interrupting a region of very strongly conserved sequence very near the amino end; the alignment generated by this model does not correctly align the sequences from Methanococcus jannaschii and Pyrococcus horikoshii in this region. [Protein synthesis, Translation factors]


Pssm-ID: 273104 [Multi-domain]  Cd Length: 591  Bit Score: 52.51  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  15 VGTIGHVDHGKTTLTAAI--TTVLAKTYGGAARAF--DQIDNAPEEKARGITINTSHVEYDTPTRHYahVDCPGHADYVK 90
Cdd:TIGR00491   7 VVVLGHVDHGKTTLLDKIrgTAVVKKEAGGITQHIgaSEVPTDVIEKICGDLLKSFKIKLKIPGLLF--IDTPGHEAFTN 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1383508603  91 NMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYiIVFLNKCD 139
Cdd:TIGR00491  85 LRKRGGALADIAILVVDINEGFKPQTLEALNILRSRKTPF-VVAANKID 132
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
18-191 1.26e-06

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


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 47.84  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  18 IGHVDHGKTTLTAAITTvlaktyggaarafDQIDNAPEEKARGITINTSHVEYDTPTRHYAHVDCPGHADYVKNMITGAA 97
Cdd:cd00882     3 VGRGGVGKSSLLNALLG-------------GEVGEVSDVPGTTRDPDVYVKELDKGKVKLVLVDTPGLDEFGGLGREELA 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  98 QM-----DGAILVVAATDGPMPQ--TREHILLGRQVGVPyIIVFLNKCDMVDDEELLELVEMEVRELLSqydfpgdDTPI 170
Cdd:cd00882    70 RLllrgaDLILLVVDSTDRESEEdaKLLILRRLRKEGIP-IILVGNKIDLLEEREVEELLRLEELAKIL-------GVPV 141
                         170       180
                  ....*....|....*....|.
gi 1383508603 171 VRGSALKaLEGDAEWEAKIIE 191
Cdd:cd00882   142 FEVSAKT-GEGVDELFEKLIE 161
Translation_Factor_II cd16265
Proteins related to domain II of EF-Tu and related translation factors; Elongation factor Tu ...
215-294 1.38e-06

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


Pssm-ID: 293910 [Multi-domain]  Cd Length: 80  Bit Score: 45.75  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 215 IEDVFSISGRgTVVTGRVERGIIKVGEEVeivgIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLRGikREEIERGQVLA 294
Cdd:cd16265     5 VEKVFKILGR-QVLTGEVESGVIYVGYKV----KGDKGVALIRAIEREHRKVDFAVAGDEVALILEG--KIKVKEGDVLE 77
CysN_NodQ_II cd03695
Domain II of the large subunit of ATP sulfurylase; This subfamily represents domain II of the ...
211-295 5.74e-06

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: 44.09  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603 211 FLLPIEDV--FSISGRGtvVTGRVERGIIKVGEEVEIvgIKETQKSTCTGVEMFRKLLDEGRAGENVGVLLrgiKRE-EI 287
Cdd:cd03695     1 FRFPVQYVnrPNLDFRG--YAGTIASGSIRVGDEVTV--LPSGKTSRVKSIVTFDGELDSAGAGEAVTLTL---EDEiDV 73

                  ....*...
gi 1383508603 288 ERGQVLAK 295
Cdd:cd03695    74 SRGDLIVR 81
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
14-137 9.83e-04

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 38.37  E-value: 9.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAITTVLAKTyggaarafdqiDNAPeekarGITINTSHVEYDTPTRHYAHVDCPG--HADYVKN 91
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALTGAKAIV-----------SDYP-----GTTRDPNEGRLELKGKQIILVDTPGliEGASEGE 64
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1383508603  92 MITGA----AQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNK 137
Cdd:pfam01926  65 GLGRAflaiIEADLILFVVDSEEGITPLDEELLELLRENKKPIILV-LNK 113
prfC PRK00741
peptide chain release factor 3; Provisional
18-139 9.98e-04

peptide chain release factor 3; Provisional


Pssm-ID: 179105 [Multi-domain]  Cd Length: 526  Bit Score: 41.27  E-value: 9.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  18 IGHVDHGKTTLT-------AAIT---TVLAKtygGAARaFDQIDNAPEEKARGITINTSHVEYDtptrhYAH-----VDC 82
Cdd:PRK00741   16 ISHPDAGKTTLTeklllfgGAIQeagTVKGR---KSGR-HATSDWMEMEKQRGISVTSSVMQFP-----YRDclinlLDT 86
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1383508603  83 PGHADYVKNMITGAAQMDGAILVVAATDGPMPQTREHILLGRQVGVPyIIVFLNKCD 139
Cdd:PRK00741   87 PGHEDFSEDTYRTLTAVDSALMVIDAAKGVEPQTRKLMEVCRLRDTP-IFTFINKLD 142
GTPBP1_like cd04165
GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 ...
14-140 1.98e-03

GTP binding protein 1 (GTPBP1)-like family includes GTPBP2; Mammalian GTP binding protein 1 (GTPBP1), GTPBP2, and nematode homologs AGP-1 and CGP-1 are GTPases whose specific functions remain unknown. In mouse, GTPBP1 is expressed in macrophages, in smooth muscle cells of various tissues and in some neurons of the cerebral cortex; GTPBP2 tissue distribution appears to overlap that of GTPBP1. In human leukemia and macrophage cell lines, expression of both GTPBP1 and GTPBP2 is enhanced by interferon-gamma (IFN-gamma). The chromosomal location of both genes has been identified in humans, with GTPBP1 located in chromosome 22q12-13.1 and GTPBP2 located in chromosome 6p21-12. Human glioblastoma multiforme (GBM), a highly-malignant astrocytic glioma and the most common cancer in the central nervous system, has been linked to chromosomal deletions and a translocation on chromosome 6. The GBM translocation results in a fusion of GTPBP2 and PTPRZ1, a protein involved in oligodendrocyte differentiation, recovery, and survival. This fusion product may contribute to the onset of GBM.


Pssm-ID: 206728 [Multi-domain]  Cd Length: 224  Bit Score: 39.20  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  14 NVGTIGHVDHGKTTLTAAITTVLAKTYGGAARA-----------------------FDQ-------IDNAPEEKARGITI 63
Cdd:cd04165     1 RVAVVGNVDAGKSTLLGVLTQGELDNGRGKARLnlfrhkhevesgrtssvsndilgFDSdgevvnyPDNHLGELDVEICE 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1383508603  64 NTSHVEYdtptrhyaHVDCPGHADYVKNMITG--AAQMDGAILVVAATDGPMPQTREHILLGRQVGVPYIIVfLNKCDM 140
Cdd:cd04165    81 KSSKVVT--------FIDLAGHERYLKTTVFGmtGYAPDYAMLVVGANAGIIGMTKEHLGLALALKVPVFVV-VTKIDM 150
Era_like cd00880
E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family ...
96-193 2.41e-03

E. coli Ras-like protein (Era)-like GTPase; The Era (E. coli Ras-like protein)-like family includes several distinct subfamilies (TrmE/ThdF, FeoB, YihA (EngB), Era, and EngA/YfgK) that generally show sequence conservation in the region between the Walker A and B motifs (G1 and G3 box motifs), to the exclusion of other GTPases. TrmE is ubiquitous in bacteria and is a widespread mitochondrial protein in eukaryotes, but is absent from archaea. The yeast member of TrmE family, MSS1, is involved in mitochondrial translation; bacterial members are often present in translation-related operons. FeoB represents an unusual adaptation of GTPases for high-affinity iron (II) transport. YihA (EngB) family of GTPases is typified by the E. coli YihA, which is an essential protein involved in cell division control. Era is characterized by a distinct derivative of the KH domain (the pseudo-KH domain) which is located C-terminal to the GTPase domain. EngA and its orthologs are composed of two GTPase domains and, since the sequences of the two domains are more similar to each other than to other GTPases, it is likely that an ancient gene duplication, rather than a fusion of evolutionarily distinct GTPases, gave rise to this family.


Pssm-ID: 206646 [Multi-domain]  Cd Length: 161  Bit Score: 38.38  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1383508603  96 AAQMDGAILVVAATDGPMPQTREHILLgRQVGVPYIIVFlNKCDMVDDEELLELVEMEVRELLSQYdfpgddtPIVRGSA 175
Cdd:cd00880    74 ADRADLVLLVVDSDLTPVEEEAKLGLL-RERGKPVLLVL-NKIDLVPESEEEELLRERKLELLPDL-------PVIAVSA 144
                          90
                  ....*....|....*...
gi 1383508603 176 LKaLEGDAEWEAKIIELA 193
Cdd:cd00880   145 LP-GEGIDELRKKIAELL 161
 
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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